No retraction, correction or concern found when last checked on Oct 17, 2026.

RNA modifications: importance in immune cell biology and related diseases

Lian Cui, Rui Ma, Jiangluyi Cai and 7 more

Signal Transduction and Targeted Therapy · 2022 · Review · CC BY

Abstract

RNA modifications have become hot topics recently. By influencing RNA processes, including generation, transportation, function, and metabolization, they act as critical regulators of cell biology. The immune cell abnormality in human diseases is also a research focus and progressing rapidly these years. Studies have demonstrated that RNA modifications participate in the multiple biological processes of immune cells, including development, differentiation, activation, migration, and polarization, thereby modulating the immune responses and are involved in some immune related diseases. In this review, we present existing knowledge of the biological functions and underlying mechanisms of RNA modifications, including N 6 -methyladenosine (m 6 A), 5-methylcytosine (m 5 C), N 1 -methyladenosine (m 1 A), N 7 -methylguanosine (m 7 G), N 4 -acetylcytosine (ac 4 C), pseudouridine (Ψ), uridylation, and adenosine-to-inosine (A-to-I) RNA editing, and summarize their critical roles in immune cell biology. Via regulating the biological processes of immune cells, RNA modifications can participate in the pathogenesis of immune related diseases, such as cancers, infection, inflammatory and autoimmune diseases. We further highlight the challenges and future directions based on the existing knowledge. All in all, this review will provide helpful knowledge as well as novel ideas for the researchers in this area.

Full text

From PubMed Central, U.S. National Library of Medicine, as current on Oct 17, 2026. Paragraph numbers are ours, so an answer can point at one.

Introduction

1Chemical modification occurs on many types of biological macromolecules, such as nucleic acids, sugars, lipids, and proteins, and is specific and efficient for regulating their functions.– RNA modifications, such as N6-methyladenosine (m6A), 5-methylcytosine (m5C), N1-methyladenosine (m1A), N7-methylguanosine (m7G), N4-acetylcytosine (ac4C), pseudouridine (Ψ), uridylation, and adenosine-to-inosine (A-to-I) RNA editing, are RNA features that alter the canonical AUGC bases and function as emerging and critical post-transcriptional regulators.–, The RNA modifications catalyzed by “writer” enzymes can be removed by “eraser” enzymes., However, some modifications are further modified by enzymes, which we term for the first time as “modifiers”. The modifications are identified by RNA-binding proteins (RBP) known as “readers” to participate in various physiological and pathological processes.–,,

2The immune cell abnormality in human diseases is also a research focus and progressing rapidly these years. In 2005, a study demonstrated that RNA modifications, such as m6A, m5C, m5U, s2U, or Ψ, may influence the activations of dendritic cells (DCs) and toll-like receptor (TLR)-expressing cells. Although this research was a preliminary exploration, it gave us knowledge that RNA modification could affect the biology of immune cells. In recent years, advances in new technologies and ideas have led to an increasing number of researchers focusing on the influence of RNA modifications on immune cell biology, and their roles in immune related diseases. m6A is the modification most frequently studied and there already have some reviews summarized its important roles in immune processes., Although not thoroughly and comprehensively, other RNA modifications have also been confirmed to participate in the immune cell biology and immune related diseases. However, due to the complexity of RNA modification and the diversity of immune cells, the interaction network between RNA modification and immune cells remains largely unclear, which needs to be further consummated. Hence, based on the research status, we write this review, which we hope to be helpful for researchers and promote progress in this area.

3In this review, we clarify the current understanding of eight RNA modifications and focus on their critical roles in regulating immune cell biology and immune related diseases. We also highlight questions that remain to be addressed in this area and provide perspectives for further studies.

N6-methyladenosine

4The methylation of adenosine at position N6, m6A modification has emerged as the most prevalent and abundant mRNA modification in eukaryotes (m6A/A = 0.1–0.6%)., It appears in the full-length sequence but is enriched in the vicinity of the stop codon and the 3ʹ untranslated region (3ʹUTR) of mRNAs, within the consensus motif RRACH (R = G or A; H = A, C, or U)., It also occurs in most non-coding RNAs, including ribosomal RNAs (rRNAs), small nuclear RNAs (snRNAs), small nucleolar RNAs (snoRNAs), microRNAs (miRNAs), long non-coding RNAs (lncRNAs), and circular RNAs (circRNAs) (Fig. 1).–

5m6A deposition in mRNA is mostly mediated by the m6A methyltransferase complex (MTC) (Fig. 2 and Table 1).– The key MTC components are methyltransferase-like 3 (METTL3), METTL14, Wilms’ tumor 1-associating protein (WTAP), vir-like m6A methyltransferase-associated (VIRMA, also known as KIAA1429), Cbl proto-oncogene-like 1 (HAKAI), zinc finger CCCH-type containing 13 (ZC3H13), and RNA-binding motif protein 15/15B (RBM15/15B).,, Among them, METTL3 is considered the only putative S-adenosylmethionine (SAM)-dependent methyltransferase with its own catalytic ability and can form a tight heterodimer with METTL14 to perform catalysis.– The other aforementioned writers act as regulatory factors., Zinc finger CCCH-type containing 4 (ZCCHC4) and METTL5 mediate m6A formation on 28S and 18S rRNA, respectively, to accelerate the global translation rate (Fig. 3 and Table 1).– In U6 snRNA, m6A is executed by METTL16 to participate in RNA splicing regulation (Fig. 4 and Table 1).–

6To date, two m6A erasers have been identified, both belonging to the AlkB family of the Fe (II)/α-ketoglutarate-dependent dioxygenase superfamily.– The first eraser is fat mass and obesity-associated protein (FTO) that mediates mRNA and snRNA demethylation in m6A and m6Am residues, and tRNA in m1A residue (Figs. 2, 4, 5 and Table 1).,, The other m6A eraser, AlkB homolog 5 (ALKBH5), only oxidatively reverses m6A in mRNA (Fig. 2 and Table 1).,

7Many reader proteins influence the fate of m6A RNAs in various ways, which is largely determined by their subcellular localization. The most studied readers are the YT521-B homology (YTH) domain family members, which share the m6A-recognizing YTH domain but exert different effects on RNA fate., The YTH domain family includes YTHDF1–3 and YTHDC1–2., YTHDF1 and YTHDF3 actively promote protein synthesis by interacting with translation machinery, whereas YTHDF2 recruits RNA-degrading enzymes or adaptor proteins to trigger the rapid degradation of its target mRNA.– YTHDC1 not only facilitates the decay of m6A-modified chromosome-associated regulatory RNAs to influence the open chromatin state and downstream transcription but also mediates mRNA splicing by recruiting and regulating pre-mRNA splicing factors.– YTHDC2 may participate in mRNA stability and translation in an m6A-dependent or -independent manner.– Insulin-like growth factor 2 mRNA-binding proteins (IGF2BPs, which include IGF2BP1–3), identify m6A through K homology domains to enhance mRNA stability and translation., The heterogeneous nuclear ribonucleoprotein (HNRNP) family members, which include HNRNPC, HNRNPG, and HNRNPA2B1, can identify m6A on precursor (pre)-mRNAs and/or primary (pri)-miRNAs to mediate splicing and/or nucleocytoplasmic trafficking.– Eukaryotic initiation factor 3 (eIF3) promotes cap-independent translation upon the induction of cellular stress by recruiting the 43S complex to initiate translation., Both proline rich coiled-coil 2A (PRRC2A) Staphylococcal nuclease and tudor domain-containing 1 (SND1) function as m6A readers, facilitating the stabilization of modified RNA., In particular, m6A participates in transcription termination by promoting co-transcriptional R-loop formation to prevent the readthrough activity of Pol II, while it is unclear whether other readers are involved in this process. The specific roles of m6A in various RNA molecules are presented in Figs. 2 to 4 and Table 1.

8Collectively, m6A modification plays a regulatory role in various cellular processes by affecting transcription, maturation, localization, function, and metabolism in different RNA classes.,,, (Table 1) In mRNAs, m6A can affect transcription, maturation, localization, translation and degradation, eventually influencing the proteins encoded (Fig. 2)., In rRNAs, the m6A1832 modification in 18s rRNA as well as the m6A4220 modification in 28S rRNA are required for global translation (Fig. 3)., In snRNAs and snoRNAs, m6A modification may regulate snRNA pre-mRNA or pre-lncRNA splicing processes (Fig. 4)., In miRNAs, m6A facilitates pri-miRNA processing by recruiting the miRNA microprocessor complex protein DGCR8 depending on HNRNPA2B1 (Fig. 4).,, In lncRNAs and circRNAs, m6A has been verified to modulate generation, structure, distribution, function and metabolism (Fig. 1), and m6A is also a critical translation initiator in circRNAs with coding potential.,

9Although m6A has been widely investigated, there are still some important questions remain to be solved. For example, m6A is a widespread modification that can affect a variety kind of RNA, existing studies mainly focus on the effect of m6A on mRNA, and its effect on non-coding RNA may be of good research interest. The current study shows that the effect of m6A on RNA stability is bidirectional, i.e., increasing stability or promoting degradation. For this issue, it is necessary to fully consider the modification sites of m6A in RNAs as well as the imbalance of different readers, such as YTHDF2 and IGF2BPs. m6A may affect circRNA generation and circRNA-mRNA imbalance by mediating pre-mRNA splicing, which is also a potential study focus due to the recent research upsurge on circRNAs. Although existing inhibitors can interfere m6A levels by inhibiting writers,,, they are often nonspecific and affects overall m6A levels. It is more significant to explore gene specific m6A interference.

5-methylcytosine

10m5C methylation occurs at position 5 of the cytidine residues of both DNA and RNA. Identified in 1958, m5C is described as a widespread mark in the epitranscriptome on tRNA, rRNA, mRNA, enhancer RNA (eRNA), and miRNA and is most abundant in eukaryotic tRNAs and rRNAs (Fig. 1).–

11In eukaryotes, m5C methylation is introduced by the NOL1/NOP2/SUN domain (NSUN) family members, NSUN1–7, and DNA methyltransferase-like 2 (DNMT2) as presented in Table 1.,, Specific m5C writers catalyze different RNA subsets. According to current knowledge, cytoplasmic tRNAs are methylated by NSUN2, NSUN6, and DNMT2, while mitochondrial tRNAs are catalyzed by NSUN2 and NSUN3 (Fig. 5 and Table 1).– rRNAs are methylated by NSUN1 and NSUN5 in the nucleus and by NSUN4 in the mitochondria (Fig. 3 and Table 1).– mRNAs are methylated by NSUN2 and NSUN6, whereas ncRNA and eRNAs can be modified by NSUN2 and NSUN7, respectively (Fig. 2 and Table 1).,,,,

12Recently, some m5C erasers or modifiers have been concerned in RNA molecules. The known erasers/modifiers include ten-eleven translocation (TET) proteins (TET1–3) and α-ketoglutarate-dependent dioxygenase ABH1 (ALKBH1), which possess the activity of oxidizing m5C to 5-hydroxymethylcytidine (hm5C) (Fig. 5 and Table 1).– In DNA, TETs successively convert m5C to hm5C, 5-formylcytosine (f5C), and 5-carboxylcytosine, the latter two of which are identified and removed by thymine DNA glycosylase;– whereas in RNA, TETs has been only reported to convert m5C to hm5C (Fig. 5).– ALKBH1 can successively convert m5C into hm5C and f5C at position 34 of cytoplasmic and mitochondrial tRNA, and the process in mitochondria is required for mitochondrial functions (Fig. 5)., Under all circumstances, hm5C formation from m5C reduces the m5C modification, which is why previous studies considered TETs and ALKBH1 erasers.

13Like m6A modification, m5C also involves binding proteins to change the fate of the modified RNA. The first identified mRNA m5C reader was RNA and export factor-binding protein 2 (ALYREF), a well-known protein complex that facilitates the nuclear export of mRNAs (Fig. 1 and Table 1)., Y-box-binding protein 1 (YBX1) is a reader located in the cytoplasm that enhances the stability of m5C-modified mRNA by recruiting ELAV like RNA binding protein 1 (ELAVL1), an mRNA stability maintainer (Fig. 2 and Table 1)., Besides, YTHDF2, also an m6A reader protein, could directly bind to m5C in RNA to modulate the distribution of m5C in both coding and noncoding RNA and influence rRNA maturation by regulating m5C levels (Table 1). Recently, Lan and colleagues presented a novel m5C reader, fragile X messenger ribonucleoprotein 1 (FMRP), which could be recruited to DNA damage sites by DNMT2 and promote TET1-mediated RNA m5C demethylation in DNA:RNA hybrids (Table 1).

14Generally, m5C plays a critical role in stabilizing both non-coding and coding RNAs. In tRNAs, m5C regulates RNA structure and stability and is required for translation accuracy (Fig. 5 and Table 1).,, m5C methylation at C2278 within a conserved region of 25S rRNA stabilizes the structural conformation of the ribosome, ensures translation fidelity, and recruits oxidative stress-responsive mRNA subsets to polysomes (Fig. 3 and Table 1). m5C methylation on vault RNAs affects their processing into derived small RNAs, while m5C in eRNAs protects them from degradation (Table 1). In mRNAs, m5C is vital for modulating stability, nuclear export, and translation (Table 1).,,– For example, a subset of mRNAs with hypermethylated m5C sites was stabilized in an NSUN2- or YBX1-dependent manner, which influenced bladder carcinogenesis or embryonic development in zebrafish. NSUN2 enhanced the recognition of cyclin-dependent kinase inhibitor 1A (CDKN1A) mRNA by ALYREF, which functionally promoted the nuclear export capacity and translation of CDKN1A mRNA in 3T3-L1 preadipocytes.

15As we described above, m5C is abundant and required for maintaining RNA structure and stability in eukaryotic tRNAs and rRNAs, which are vital molecules in maintaining the normal physiology of almost all types of eukaryotic cells. Thus, targeting m5C as a therapeutic approach may have a long way to go. Fortunately, different RNAs possess different writers, and targeting specific writers can affect the function of specific RNAs. For instance, a recent study revealed that targeting NSUN3 to regulate site-specific mitochondrial RNA m5C modification shows therapeutic effects in combating cancer metastasis.

N1-methyladenosine

16Identified in the 1960s, m1A was reported as the methylation of adenosine at position N1 and has been observed in tRNAs, rRNAs, mRNAs, and lncRNAs., m1A is inextricably linked with m6A modification, as not only does m1A rearrange to m6A under alkaline conditions (Dimroth rearrangement), they also share some regulators (Fig. 1).,

17The current reported human m1A writers include nucleomethylin (NML, also known as RRP8) (for rRNA), the tRNA methyltransferase 6 non-catalytic subunit (TRMT6)–RNA methyltransferase 61A (TRMT61A) complex (for mRNA and mitochondrial tRNA), TRMT61B (for mitochondrial tRNA and rRNA), TRMT10B (for tRNA), and TRMT10C (for mitochondrial tRNA and mRNA).– m1A erasers, including FTO (for tRNA) and the ALKBH family members ALKBH1 (for mitochondrial tRNA), ALKBH3 (for tRNA and mRNA), and ALKBH7 (for mitochondrial tRNA), overlap or are closely related to some m6A erasers. Accordingly, it has been verified that some m6A readers, i.e., YTH domain family proteins including YTHDF1–3 and YTHDC1, identify m1A modifications (Figs. 2, 3, 5 and Table 1).,,–

18Generally, m1A affects RNA base pairing and subsequently influences the target RNA molecule structure and function.,, Human rRNAs and tRNAs contain many different m1A modification sites. For example, m1A at position 1322 of 28S rRNA promotes 60S ribosomal subunit formation and m1A at position 947 is essential for mitoribosomal structure and function., m1A at position 58 of tRNA is essential for tRNA structure, stability, and translational initiation; in this position, absent m1A may promote the generation of tRNA-derived small RNAs (tDRs), enhancing ribosome assembly and causing malignant phenotypes., In mRNA, m1A is distributed in every mRNA segment, which includes the coding sequence (CDS), 5′UTR, and 3′UTR, and its roles appear region- or subcellular location-dependent., Near the start codon, m1A might regulate translation initiation by altering the secondary/tertiary structure or reader recognition of translation initiation sites (TISs), thereby promoting translation. In mitochondria, m1A in the 5′UTR or CDS repressed translation, probably by affecting ribosome scanning or translation (Figs. 2, 3, 5 and Table 1).,

19Because m1A shares some regulators, such as YTHDF1–3 and YTHDC1, with m6A modification, the research ideas of m6A can provide reference for m1A. Since m1A modification can affect RNA base pairing, we expect that it might affect the binding of miRNAs with other RNA structures, such as mRNA 3ʹUTR, lncRNA and circRNA. Competing endogenous RNAs (ceRNA) regulatory network is attracting much attention these years, and m1A modification may add novel conceptions to this theory.

N7-methylguanosine

20m7G refers to the RNA methylation of guanine at position N7 and is present in approximately 0.4% of all guanosine, a level similar to that of m1A modification.– m7G is well known for the formation of the 5ʹ cap (m7GPPPN) structure of mature mRNA, snRNA, and snoRNA; moreover, it is enriched in all three transcript segments of mRNA 5ʹUTR, CDS, and 3ʹUTR and in pre-mRNAs.,– m7G is also present in noncoding RNAs, such as position 46 of tRNA, G1575/G1639 of 18S rRNA, and even mature and pre-miRNAs (Fig. 1).–

21RNA guanine-7 methyltransferase (RNMT), METTL1–WD repeat domain 4 (WDR4) complex, and Williams–Beuren syndrome chromosomal region 22 protein (WBSCR22, also known as BUD23) are considered m7G writers. Activated by RNMT-activating mini-protein (RAM), RNMT is required for efficient cap methylation.– By forming a complex with WDR4 or other partners, METTL1 has m7G methyltransferase activity for tRNA, internal mRNA, and pri-miRNA/miRNA.,,, Requiring the methyltransferase adapter protein TRM112, WBSCR22 specifically methylates m7G in 18S rRNA. In most non-coding RNAs, the m7G cap can be lost during maturation by cleavage or further modification to m2,2,7G trimethylguanosine. For example, trimethylguanosine synthase 1 (TGS1) might function as a modifier, which hypermethylated the m7G caps of snRNAs and snoRNAs to a m2,2,7G cap structure, leading to their concentration in nuclear foci. The m7G cap can be recognized by eIF4E and the cap-binding complex (CBC) composed of CBP80 and CBP20, thereby affecting RNA maturation, nuclear export, and translation (Figs. 2 to 5 and Table 1).–

22On mRNA, the m7G cap regulates multiple stages of mRNA processes, including pre-mRNA slicing, nuclear export, transcription elongation, translation, and degradation and indirectly augments ribosome synthesis and translation rates.,, On internal mRNA, m7G methylation might influence mRNA translation. m7G in tRNAs remodels the mRNA translatome by maintaining tRNA structural integrity to promote its stability, translation ability, and reduce ribosome pausing.,,, However, the effects of m7G on rRNA have not been studied in-depth. In miRNA, m7G promoted miRNA processing by antagonizing G-quadruplex structures in pri-miRNA (Figs. 2 to 5 and Table 1).,,

23As we know, m7G is widely present in mRNAs and is a critical regulator in the translation process, therefore, it may not be a good therapic target in human diseases. The roles of m7G regulators may vary in different RNAs and diseases. For example, m7G modification on tRNA promoted the progression of lung cancer, while m7G modification on let-7 miRNA showed the opposite effect. m7G modification promoted the progression of hepatocellular carcinoma and bladder cancer,, while it exerted an opposite opposite effect in teratoma.

N4-acetylcytosine

24Aside from m5C and hm5C, ac4C (acetylation of the N4 position of cytosine) is another conserved modification in cytidine and is currently the only acetylation event described in eukaryotic RNA.– As with many RNA modifications, ac4C was detected initially in tRNA and rRNA, followed by mRNA., In rRNA, ac4C is distributed in helix 34 and helix 45 near the decoding site of mammalian 18S rRNA; in tRNA, it is detected at the D-stem of tRNASer/Leu in eukaryotes.– In mRNA, the deposition of ac4C sites is detected mainly in the CDS region, and also in the 5ʹUTR (Fig. 1).

25N-acetyltransferase 10 (NAT10), an essential ATP-dependent RNA acetyltransferase, is currently considered the only writer of ac4C. It catalyzes ac4C modification in 18S rRNA, tRNA, and a broad range of mRNA.,,, Two additional proteins are required in ac4C formation in human rRNA or tRNA, respectively. The first is the box C/D snoRNA U13, which is essential and specific for 18S rRNA acetylation by timely pre-rRNA folding. The other is THUMP domain-containing 1 (THUMPD1), a specific RNA adaptor protein harboring an RNA-binding motif that can interact with NAT10 to cooperate in tRNA acetylation (Figs. 2, 3, 5 and Table 1).,

26In 18S rRNAs, ac4C is critical for pre-rRNA processing and ribosome synthesis and influences translation ability possibly by turning the 18S rRNA 3′ end into an environment rich in base modifications to interact with mRNA or tRNA. The function of ac4C formation in tRNA is not fully understood, but ac4C of tRNA can promote its stability and is considered a monitoring indicator of eukaryotic tRNA maturation due to the rapid tRNA degradation pathway., Furthermore, ac4C can influence mRNA translation. The presence of ac4C on mRNA CDS region robustly boosts mRNA stability and promotes protein translation, probably by affecting its interaction with cognate tRNAs during translation.,, However, ac4C modification on 5ʹUTR mainly affects translation initiation by directly and indirectly mediating exquisite locational specificity: ac4C modification immediately adjacent to a strong AUG start codon can repress translation, while ac4C modification downstream of a weak translation initiation site can facilitate translation (Figs. 2, 3, 5 and Table 1).

27As a newly identified RNA modification, ac4C remains largely unknown, particularly its regulators and molecular functions. Only one writer and no erasers or readers have been identified. The functions of ac4C in rRNA, tRNA, and the CDS as well as UTR regions of mRNAs have been reported, however, relevant studies are rare. More investigations are required.

Pseudouridine

28Identified nearly 70 years ago, Ψ is the C5-glycoside isomer of uridine, of which the C5 atom (instead of N1) of the heterocyclic ring is bonded to the C1′ atom of the pentose.– Ψ is present in almost all kinds of RNAs, including coding and non-coding RNAs, and is highly conserved among species (Fig. 1).,,

29Thirteen writers for Ψ have been identified in humans, one of which is Dyskerin pseudouridine synthase 1 (DKC1), a catalytic subunit of the H/ACA snoRNP complex that catalyzes rRNA pseudouridylation, which requires an RNA guide for its catalytic activity.– The remaining 12 writers are RNA-independent single pseudouridine synthases (PUSs): PUS1, PUSL1, PUS3, TRUB1, TRUB2, PUS7, PUS7L, RPUSD1–4, and PUS10; these enzymes have specific cellular localizations and RNA targets.– To date, there are no known Ψ erasers and readers. The absence of erasers may be due to the relatively inert C–C bond formed by the ribose sugar and base, leading to the pseudouridylation process being irreversible (Figs. 2 to 5 and Table 1).

30Previous studies have shown that Ψ plays functional roles in RNA biogenesis, structure, stability, and function to participate in regulating gene expression. tRNAs contain many pseudouridylation sites, which are critical for maintaining stable tRNA structure and mediating tRNA codon–anticodon base pairing and are thereby involved in translation processes.,,– Ψ also represses aberrant protein synthesis by altering the properties of tRNA-derived fragments. Similar to that in tRNA, Ψ is also abundant and present in various rRNA regions, aiding the formation of stable structures.– Moreover, Ψ contributes to ribosome processing and function to ensure translational fidelity in protein synthesis., In snRNAs, Ψ was predicted to influence structure and RNA–RNA or RNA–RBP interactions to function in pre-mRNA splicing.,– Ψ is also involved in regulating pre-mRNA processing, mRNA structure, stability, translational fidelity, and termination, which is another mechanism of translation control apart from tRNA and rRNA modification (Figs. 2–5 and Table 1).,,–

31Despite being identified several decades ago, the contributions of Ψ to multiple cellular processes are just starting to be revealed. Similar to ac4C, new things always take time to be understood. The elucidation of erasers and readers of Ψ will be one of the key directions in the future. Specially, Ψ have already been applied to generating highly effective COVID-19 mRNA vaccines, which is the clinical application of this modification and has potential value for further research.

Uridylation

32In addition to the most widespread homomeric poly (A) tails, uridylation, which consists of the untemplated addition, appears to be the second most prevalent modification at the 3ʹ RNA termini.– Virtually, uridylation can occur on all classes of eukaryotic RNAs including mRNAs, and noncoding RNAs including U6 spliceosomal RNA, guide RNA (gRNA), small interfering RNA (siRNA), miRNA, Piwi-interacting RNA (piRNA), rRNA, and tRNA. Uridylation also targets viral RNA tagging (Fig. 1).,,

33In different substrates, uridylation is catalyzed by different terminal uridylyltransferases (TUTases), which belong to the noncanonical terminal nucleotidyltransferases (TENTs)., In nuclear U6 snRNA, the U6 TUTase (TUT1) specifically added or restored at least four uridines at the 3′ end., TUT4 and/or TUT7 belonging to the TENT3 subfamily are the predominant writers of other cellular uridylation.,– Uridylation erasers or modifiers have not been reported and the uridylation readers include the LSM1-7 complex (for oligouridylation), DIS3L2 (for oligouridylation and polyuridylation), and La protein (Fig. 2 and Table 1).–

34Uridylation alters RNA fate from diverse aspects, including RNA maturation, function, stability, and decay. Uridylation is essential for U6 snRNA maturation and 3′ stabilization to perform splicing function and initiating gRNA maturation.,– The functions of uridylation in miRNAs are diverse. For example, TUTs-mediated pre-miRNA uridylation is a critical step in miRNA biogenesis, which involves repairing or removing defective pre-miRNAs, arm switching, and Dicer processing.– Uridylation on the miRNA 3′ end can recognize noncanonical target sites; on the other hand, it may abrogate target gene repression by directly affecting miRNA 3ʹUTR interactions., Moreover, the 3ʹ addition of uridine promotes miRNA degradation, which also applies to other small RNAs, such as siRNAs and piRNAs., Many studies have demonstrated that uridylation facilitates 5ʹ-to-3ʹ or 3ʹ-to-5ʹ mRNA decay, which is mediated by the recruitment of deadenylases, decapping enzymes, and exonucleases., Uridylation also regulates translation efficiency via various mechanisms, for example, mRNA destabilization, and rRNA and tRNA turnover.,,, Moreover, viral RNA uridylation is involved in antiviral defense.– Uridylated ncRNAs appear overrepresented in exosomes, indicating that uridylation directs RNA sorting into exosomes (Figs. 2, 4 and Table 1).

35Uridylation can act on almost all classes of RNAs in eukaryotic cells, further identification of writers and their auxiliary factors in recognizing specific RNA substrates, as well as of erasers and readers that regulate the deuridylation and decide the fate of uridylated transcripts, will no doubt be key to further understanding the regulatory network. The cell-type and disease-specific patterns of uridylation are also crucial in unraveling the roles of uridylation in cellular biology. Viral RNAs are also targets of uridylation, and the contributions of uridylation in fighting viruses and controlling transposons might be interesting topics of future research considering the current epidemic situation of COVID-19.

Adenosine-to-inosine editing

36A-to-I editing, which converts adenosines to inosines by deamination in RNA molecules, is a widespread co-transcriptional and post-transcriptional modification in mammals., A-to-I editing occurs widely in pre-mRNAs, mRNAs, noncoding RNAs such as miRNAs, lncRNAs as well as tRNAs, and even in virus RNAs (Fig. 1).– The most common targets of A-to-I RNA editing are dsRNA hairpin structures forming from inverted Alu repetitive elements, which are located mainly within introns and untranslated regions and fewer in coding exons.–

37A-to-I editing is the direct conversion of adenosine residues to inosine residues, which is not a conventional “writing” process, so the writers of A-to-I editing are also editors. Adenosine Deaminase TRNA Specific 1 (ADAT1) is responsible for the deamination of adenosine 37 to inosine in eukaryotic tRNA,,, while A-to-I conversion at position 34 of certain tRNAs is catalyzed by ADAT2 and ADAT3 (Fig. 5 and Table 1).– Other A-to-I editing events are catalyzed by adenosine deaminases acting on RNAs (ADAR) family members, which are conserved in mammals.– ADARs share similar functional domain structures of dsRNA-binding domains (dsRBDs) and a larger catalytic adenosine deaminase domain., There are three ADAR members: ADAR1 and ADAR2 deaminate double-stranded (ds)RNA, whereas ADAR3 binds to dsRNA as well as single-stranded (ss)RNA.,, ADAR3 lacks editing activity, and it may competitively bind to dsRNAs with other ADARs to decrease the efficiency of these enzymes.– Different from other additive chemical modifications, A-to-I editing may not be further regulated by erasers/modifiers and readers.

38Generally, this specific adenosine editing can cause transcriptomic diversity and influence the functions of the target RNAs.– Although the probability of A-to-I editing occurrence in the coding regions is relatively low,, studies have revealed its role in impacting the protein translation and function by altering the protein codon.– For example, in colorectal cancer, the A-to-I editing of ras homolog family member Q (RHOQ) transcripts results in the substitution of asparagine with serine at residue 136 of RHOQ protein, leading to increased RHOQ activity and cancer invasion potential. In UTRs, A-to-I RNA editing can regulate RNA processes including transport, translation, and degradation.,– For example, ADAR1 directly edits 3ʹ UTR of XIAP and MDM2 mRNAs to promote nuclear retention of these mRNAs. A-to-I editing facilitates the recruitment of the stabilizing RNA-binding protein human antigen R (HuR) to the 3ʹ UTR of the CTSS mRNA, thereby enhancing the stability and translation CTSS mRNA. In addition, the A-to-I RNA editing in 3ʹUTR has a potential to block the interaction between miRNAs and target genes to hinder the post-transcriptional repression activity. The A-to-I RNA editing in introns usually regulates alternative splicing processes., For example, ADAR1 deficiency may cause alternative splicing in intron 27 of the ABCB1 gene to produce transcripts with retained intron, resulting in nonsense-mediated mRNA decay and decreased ABCB1 mRNA stability. The A-to-I RNA editing in miRNAs may influence the biogenesis and function of miRNAs., A-to-I RNA editing also represses Alu elements in introns to form dsRNA structures, leading to altered linear mRNA and circRNAs generation (Figs. 2, 4 and Table 1).–

39Some reports indicate that A-to-I RNA editing in pri- or pre-miRNA may induce local structural conformation changes, leading to cleavage suppression and decreased mature miRNA biogenesis.– Conversely, some A-to-I RNA editing may not interfere or promote miRNA biogenesis., Specially, ADARs may also bind directly to miRNA precursors to promote miRNA processing by acting as an RNA-binding protein, independent of adjacent A-to-I editing events.– The A-to-I editing in mature miRNAs or siRNAs may impact their target mRNA selection and silencing efficiency.– In lncRNAs, A-to-I editing can affect their secondary structures, stability and interactions with other molecules.,, For example, the A-to-I RNA editing in lncRNAs may impact lncRNA-miRNA interactions and, consequently, change their miRNA sponge function. In tRNAs, A-to-I editing is closely associated with their decoding capacity (Fig. 5 and Table 1). In virus RNAs, A-to-I RNA editing can directly target the genome or transcriptome of RNA viruses to regulate viral pathogenicity as well as host innate immune response, which we will discuss in detail below.–

40Nonetheless, there are many questions that remain to be answered in this field. How the target sites of A-to-I editing are chosen by editors? Although previous studies have identified lots of A-to-I editing sites in human RNA molecules, the significance of such editing for the vast majority of RNA sites remains unclear. Due to A-to-I editing can regulate gene expression through multiple mechanisms, it may be a potential approach to assist or replace RNA interference. Except for influencing miRNA-3ʹUTR and miRNA-lncRNA interaction, A-to-I editing may also affect miRNA-circRNA interaction, which has not been validated yet. Further investigations of RNA editing may provide lessons for precise gene editing.

RNA modifications and T lymphocytes

41T lymphocytes originate from bone marrow progenitors, mature in the thymus, and are transported to the periphery to fulfill immune functions after activation, proliferation, and differentiation., The m5C methyltransferase NSUN2 mediates hyperhomocysteinemia-induced interleukin-17A (IL-17A) upregulation by methylating IL17A mRNA and enhancing its translation in T lymphocytes. A recent study discovered that the m7G cap methyltransferase RNMT plays critical roles in T cell activation by specifically regulating ribosome synthesis. Enzymes modulating miRNA uridylation and uridylated miRNAs are regulated during T cell activation; TUT4 is critical for maintaining miRNA uridylation in the steady state of T lymphocytes and is downregulated during T cell activation, leading to the degradation of uridylated miRNAs. A-to-I RNA editing induced by ADAT1 prevents the sensing of endogenous dsRNAs by MDA5 to participate in thymic T cell maturation, which includes negative selection., Specifically, m5C and Ψ mRNA modification may be promising in the systemic delivery of nanoparticle formulations for regulating T cell immunity and inflammation. Many studies have uncovered the key functions of RNA modifications in the biology of multiple T lymphocyte subsets, which are presented below.

CD4+ T cells

42Naive CD4+ T cells exit the thymus as Th0 cells and differentiate into various cell subsets following different activation signals., The best understood effector cell subsets include T helper (Th) cells (Th1, Th2, Th9, Th17, Th22, et al.), T follicular helper (Tfh) cells, and T regulatory (Treg) cells.– Up to now, there have been some studies revealed that m6A participates in the biology of CD4+ T cells, as well as several subsets.

43First, m6A can affect the functions of CD4+ T cells. For example, ALKBH5 decreases m6A levels in CXCL2 and IFNG mRNA to enhance mRNA stability and translation, thereby promoting CD4+ T cell responses. m6A can also influence CD4+ T cell differentiation and subset functions, which are discussed in detail below. In particular, as CD4+ T cells are the target cells of HIV infection, HIV infection leads to an extensive increase in m6A levels in both host and viral mRNAs, thereby influencing HIV replication and viral RNA nuclear export. During the latent phase of HIV-1 infection, NSUN1 binds with HIV-1 TAR RNA at the 5′ long terminal repeat and generates its m5C methylation, and NSUN1 binding with TAR competes with Tat–TAR interaction, leading to hampered HIV-1 transcriptional elongation and viral latency in CD4+ T cells.

44m5C levels and NSUN2 expression are decreased in the CD4+ T cells of systemic lupus erythematosus (SLE) patients, and hypermethylated m5C in SLE is closely associated with the immune- and inflammation-related pathways, including the immune system, cytokine signaling, and interferon (IFN) signaling. In the CD4+ T cells of SLE patients, ac4C modification in mRNAs is highly conserved and enriched in mRNA CDS regions and participates in critical immune and inflammatory signaling in SLE pathogenesis.

45Th1/Th2 cells Th1 cells are characterized by the expression of the transcription factor T-bet and IFN-γ secretion, and participate in immune responses against intracellular pathogens.– Th2 cells are characterized by the expression of the transcription factor GAΤA3 and IL-4/5/13 and participate in immune responses against larger extracellular pathogens.– A preliminary study using the clustering method demonstrated that m6A may be involved in the Th1/Th2 imbalance and the occurrence of allergic asthma.

46Th17 cells Defined by expression of the master transcription factor RORγt and the production of the lineage cytokines IL-17/IL-22, Th17 cells participate in the elimination of bacteria and fungi and in the pathogenesis of autoimmune diseases.– In enterotoxigenic Bacteroides fragilis-induced intestinal inflammation and tumorigenesis, METTL14-dependent m6A modification promoted the splicing and generation of miR-149-3p to regulate Th17 differentiation.

47Tfh cells With Bcl6 as the lineage-defining transcription factor, Tfh cells are a specialized CD4+ T cell subset essential for germinal centers and B cell responses.– METTL3/METTL14-catalyzed m6A modification of ICOS mRNA suppressed ICOS expression, resulting in impaired Tfh cell differentiation. METTL3-catalyzed m6A modification on the Tcf7 mRNA 3ʹUTR enhanced the stability of Tcf7 mRNA, ensuring TCF-1 expression in maintaining Tfh differentiation.

48Treg cells Specifically expressing FoxP3 in the nucleus, Treg cells play immune regulatory roles in maintaining immune cell homeostasis and preventing immunopathology.– Mettl14 deficiency led to the inability to maintain the differentiation of naïve T cells into induced Treg cells and the Mettl14-deficient Treg cells exhibited impaired function in suppressing naïve T cell–induced inflammation. Mettl3/m6A deficiency in Treg cells increased Socs mRNA levels, leading to deactivation of the IL-2–STAT5 signaling which is integral in maintaining the functions and stability of Treg cells.

CD8+ T cells

49Naive CD8+ T cells proliferate and differentiate into various effector and memory cell types following different activation signals. CD8+ T cells can persist for years and are involved in protective immunity against intracellular pathogens and tumors.– Many studies have demonstrated that m6A methylation regulators are closely associated with CD8+ T cell infiltration in various cancers.– Furthermore, m6A methylation regulators are involved in regulating CD8+ T cell functions. For example, Ythdf1-deficient mice exhibited an elevated antigen-specific CD8+ T cell antitumor response. In tumor-associated macrophages, METTL14 deficiency led to anomalous CD8+ T cell differentiation, driving CD8+ T cell dysfunction and repressing CD8+ T effector cell activation. Tumor-intrinsic FTO restricted the activation and effector states of CD8+ T cells; knockdown of FTO impaired tumor cell glycolytic activity, which restored CD8+ T cell function. m1A levels were negatively related to CD8+ T effector cell proliferation in colon cancer.

RNA modifications and B lymphocytes

50Generally, B lymphocytes are well known for their function of producing antibodies in the adaptive immune response; they are also key modulators of the innate immune response.– Under antigen stimulation, mature B cells are activated and differentiate into memory B cells or plasma cells, which secrete antibodies.– Some studies have reported that m6A modification also participates in B cell biology. For example, METTL14 deficiency inhibits mRNA m6A methylation in developing B cells and blocks IL-7-induced pro-B cell proliferation and the large-pre-B to small-pre-B transition, resulting in severe B cell development stagnation in mice. The RNA exosome cofactor MPP6, m6A modification, and m6A readers play vital roles in modulating lncRNA processing, DNA recombination, and development in B cells. m6A methylation was significantly decreased in the plasma cells of patients with multiple myeloma, which was due to the upregulation of FTO; FTO facilitated multiple myeloma cell proliferation, migration, and invasion by targeting HSF1–HSPs in a YTHDF2-dependent manner. In addition, ADAR1 is essential for normal B lymphopoiesis in the bone marrow and peripheral maintenance.

RNA modifications and DCs

51DCs are key regulators of the innate and adaptive immune responses. They integrate signals from pathogens or other damage and present processed antigens to naïve T cells to control T cell differentiation.– Similar to other immune cell types, the expression of the m6A methylation regulators in diseases is also associated with DC infiltration or depletion., Specially, chemokine receptor 7 (CCR7) increases lnc-Dpf3 expression by reducing m6A modification to prevent its degradation, and lnc-Dpf3 functions in the feedback control of DC migration and inflammatory responses by coupling the epigenetic and metabolic pathways. YTHDF1 identifies m6A-modified mRNAs encoding lysosomal proteases and promotes the translation of these transcripts in DCs, thereby suppressing the cross-presentation of wild-type DCs. DCs exposed to m5C-, m6A-, m5U-, s2U-, or Ψ-modified RNAs express decreased cytokines and activation markers, suggesting that nucleoside modifications repress the latent capacity of RNAs to activate DCs. Mettl3-mediated m6A modification maintained DC maturation and activation by promoting the translation of key factors, including CD40, CD80, and the TLR signaling adaptor TIRAP. Recognition of mRNA m6A methylation by YTHDF1 promoted the translation of lysosomal proteases in DCs and suppressed cross-priming of CD8+ T cells, resulting in defective immune recognition and tumor immune evasion. ADAR1 is required for the differentiation, functionality, and survival of DCs and alveolar macrophages, which involves the A-to-I editing of several coding genes and lncRNAs.

RNA modifications and natural killer cells

52Natural killer (NK) cells are cytotoxic lymphocytes of the innate immune system characterized by target cell killing and cytokine production, functioning in controlling viral and intracellular bacterial infections and tumors, as well as regulating other immune cells.– m6A also influences the functions of NK cells. METTL3-mediated m6A methylation guaranteed the sufficient response of AKT and MAPK signaling to IL-15 by raising SHP-2 expression, thus exerting critical roles in maintaining NK cell homeostasis and anti-tumor immunity. YTHDF2 is increased in NK cells activated by cytokines, tumors, and cytomegalovirus infection, and is essential for maintaining NK cell homeostasis and maturation; YTHDF2 is also required for IL-15–mediated NK cell survival, proliferation, and effector functions by forming a STAT5–YTHDF2 positive feedback loop. In addition, YTHDF2 modulates NK cell proliferation and division partially via reducing Tardbp mRNA stability.

RNA modifications and monocytes or macrophages

53Monocytes and macrophages play an essential role in the innate immune system and present phagocytic activity to exhibit antimicrobial, homeostatic, and immunoregulatory functions.– Due to the wide application of monocyte/macrophage cell lines such as THP-1 and RAW264.7,, there have been many studies investigating the roles of RNA modifications in monocytes or macrophages.

54Some recent studies demonstrate that m6A modification plays critical roles in the antiviral immunity of monocytes and macrophages. For example, m6A-modified HIV-1 RNA escaped RIG-I-mediated RNA sensing and IFN-I-mediated innate antiviral immune responses in differentiated human monocytic cells and primary monocyte-derived macrophages. After vesicular stomatitis virus infection, METTL3 in monocytes/macrophages translocated to the cytoplasm to promote m6A modification of viral RNAs. Then, the m6A-modified viral RNAs were reshaped with decreased double-stranded RNA loads to restrain innate sensing efficacy by MDA5 or RIG-I, resulting in inactivation of the global innate immune signaling pathways. In response to viral infection, macrophages impaired ALKBH5 enzymatic activity and induced m6A modification-mediated inactivation of the OGDH–itaconate pathway to inhibit viral replication. In response to DNA viruses, HNRNPA2B1 promoted m6A modification and nucleocytoplasmic trafficking of CGAS, IFI16, and STING mRNAs, thereby triggering the downstream cytoplasmic TBK1–IRF3 signaling in macrophages. DDX46 recruited ALKBH5 via its DEAD helicase domain to demethylate m6A-modified antiviral transcripts, impeding their nuclear exportation and translation and resulting in impaired IFN production and antiviral innate responses. Under homeostatic conditions, YTHDF3 cooperated with PABP1 and eIF4G2 to enhance FOXO3 translation by binding to the translation initiation region of FOXO3 mRNA and functioning as a negative regulator of antiviral immunity. BCG vaccine exposure can cause increased ADAR1 expression and subsequent enhanced A-to-I editing events in human macrophages to participate in trained immunity.

55m6A modification also regulates monocyte inflammation and immune activity. METTL3-mediated m6A modification and YTHDF2-mediated recognition promoted PGC1A mRNA degradation, leading to insufficient ATP production and excessive reactive oxygen species accumulation in monocyte inflammation. In the peripheral blood immune cells from patients with colorectal cancer, m6A modification was the most abundant in monocytes, and the m6A levels in the monocytes were negatively related to the monocyte immune response.

56m6A modification is involved in various aspects of macrophage biology, including polarization, differentiation, activation, inflammation, and pyroptosis.– For example, IGF2BP2 reads the m6A modification on TSC1 and PPARG mRNA to regulate TSC1 and PPAR-γ expression, thereby skewing M1 macrophages to M2 activation through the TSC1–mTORC1 pathway and PPAR-γ-mediated fatty acid uptake. METTL3-mediated m6A modification of Irakm mRNA accelerated its degradation, resulting in TLR signaling-mediated macrophage activation. METTL3 increased MALAT1 levels through m6A methylation to downregulate USP8; the reduced USP8 decreased TAK1 ubiquitination and degradation, which promoted macrophage pyroptosis and inflammation. TUT7 functioned as a regulator in TLR4-mediated inflammation in macrophages by uridylating and thereby destabilizing the mRNAs of inflammatory mediators, including Zc3h12a. Through targeting the miR-21 precursor, ADAR1 reduces the generation of mature miR-21, then facilitating the polarization of macrophages toward the M2 phenotype via regulating the Foxo1-IL-10 axis.

RNA modifications and granulocytes

57It is well known that granulocytes are divided into three types—neutrophils, eosinophils and basophils., There are relatively few and superficial studies on m6A regulation of granulocytes. m6A modification on c-Rel and Rela mRNA inactivated the NF-κB pathway to suppress IL-8 secretion, thereby inhibiting neutrophil infiltration in papillary thyroid cancer progression in a METTL3- and YTHDF2-dependent manner. Other studies only found that the expression of m6A methylation regulators in tumors was associated with the infiltration of granulocytes, especially neutrophils.–

58To summarize, for functions, RNA modifications regulate various biological processes of immune cells, including development, differentiation, activation, migration and polarization, thus modulating the immune responses. For molecular mechanism, RNA modifications target immune cell RNAs that are responsible for those biological processes and influence RNA processes including generation, transportation, function and metabolization, leading to alterant immune cell biology. However, there are many kinds of RNA modifications and their functions are complex; immune cells are also diverse, and each cell type has its own unique cellular processes. Therefore, although the mechanism presented above is a common one explicating the interaction between RNA modifications and immune cells, the roles of a certain RNA modification in a specific immune cell need to be concretely investigated. Since the relevant research is still in its infancy, more work is needed to further improve the interaction network between RNA modification and immune cells.

Roles of RNA modifications in immune related diseases

59The immune system, consists of innate and adaptive immune, functions in the host defense against harmful antigens and immune homeostasis.– Immune cells are important constituents of the immune system, the dysregulation of which can result in immune related diseases, such as cancers, infection, inflammatory disorders, and autoimmune diseases.– Therefore, via regulating the biological processes of immune cells, RNA modifications can participate in the pathogenesis of immune related diseases.

Cancers

60Although previous research on cancers mainly focused on the malignant phenotypes of the cancer cell itself, in recent years, there are more and more studies on anti-tumor immunity, such as immune checkpoint, immune cell infiltration, cancer immune escape, and cancer immunotherapy.– RNA modifications have been widely investigated in cancers, and they play vital roles in various cellular biology aspects of cancer cells, such as proliferation, metastasis, metabolism, apoptosis, and treatment resistance.,,,, Relatively, the roles of RNA modifications mediating immune cell biology in tumor immunization are not extensively and profoundly considered.

61The most reported RNA modification mediating immune cells in cancers is their influence on immune cell infiltration of tumors.– m6A modification and multiple m6A regulators have been verified to be closely associated with the infiltration of various immune cells in plenty of human cancers.,, Relatively less, m5C, m1A, m7G, ac4C, and Ψ are also found to be related to immune cell infiltration in cancers (Fig. 6).– However, most of these studies investigated the RNA modifications and regulators in cancer tissues and cells, but not in immune cells, and they did not elaborately explain how RNA modification disorders affect immune cell infiltration. Here, we propose an idea that chemokines secreted by tumors may be an intermediate medium regulated by RNA modification in this process.

62There have been some studies exploring the RNA modification dysregulations in immune cells in the tumor immune microenvironment (TIME) and their roles in cancer progression.,– As expected, m6A is the most extensive and in-depth modification inquired. METTL3 is downregulated in tumor-infiltrating NK cells, which affects Ptpn11 m6A modification and downstream IL-15-induced signaling, leading to homeostasis disruption, impaired infiltration, and function of NK cells in TIME, resulting in cancer development. Through targeting and inhibiting the stability of Tardbp mRNA, YTHDF2 is involved in maintaining NK cell homeostasis, maturation, IL-15–mediated survival, and antitumor activity. m6A modification can also influence macrophage reprogramming by mediating SPRED2 translation, and, thereby regulating the activation of NF-κB and STAT3 signaling; METTL3 deficiency impairs the YTHDF1-mediated translation of SPRED2, orchestrating growth, metastasis, and anti-PD-1 therapeutic efficacy of cancer. Another study confirmed this biological effect of m6A in macrophages from another aspect that loss of Mettl3 impairs the TLR4 signaling in macrophage activation by reducing Irakm mRNA degradation. Additionally, lncRNA-PACERR induces the polarization of pro-tumor macrophages in an IGF2BP2 and m6A-dependent manner. YTHDF1 negatively regulates the anti-tumor immune responses of DCs by promoting the translation of m6A-modified mRNAs encoding lysosomal proteases to impair immune recognition, leading to tumor immune evasion. In T cells, m6A modification targets specific genes to control T cell differentiation and maintains the suppressive effects of Tregs, functioning as a negative regulator in the anti-tumor immune responses. CD8+ T cells are direct effector cells of anti-tumor immunity, but there are few studies revealing the m6A disorders in this cell type in cancers. Nevertheless, m6A can influence the anti-tumor response of CD8+ T cells via controlling the biological processes of other related cells in the TIME, such as tumor cells, macrophages, and DCs.,, Especially, the progression of multiple myeloma, a B-cell lymphoma, is mediated by m6A in an FTO and YTHDF2 dependent manner. Relatively, there are no comprehensive studies on the biological functions and molecular mechanisms of other modifications regulating immune cells in cancers till now. (Fig. 6 and Table 2).

63Despite all this, the roles of RNA modifications mediating immune cell biology in cancer immunization remains largely unclear. There seem to be some paradoxes as well as enlightenments. For instance, as we discussed above, m6A deficiency will lead to the disability of some anti-tumor immune cells, whereas YTHDF1 deficiency enhances anti-tumor immune responses. In this regard, we think researchers should comprehensively consider the other roles of writers, erasers, and readers, not just focusing on their regulation of RNA modifications. Moreover, as we know, RNA modifications are vital modulators of normal cell biology, and it is easy to understand that their delicacy may cause the disability of immune cells; but we don’t know what will happen if these modifications are excessive, and whether there is a balance. Besides, the level and functions of some modifications, such as m6A, are diverse between cancer cells and infiltrated immune cells., This indicates researchers to separate cancer cells and infiltrated immune cells when analyzing human or animal tumor samples.

Infectious diseases

64Similar to cancers, the pathogenesis and development of infectious diseases are closely related to the immune defense deficiency that involves the deficiency of the immune system itself and immune escape from pathogens.– According to existing literature, RNA modifications are critical participators in the progression of infectious diseases by affecting the biology of immune cells.

65In recent years, many studies have focused attention on the roles of RNA modifications in viral infection.,,– On one aspect, RNA modifications, such as m6A, m5C, ac4C, Ψ, and RNA editing, directly act on viral RNAs, thus influencing RNA structure, RNA nuclear export, translation, stability, and replication.,– On the other aspect, RNA modifications can regulate host responses to viral infection by mediating viral RNA sensing and signaling, cytokine responses, as well as immune cell functions, which are emphasis discussion of this text. The roles of RNA modifications in regulating immune cell functions in antiviral infection can also be explicated from two perspectives. The first one is that RNA modifications on viral RNAs repress innate immune signaling pathways. For example, m6A-modified HIV-1 and vesicular stomatitis virus RNAs restrain the innate sensing efficacy of MDA5 or RIG-I and thereby impaired IFN-I-mediated innate antiviral immune responses in monocytes and macrophages., The other one is that RNA modifications affect the key factors of antiviral immunity in immune cells, especially in innate immune cells. For example, in monocytes and macrophages, m6A modification affects antiviral transcripts including CGAS, IFI16, STING, Mavs, Traf3, Traf6, and FOXO3, as well as signaling pathways including OGDH–itaconate, TBK1–IRF3, and IFN signaling to function in inhibiting viral replication and antiviral innate immunity.–, In NK cells, except for the antitumor activity, YTHDF2 is also essential for the antiviral activity of NK cells by targeting Tardbp. Especially, as CD4+ T cells are the target of HIV infection, RNA modification participates in the viral processes including replication, nuclear export, transcriptional elongation, and viral latency in CD4+ T cells via modulating biological processes inside CD4+ T cells as described above. After COVID-19 infection, A-to-I editing of endogenous Alu RNAs is decreased in normal human lung cells and in lung biopsies, which may represent the responses of the hosts. ADAR1 mediated RNA editing on extensive duplex RNA structures can lead to repressed innate immune responses and is profitable for viral replication, which indicates that A-to-I editing prevents autoimmunity while also favoring pathogens (Table 3).

66Unfortunately, there is no report on the roles of other RNA modifications other than m6A or A-to-I editing in regulating immune cells in infectious diseases. Also, there is few study on the roles of RNA modifications regulating immune cells in infectious diseases induced by other pathogens such as bacteria and fungi. In addition, as we reviewed above, the roles of RNA modifications in antiviral processes are reported only in innate immunity, while its functions in adaptive immunity are ignored and may be of good research interest. Due to the pathogenesis similarity in immune defense deficiency, the research ideas on cancer may provide lessons for infectious diseases in this field.

Inflammatory and autoimmune diseases

67Inflammation and immune responses are critical in opposing harmful stimuli and injury, while their overreaction or being out of control will lead to inflammatory and autoimmune diseases, causing tissue damage and organ dysfunction.– Generally speaking, inflammatory diseases and autoimmune diseases are different, but they share some similar pathogenesis,– so we discuss them together here. To date, there have some studies verified that RNA modifications may exert biological functions during inflammation and autoimmunity by regulating immune cells.

68In hyperhomocysteinemia, NSUN2 upregulates IL-17A expression by inducing IL-17A mRNA m5C modification in T lymphocytes to mediate chronic inflammation. In allergic asthma, m6A may participate in the Th1/Th2 imbalance. In inflammatory bowel disease (IBD), m6A modification may affect immune infiltration and therapeutic response, and Mettl14 deficiency can cause impaired induction of naïve T cells into iTreg cells by decreasing RORγt expression, thereby leading to spontaneous colitis. Deficiency of Adar1 mediated impaired A-to-I editing in CD4+ T cell will lead to abnormal thymic T cell maturation and impaired negative selection, thereby resulting in autoimmunity disease such as spontaneous colitis., By regulating various aspects of macrophage biology, including polarization, differentiation, activation, inflammation, and pyroptosis, m6A has been found to serve as a mediator in inflammatory diseases including ulcerative colitis, cytokine storm after bacterial infection and liver fibrosis (Table 3).,,

69In SLE, m5C level and NSUN2 expression are decreased in CD4+ T cells, and hypermethylated m5C is related to the immune- and inflammation-related pathways. ac4C modification in mRNAs of SLE CD4+ T cells is highly conserved and enriched in CDS regions and involved in the immune and inflammatory signaling of SLE pathogenesis. ADAR1 mRNA was significantly up-regulated in SLE T cells, which may be a potential mechanism accounting for the mutations in the RI alpha subunit of type 1 protein kinase A. In SLE and some other autoimmune diseases, increased A-to-I RNA editing is involved in generating or elevating the autoantigen load to facilitate autoimmunity progression. In autoimmune encephalomyelitis, ablation of ALKBH5 resulted in increased m6A modification on IFNG and CXCL2 mRNA, as well as impaired responses of CD4+ T cells to repress autoimmunity. In systemic autoimmunity characterized by chronic or acute type I IFN pathway such as systemic sclerosis and other disease contexts, ADAR1p150 isoform mediated A-to-I editing in PBMCs are closely related to type I IFN responses. ADAR1 can edit putatively immunogenic dsRNA substrates to evade MDA5-mediated dsRNA sensing to suppress inflammatory and autoimmune diseases. In the allogeneic transplant model, ADAR1 mediated RNA editing can suppress the host antigraft response and promote graft survival through the ADAR1-miR-21-Foxo1-IL-10 axis (Table 3).

70Although there are few studies on RNA modification regulating immune cells in inflammatory and autoimmune diseases, as we described above, many studies have confirmed the modulation of RNA modifications on the biology of immune cell closely related to these diseases, which build potential connections between cell biology and human diseases. For example, RNA modifications can influence the biology of DCs, monocytes and macrophages, and mediate inflammatory cytokine secretion,,,,, they also probably function in many inflammatory diseases. RNA modifications can affect the activation of T cells and differentiation of Th17 cells, Tfh cells and Treg cells,,,, which play critical roles in the immune dysregulation of some autoimmune diseases such as SLE and multiple sclerosis,, they are likely to participate in the pathogenesis of these diseases. In addition, the research on cancers and infectious diseases listed above may also provide feasible ideas. Due to the contrary roles of immune cell activation and infiltration in cancers and infectious diseases with inflammatory and autoimmune diseases, it is possible that the roles of RNA modifications regulating immune cells are opposite in these diseases.

Conclusions and perspectives

71In this review, we introduced eight RNA modifications including m6A, m5C, m1A, m7G, ac4C, Ψ, uridylation, and A-to-I editing, and summarized their influence on the biology of immune cells, as well as their roles in immune related diseases by regulating immune cells. The modifications involve various kinds of RNAs, such as mRNAs, noncoding RNAs, tRNAs, rRNAs, or even exogenous RNAs (eg., viral RNAs and synthetic RNAs). These modifications are executed by RNA-modifying enzymes such as writers, erasers and readers, and influence RNA processes including generation, transportation, function, and metabolization. Based on these molecular functions, RNA modifications participate in various biological processes of immune cells, including development, differentiation, activation, migration, and polarization, thus modulating the immune response and participating in the pathogenesis of immune related diseases (Fig. 6 and Table 3).

72Currently and a long time in the future, m6A will continue to be a research hotspot in this field, especially in the field of anti-tumor immunity, with relatively adequate background knowledge and mature research technology available. In addition, RNA modifications are mostly investigated in T lymphocytes and monocytes/macrophages, which are relatively easy to obtain, and in T cells or monocytes/macrophages related immune processes and diseases. Moreover, due to the global epidemic of COVID-19, RNA modifications that are involved in antiviral immunity may also be of promising research interest.

73There remain many questions that should be addressed to fully understand the impact of RNA modifications on immune cell biology. Nevertheless, there is continuous progress in this field and there are presently many meaningful points to study. First, to what extent do RNA modifications regulate immune cell biological processes? Are they the main mediators or auxiliary participants? In other words, how helpful would it to rectify RNA modification abnormalities in the treatment of immune related diseases? This is important for designing therapeutic targets and a critical issue to be solved. Second, some RNA modifications have been proven feasible in the systemic delivery of nanoparticle formulations for regulating both immune cell immunity and inflammation in the laboratory.,, Clinical practice is still the grandest challenge, which will be a valuable research direction. Third, essentially, RNA modifications and their functions are regulated by writers, erasers and readers. However, many studies have failed to elucidate the mechanisms causing the anomalies of these regulators. As RNA modifications can target many downstream RNAs and there are no effective interfering drugs, research on the upstream factors is particularly important. Fourth, further exploration of the role of RNA modifications in various immune cells needs to be done, since the current research is mainly focused on a few modifications (e.g., m6A) and immune cells (e.g., T lymphocytes) while overlooking other modifications and immune cells. Immune cells are interconnected and RNA modifications regulate various immune and inflammatory-related factors and signaling pathways. This is a complicated regulatory network that requires us to consummate. Most important, targeting RNA modifications as a treatment in immune related diseases remains in the theoretical stage, and there are no clinical application examples at present. RNA modifications may influence almost all types of RNA, and interfering RNA modifications may cause a wide range of effects. Therefore, gene-specific RNA modification interference is a vital research bottleneck in this area.

References 464

1.
Barbieri I, Kouzarides T. Role of RNA modifications in cancer. Nat. Rev. Cancer. 2020;20:303-322.
Not in our library10.1038/s41568-020-0253-2
2.
Delaunay S, Frye M. RNA modifications regulating cell fate in cancer. Nat. Cell Biol. 2019;21:552-559.
Not in our library10.1038/s41556-019-0319-0
3.
Frye M, Harada BT, Behm M, He C. RNA modifications modulate gene expression during development. Science. 2018;361:1346-1349.
Not in our library10.1126/science.aau1646
4.
Mapping the epigenetic modifications of DNA and RNA · 2020
No notice
5.
Roundtree IA, Evans ME, Pan T, He C. Dynamic RNA modifications in gene expression regulation. Cell. 2017;169:1187-1200.
Not in our library10.1016/j.cell.2017.05.045
6.
Shi H, Wei J, He C. Where, when, and how: context-dependent functions of RNA methylation writers, readers, and erasers. Mol. Cell. 2019;74:640-650.
Not in our library10.1016/j.molcel.2019.04.025
7.
Zaccara S, Ries RJ, Jaffrey SR. Reading, writing and erasing mRNA methylation. Nat. Rev. Mol. Cell Biol. 2019;20:608-624.
Not in our library10.1038/s41580-019-0168-5
8.
Kariko K, Buckstein M, Ni H, Weissman D. Suppression of RNA recognition by toll-like receptors: the impact of nucleoside modification and the evolutionary origin of RNA. Immunity. 2005;23:165-175.
Not in our library10.1016/j.immuni.2005.06.008
9.
Wang Y, et al. The emerging role of m6A modification in regulating the immune system and autoimmune diseases. Front Cell Dev. Biol. 2021;9:755691.
Not in our library10.3389/fcell.2021.755691
10.
Dong L, Cao Y, Hou Y, Liu G. N(6) -methyladenosine RNA methylation: A novel regulator of the development and function of immune cells. J. Cell Physiol. 2022;237:329-345.
Not in our library10.1002/jcp.30576
11.
Xiong X, Yi C, Peng J. Epitranscriptomics: toward a better understanding of RNA modifications. Genomics Proteom. Bioinforma. 2017;15:147-153.
Not in our library10.1016/j.gpb.2017.03.003
12.
The role of m6A modification in the biological functions and diseases · 2021
No notice
13.
The role of m6A RNA methylation in cancer metabolism · 2022
No notice
14.
m6A modification: recent advances, anticancer targeted drug discovery and beyond · 2022
No notice
15.
Huang H, Weng H, Chen J. m(6)A modification in coding and non-coding RNAs: roles and therapeutic implications in cancer. Cancer Cell. 2020;37:270-288.
Not in our library10.1016/j.ccell.2020.02.004
16.
Xu T, et al. Novel insights into the interaction between N6-methyladenosine modification and circular RNA. Mol. Ther. Nucleic Acids. 2022;27:824-837.
Not in our library10.1016/j.omtn.2022.01.007
17.
Zhu ZM, Huo FC, Pei DS. Function and evolution of RNA N6-methyladenosine modification. Int. J. Biol. Sci. 2020;16:1929-1940.
Not in our library10.7150/ijbs.45231
18.
Insights into N6-methyladenosine and programmed cell death in cancer · 2022
No notice
19.
RNA N6-methyladenosine modification in cancers: current status and perspectives · 2018
No notice
20.
Kan RL, Chen J, Sallam T. Crosstalk between epitranscriptomic and epigenetic mechanisms in gene regulation. Trends Genet. 2022;38:182-193.
Not in our library10.1016/j.tig.2021.06.014
21.
Garcias Morales D, Reyes JL. A birds’-eye view of the activity and specificity of the mRNA m(6) A methyltransferase complex. Wiley Interdiscip. Rev. RNA. 2021;12:e1618.
Not in our library10.1002/wrna.1618
22.
N6-methyladenosine methyltransferases: functions, regulation, and clinical potential · 2021
No notice
23.
Wang X, et al. Structural basis of N(6)-adenosine methylation by the METTL3-METTL14 complex. Nature. 2016;534:575-578.
Not in our library10.1038/nature18298
24.
Liu J, et al. A METTL3-METTL14 complex mediates mammalian nuclear RNA N6-adenosine methylation. Nat. Chem. Biol. 2014;10:93-95.
Not in our library10.1038/nchembio.1432
25.
Wang P, Doxtader KA, Nam Y. Structural Basis for Cooperative Function of Mettl3 and Mettl14 Methyltransferases. Mol. Cell. 2016;63:306-317.
Not in our library10.1016/j.molcel.2016.05.041
26.
Ma H, et al. N(6-)Methyladenosine methyltransferase ZCCHC4 mediates ribosomal RNA methylation. Nat. Chem. Biol. 2019;15:88-94.
Not in our library10.1038/s41589-018-0184-3
27.
Ignatova VV, et al. The rRNA m(6)A methyltransferase METTL5 is involved in pluripotency and developmental programs. Genes Dev. 2020;34:715-729.
Not in our library10.1101/gad.333369.119
28.
Ren W, et al. Structure and regulation of ZCCHC4 in m(6)A-methylation of 28S rRNA. Nat. Commun. 2019;10:5042.
Not in our library10.1038/s41467-019-12923-x
29.
van Tran N, et al. The human 18S rRNA m6A methyltransferase METTL5 is stabilized by TRMT112. Nucleic Acids Res. 2019;47:7719-7733.
Not in our library10.1093/nar/gkz619
30.
Pinto R, et al. The human methyltransferase ZCCHC4 catalyses N6-methyladenosine modification of 28S ribosomal RNA. Nucleic Acids Res. 2020;48:830-846.
Not in our library10.1093/nar/gkz1147
31.
Pendleton KE, et al. The U6 snRNA m(6)A methyltransferase METTL16 regulates SAM synthetase intron retention. Cell. 2017;169:824-835.e814.
Not in our library10.1016/j.cell.2017.05.003
32.
Aoyama T, Yamashita S, Tomita K. Mechanistic insights into m6A modification of U6 snRNA by human METTL16. Nucleic Acids Res. 2020;48:5157-5168.
Not in our library10.1093/nar/gkaa227
33.
Su R, et al. METTL16 exerts an m(6)A-independent function to facilitate translation and tumorigenesis. Nat. Cell Biol. 2022;24:205-216.
Not in our library10.1038/s41556-021-00835-2
34.
Jia G, et al. N6-methyladenosine in nuclear RNA is a major substrate of the obesity-associated FTO. Nat. Chem. Biol. 2011;7:885-887.
Not in our library10.1038/nchembio.687
35.
Mauer J, et al. Reversible methylation of m(6)A(m) in the 5’ cap controls mRNA stability. Nature. 2017;541:371-375.
Not in our library10.1038/nature21022
36.
Wei J, et al. Differential m(6)A, m(6)A(m), and m(1)A Demethylation Mediated by FTO in the Cell Nucleus and Cytoplasm. Mol. Cell. 2018;71:973-985.e975.
Not in our library10.1016/j.molcel.2018.08.011
37.
Zheng G, et al. ALKBH5 is a mammalian RNA demethylase that impacts RNA metabolism and mouse fertility. Mol. Cell. 2013;49:18-29.
Not in our library10.1016/j.molcel.2012.10.015
38.
Wei J, et al. FTO mediates LINE1 m(6)A demethylation and chromatin regulation in mESCs and mouse development. Science. 2022;376:968-973.
Not in our library10.1126/science.abe9582
39.
RNA demethylase ALKBH5 in cancer: from mechanisms to therapeutic potential · 2022
No notice
40.
Essential role of ALKBH5-mediated RNA demethylation modification in bile acid-induced gastric intestinal metaplasia · 2021
Not checked
41.
Shi R, et al. Linking the YTH domain to cancer: the importance of YTH family proteins in epigenetics. Cell Death Dis. 2021;12:346.
Not in our library10.1038/s41419-021-03625-8
42.
Lasman L, et al. Context-dependent functional compensation between Ythdf m(6)A reader proteins. Genes Dev. 2020;34:1373-1391.
Not in our library10.1101/gad.340695.120
43.
Wang X, et al. N(6)-methyladenosine modulates messenger RNA translation efficiency. Cell. 2015;161:1388-1399.
Not in our library10.1016/j.cell.2015.05.014
44.
Li A, et al. Cytoplasmic m(6)A reader YTHDF3 promotes mRNA translation. Cell Res. 2017;27:444-447.
Not in our library10.1038/cr.2017.10
45.
Lee Y, Choe J, Park OH, Kim YK. Molecular mechanisms driving mRNA degradation by m(6)A modification. Trends Genet. 2020;36:177-188.
Not in our library10.1016/j.tig.2019.12.007
46.
Ries RJ, et al. m(6)A enhances the phase separation potential of mRNA. Nature. 2019;571:424-428.
Not in our library10.1038/s41586-019-1374-1
47.
Zaccara S, Jaffrey SR. A unified model for the function of YTHDF proteins in regulating m(6)A-modified mRNA. Cell. 2020;181:1582-1595.e1518.
Not in our library10.1016/j.cell.2020.05.012
48.
Liu J, et al. N (6)-methyladenosine of chromosome-associated regulatory RNA regulates chromatin state and transcription. Science. 2020;367:580-586.
Not in our library10.1126/science.aay6018
49.
Xiao W, et al. Nuclear m(6)A Reader YTHDC1 regulates mRNA splicing. Mol. Cell. 2016;61:507-519.
Not in our library10.1016/j.molcel.2016.01.012
50.
Widagdo J, Anggono V, Wong JJ. The multifaceted effects of YTHDC1-mediated nuclear m(6)A recognition. Trends Genet. 2022;38:325-332.
Not in our library10.1016/j.tig.2021.11.005
51.
m6A in mRNA coding regions promotes translation via the RNA helicase-containing YTHDC2 · 2019
No notice
52.
Zhou B, et al. N(6) -methyladenosine reader protein YT521-B homology domain-containing 2 suppresses liver steatosis by regulation of mRNA stability of lipogenic genes. Hepatology. 2021;73:91-103.
Not in our library10.1002/hep.31220
53.
Li, N. & Rana, T. M. Regulation of antiviral innate immunity by chemical modification of viral RNA. Wiley Interdiscip Rev RNA. e1720 (2022).
Not in our library10.1002/wrna.1720
54.
Huang H, et al. Recognition of RNA N(6)-methyladenosine by IGF2BP proteins enhances mRNA stability and translation. Nat. Cell Biol. 2018;20:285-295.
Not in our library10.1038/s41556-018-0045-z
55.
Sun CY, Cao D, Du BB, Chen CW, Liu D. The role of Insulin-like growth factor 2 mRNA-binding proteins (IGF2BPs) as m(6)A readers in cancer. Int J. Biol. Sci. 2022;18:2744-2758.
Not in our library10.7150/ijbs.70458
56.
Alarcon CR, et al. HNRNPA2B1 is a mediator of m(6)A-dependent nuclear RNA processing events. Cell. 2015;162:1299-1308.
Not in our library10.1016/j.cell.2015.08.011
57.
Liu N, et al. N(6)-methyladenosine-dependent RNA structural switches regulate RNA-protein interactions. Nature. 2015;518:560-564.
Not in our library10.1038/nature14234
58.
Liu N, et al. N6-methyladenosine alters RNA structure to regulate binding of a low-complexity protein. Nucleic Acids Res. 2017;45:6051-6063.
Not in our library10.1093/nar/gkx141
59.
Zhou KI, et al. Regulation of co-transcriptional pre-mRNA splicing by m(6)A through the low-complexity protein hnRNPG. Mol. Cell. 2019;76:70-81.e79.
Not in our library10.1016/j.molcel.2019.07.005
60.
Jiang L, et al. Interaction of tau with HNRNPA2B1 and N(6)-methyladenosine RNA mediates the progression of tauopathy. Mol. Cell. 2021;81:4209-4227.e4212.
Not in our library10.1016/j.molcel.2021.07.038
61.
Meyer KD, et al. 5’ UTR m(6)a promotes cap-independent translation. Cell. 2015;163:999-1010.
Not in our library10.1016/j.cell.2015.10.012
62.
Choe J, et al. mRNA circularization by METTL3-eIF3h enhances translation and promotes oncogenesis. Nature. 2018;561:556-560.
Not in our library10.1038/s41586-018-0538-8
63.
A novel m6A reader Prrc2a controls oligodendroglial specification and myelination · 2018
No notice
64.
The Tudor SND1 protein is an m6A RNA reader essential for replication of Kaposi’s sarcoma-associated herpesvirus · 2019
No notice
65.
Yang X, et al. m(6)A promotes R-loop formation to facilitate transcription termination. Cell Res. 2019;29:1035-1038.
Not in our library10.1038/s41422-019-0235-7
66.
Wang X, et al. Crosstalk between N6-methyladenosine modification and circular RNAs: current understanding and future directions. Mol. Cancer. 2021;20:121.
Not in our library10.1186/s12943-021-01415-6
67.
He PC, He C. m(6) A RNA methylation: from mechanisms to therapeutic potential. EMBO J. 2021;40:e105977.
Not in our library10.15252/embj.2020105977
68.
Wiener D, Schwartz S. The epitranscriptome beyond m(6)A. Nat. Rev. Genet. 2021;22:119-131.
Not in our library10.1038/s41576-020-00295-8
69.
Are Small Nucleolar RNAs “CRISPRable”? A Report on Box C/D Small Nucleolar RNA Editing in Human Cells · 2019
Not checked
70.
Novel insights into the interplay between m6A modification and noncoding RNAs in cancer · 2020
No notice
71.
Alarcon CR, Lee H, Goodarzi H, Halberg N, Tavazoie SF. N6-methyladenosine marks primary microRNAs for processing. Nature. 2015;519:482-485.
Not in our library10.1038/nature14281
72.
Interaction between N6-methyladenosine (m6A) modification and noncoding RNAs in cancer · 2020
No notice
73.
Yankova E, et al. Small-molecule inhibition of METTL3 as a strategy against myeloid leukaemia. Nature. 2021;593:597-601.
Not in our library10.1038/s41586-021-03536-w
74.
Dolbois A, et al. 1,4,9-triazaspiro[5.5]undecan-2-one derivatives as potent and selective METTL3 inhibitors. J. Med. Chem. 2021;64:12738-12760.
Not in our library10.1021/acs.jmedchem.1c00773
75.
Amos H, Korn M. 5-Methyl cytosine in the RNA of Escherichia coli. Biochim Biophys. Acta. 1958;29:444-445.
Not in our library10.1016/0006-3002(58)90214-2
76.
Eukaryotic 5-methylcytosine (m5C) RNA Methyltransferases: Mechanisms, Cellular Functions, and Links to Disease · 2019
No notice
77.
Garcia-Vilchez R, Sevilla A, Blanco S. Post-transcriptional regulation by cytosine-5 methylation of RNA. Biochim Biophys. Acta Gene Regul. Mech. 2019;1862:240-252.
Not in our library10.1016/j.bbagrm.2018.12.003
78.
The dynamic RNA modification 5‐methylcytosine and its emerging role as an epitranscriptomic mark · 2018
No notice
79.
The role of m6A, m5C and Ψ RNA modifications in cancer: Novel therapeutic opportunities · 2021
No notice
80.
Blaze J, et al. Neuronal Nsun2 deficiency produces tRNA epitranscriptomic alterations and proteomic shifts impacting synaptic signaling and behavior. Nat. Commun. 2021;12:4913.
Not in our library10.1038/s41467-021-24969-x
81.
Shinoda S, et al. Mammalian NSUN2 introduces 5-methylcytidines into mitochondrial tRNAs. Nucleic Acids Res. 2019;47:8734-8745.
Not in our library10.1093/nar/gkz575
82.
NSUN2 introduces 5-methylcytosines in mammalian mitochondrial tRNAs · 2019
No notice
83.
Li J, et al. Archaeal NSUN6 catalyzes m5C72 modification on a wide-range of specific tRNAs. Nucleic Acids Res. 2019;47:2041-2055.
Not in our library10.1093/nar/gky1236
84.
Squires JE, et al. Widespread occurrence of 5-methylcytosine in human coding and non-coding RNA. Nucleic Acids Res. 2012;40:5023-5033.
Not in our library10.1093/nar/gks144
85.
The ribosomal RNA m5C methyltransferase NSUN-1 modulates healthspan and oogenesis in Caenorhabditis elegans · 2020
Not checked
86.
Methylation of ribosomal RNA by NSUN5 is a conserved mechanism modulating organismal lifespan · 2015
Corrected
87.
Navarro IC, et al. Translational adaptation to heat stress is mediated by RNA 5-methylcytosine in Caenorhabditis elegans. EMBO J. 2021;40:e105496.
Not in our library10.15252/embj.2020105496
88.
Deposition of 5-Methylcytosine on Enhancer RNAs Enables the Coactivator Function of PGC-1α · 2016
Not checked
89.
Shen H, et al. TET-mediated 5-methylcytosine oxidation in tRNA promotes translation. J. Biol. Chem. 2021;296:100087.
Not in our library10.1074/jbc.ra120.014226
90.
Yang H, et al. FMRP promotes transcription-coupled homologous recombination via facilitating TET1-mediated m5C RNA modification demethylation. Proc. Natl. Acad. Sci. USA. 2022;119:e2116251119.
Not in our library10.1073/pnas.2116251119
91.
Arguello AE, et al. Reactivity-dependent profiling of RNA 5-methylcytidine dioxygenases. Nat. Commun. 2022;13:4176.
Not in our library10.1038/s41467-022-31876-2
92.
Meng H, et al. DNA methylation, its mediators and genome integrity. Int. J. Biol. Sci. 2015;11:604-617.
Not in our library10.7150/ijbs.11218
93.
Ito S, et al. Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine. Science. 2011;333:1300-1303.
Not in our library10.1126/science.1210597
94.
Hu L, et al. Structural insight into substrate preference for TET-mediated oxidation. Nature. 2015;527:118-122.
Not in our library10.1038/nature15713
95.
Pfaffeneder T, et al. Tet oxidizes thymine to 5-hydroxymethyluracil in mouse embryonic stem cell DNA. Nat. Chem. Biol. 2014;10:574-581.
Not in our library10.1038/nchembio.1532
96.
Wang L, et al. Molecular basis for 5-carboxycytosine recognition by RNA polymerase II elongation complex. Nature. 2015;523:621-625.
Not in our library10.1038/nature14482
97.
Delatte B, et al. RNA biochemistry. Transcriptome-wide distribution and function of RNA hydroxymethylcytosine. Science. 2016;351:282-285.
Not in our library10.1126/science.aac5253
98.
Fu L, et al. Tet-mediated formation of 5-hydroxymethylcytosine in RNA. J. Am. Chem. Soc. 2014;136:11582-11585.
Not in our library10.1021/ja505305z
99.
Kawarada L, et al. ALKBH1 is an RNA dioxygenase responsible for cytoplasmic and mitochondrial tRNA modifications. Nucleic Acids Res. 2017;45:7401-7415.
Not in our library10.1093/nar/gkx354
100.
Dominissini D, Rechavi G. 5-methylcytosine mediates nuclear export of mRNA. Cell Res. 2017;27:717-719.
Not in our library10.1038/cr.2017.73
101.
Liu Y, et al. mRNA m5C controls adipogenesis by promoting CDKN1A mRNA export and translation. RNA Biol. 2021;18:711-721.
Not in our library10.1080/15476286.2021.1980694
102.
Yang Y, et al. RNA 5-methylcytosine facilitates the maternal-to-zygotic transition by preventing maternal mRNA decay. Mol. Cell. 2019;75:1188-1202.e1111.
Not in our library10.1016/j.molcel.2019.06.033
103.
Chen X, et al. 5-methylcytosine promotes pathogenesis of bladder cancer through stabilizing mRNAs. Nat. Cell Biol. 2019;21:978-990.
Not in our library10.1038/s41556-019-0361-y
104.
Dai X, et al. YTHDF2 binds to 5-methylcytosine in RNA and modulates the maturation of ribosomal RNA. Anal. Chem. 2020;92:1346-1354.
Not in our library10.1021/acs.analchem.9b04505
105.
Mitochondrial RNA modifications shape metabolic plasticity in metastasis · 2022
No notice
106.
Hussain S, et al. NSun2-mediated cytosine-5 methylation of vault noncoding RNA determines its processing into regulatory small RNAs. Cell Rep. 2013;4:255-261.
Not in our library10.1016/j.celrep.2013.06.029
107.
Zhang X, et al. The tRNA methyltransferase NSun2 stabilizes p16INK(4) mRNA by methylating the 3’-untranslated region of p16. Nat. Commun. 2012;3:712.
Not in our library10.1038/ncomms1692
108.
5-methylcytosine promotes mRNA export — NSUN2 as the methyltransferase and ALYREF as an m5C reader · 2017
No notice
109.
Sequence- and structure-specific cytosine-5 mRNA methylation by NSUN6 · 2020
No notice
110.
Dunn DB. The occurrence of 1-methyladenine in ribonucleic acid. Biochim Biophys. Acta. 1961;46:198-200.
Not in our library10.1016/0006-3002(61)90668-0
111.
Zhou H, et al. Evolution of a reverse transcriptase to map N(1)-methyladenosine in human messenger RNA. Nat. Methods. 2019;16:1281-1288.
Not in our library10.1038/s41592-019-0550-4
112.
Macon JB, Wolfenden R. 1-Methyladenosine. Dimroth rearrangement and reversible reduction. Biochemistry. 1968;7:3453-3458.
Not in our library10.1021/bi00850a021
113.
Waku T, et al. NML-mediated rRNA base methylation links ribosomal subunit formation to cell proliferation in a p53-dependent manner. J. Cell Sci. 2016;129:2382-2393.
Not in our library10.1242/jcs.183723
114.
Saikia M, Fu Y, Pavon-Eternod M, He C, Pan T. Genome-wide analysis of N1-methyl-adenosine modification in human tRNAs. RNA. 2010;16:1317-1327.
Not in our library10.1261/rna.2057810
115.
Safra M, et al. The m1A landscape on cytosolic and mitochondrial mRNA at single-base resolution. Nature. 2017;551:251-255.
Not in our library10.1038/nature24456
116.
Mitochondrial 16S rRNA Is Methylated by tRNA Methyltransferase TRMT61B in All Vertebrates · 2016
Corrected
117.
Howell NW, Jora M, Jepson BF, Limbach PA, Jackman JE. Distinct substrate specificities of the human tRNA methyltransferases TRMT10A and TRMT10B. RNA. 2019;25:1366-1376.
Not in our library10.1261/rna.072090.119
118.
Liu F, et al. ALKBH1-mediated tRNA demethylation regulates translation. Cell. 2016;167:816-828.e816.
Not in our library10.1016/j.cell.2016.09.038
119.
Li X, et al. Transcriptome-wide mapping reveals reversible and dynamic N(1)-methyladenosine methylome. Nat. Chem. Biol. 2016;12:311-316.
Not in our library10.1038/nchembio.2040
120.
Woo HH, Chambers SK. Human ALKBH3-induced m(1)A demethylation increases the CSF-1 mRNA stability in breast and ovarian cancer cells. Biochim Biophys. Acta Gene Regul. Mech. 2019;1862:35-46.
Not in our library10.1016/j.bbagrm.2018.10.008
121.
Chen Z, et al. Transfer RNA demethylase ALKBH3 promotes cancer progression via induction of tRNA-derived small RNAs. Nucleic Acids Res. 2019;47:2533-2545.
Not in our library10.1093/nar/gky1250
122.
Zhang LS, et al. ALKBH7-mediated demethylation regulates mitochondrial polycistronic RNA processing. Nat. Cell Biol. 2021;23:684-691.
Not in our library10.1038/s41556-021-00709-7
123.
Dai X, Wang T, Gonzalez G, Wang Y. Identification of YTH Domain-Containing Proteins as the Readers for N1-Methyladenosine in RNA. Anal. Chem. 2018;90:6380-6384.
Not in our library10.1021/acs.analchem.8b01703
124.
Zhou H, et al. m(1)A and m(1)G disrupt A-RNA structure through the intrinsic instability of Hoogsteen base pairs. Nat. Struct. Mol. Biol. 2016;23:803-810.
Not in our library10.1038/nsmb.3270
125.
Dominissini D, et al. The dynamic N(1)-methyladenosine methylome in eukaryotic messenger RNA. Nature. 2016;530:441-446.
Not in our library10.1038/nature16998
126.
Li X, et al. Base-resolution mapping reveals distinct m(1)A methylome in nuclear- and mitochondrial-encoded transcripts. Mol. Cell. 2017;68:993-1005.e1009.
Not in our library10.1016/j.molcel.2017.10.019
127.
Zhang LS, et al. Transcriptome-wide mapping of internal N(7)-methylguanosine methylome in Mammalian mRNA. Mol. Cell. 2019;74:1304-1316.e1308.
Not in our library10.1016/j.molcel.2019.03.036
128.
Detection of internal N7-methylguanosine (m7G) RNA modifications by mutational profiling sequencing · 2019
No notice
129.
Chen, Y., Lin, H., Miao, L. & He, J. Role of N7-methylguanosine (m(7)G) in cancer. Trends Cell Biol. 32, 819–824 (2022).
Not in our library10.1016/j.tcb.2022.07.001
130.
Ramanathan A, Robb GB, Chan SH. mRNA capping: biological functions and applications. Nucleic Acids Res. 2016;44:7511-7526.
Not in our library10.1093/nar/gkw551
131.
The potential role of N7-methylguanosine (m7G) in cancer · 2022
No notice
132.
Shatsky IN, Terenin IM, Smirnova VV, Andreev DE. Cap-Independent Translation: What’s in a Name? Trends Biochem Sci. 2018;43:882-895.
Not in our library10.1016/j.tibs.2018.04.011
133.
Katsara O, Schneider RJ. m(7)G tRNA modification reveals new secrets in the translational regulation of cancer development. Mol. Cell. 2021;81:3243-3245.
Not in our library10.1016/j.molcel.2021.07.030
134.
Sloan KE, et al. Tuning the ribosome: The influence of rRNA modification on eukaryotic ribosome biogenesis and function. RNA Biol. 2017;14:1138-1152.
Not in our library10.1080/15476286.2016.1259781
135.
METTL1 Promotes let-7 MicroRNA Processing via m7G Methylation · 2019
No notice
136.
Varshney D, et al. Molecular basis of RNA guanine-7 methyltransferase (RNMT) activation by RAM. Nucleic Acids Res. 2016;44:10423-10436.
Not in our library10.1093/nar/gkw637
137.
mRNA Cap Methyltransferase, RNMT-RAM, Promotes RNA Pol II-Dependent Transcription · 2018
Not checked
138.
Aregger M, et al. CDK1-cyclin B1 activates RNMT, coordinating mRNA cap methylation with G1 phase transcription. Mol. Cell. 2016;61:734-746.
Not in our library10.1016/j.molcel.2016.02.008
139.
Ma J, et al. METTL1/WDR4-mediated m(7)G tRNA modifications and m(7)G codon usage promote mRNA translation and lung cancer progression. Mol. Ther. 2021;29:3422-3435.
Not in our library10.1016/j.ymthe.2021.08.005
140.
Lin S, et al. Mettl1/Wdr4-mediated m(7)G tRNA methylome is required for normal mRNA translation and embryonic stem cell self-renewal and differentiation. Mol. Cell. 2018;71:244-255.e245.
Not in our library10.1016/j.molcel.2018.06.001
141.
Malbec L, et al. Dynamic methylome of internal mRNA N(7)-methylguanosine and its regulatory role in translation. Cell Res. 2019;29:927-941.
Not in our library10.1038/s41422-019-0230-z
142.
Galloway A, et al. Upregulation of RNA cap methyltransferase RNMT drives ribosome biogenesis during T cell activation. Nucleic Acids Res. 2021;49:6722-6738.
Not in our library10.1093/nar/gkab465
143.
Monecke T, Dickmanns A, Ficner R. Structural basis for m7G-cap hypermethylation of small nuclear, small nucleolar and telomerase RNA by the dimethyltransferase TGS1. Nucleic Acids Res. 2009;37:3865-3877.
Not in our library10.1093/nar/gkp249
144.
Mars JC, Ghram M, Culjkovic-Kraljacic B, Borden KLB. The cap-binding complex CBC and the eukaryotic translation factor eIF4E: co-conspirators in cap-dependent RNA maturation and translation. Cancers (Basel). 2021;13:6185.
Not in our library10.3390/cancers13246185
145.
Dou Y, et al. Affinity proteomic dissection of the human nuclear cap-binding complex interactome. Nucleic Acids Res. 2020;48:10456-10469.
Not in our library10.1093/nar/gkaa743
146.
Jensen KB, et al. capCLIP: a new tool to probe translational control in human cells through capture and identification of the eIF4E-mRNA interactome. Nucleic Acids Res. 2021;49:e105.
Not in our library10.1093/nar/gkab604
147.
mRNA cap regulation in mammalian cell function and fate · 2019
No notice
148.
Orellana EA, et al. METTL1-mediated m(7)G modification of Arg-TCT tRNA drives oncogenic transformation. Mol. Cell. 2021;81:3323-3338.e3314.
Not in our library10.1016/j.molcel.2021.06.031
149.
Thongdee N, et al. TrmB, a tRNA m7G46 methyltransferase, plays a role in hydrogen peroxide resistance and positively modulates the translation of katA and katB mRNAs in Pseudomonas aeruginosa. Nucleic Acids Res. 2019;47:9271-9281.
Not in our library10.1093/nar/gkz702
150.
Kouzarides T, Pandolfini L, Barbieri I, Bannister AJ, Andrews B. Further evidence supporting N7-methylation of guanosine (m(7)G) in human MicroRNAs. Mol. Cell. 2020;79:201-202.
Not in our library10.1016/j.molcel.2020.05.023
151.
Boulias K, Greer EL. Put the pedal to the METTL1: adding internal m(7)G increases mRNA translation efficiency and augments miRNA processing. Mol. Cell. 2019;74:1105-1107.
Not in our library10.1016/j.molcel.2019.06.004
152.
MYC-targeted WDR4 promotes proliferation, metastasis, and sorafenib resistance by inducing CCNB1 translation in hepatocellular carcinoma · 2021
No notice
153.
METTL1‐m 7 G‐EGFR/EFEMP1 axis promotes the bladder cancer development · 2021
No notice
154.
Deng Y, Zhou Z, Ji W, Lin S, Wang M. METTL1-mediated m(7)G methylation maintains pluripotency in human stem cells and limits mesoderm differentiation and vascular development. Stem Cell Res Ther. 2020;11:306.
Not in our library10.1186/s13287-020-01814-4
155.
Bartee D, Nance KD, Meier JL. Site-specific synthesis of N(4)-acetylcytidine in RNA reveals physiological duplex stabilization. J. Am. Chem. Soc. 2022;144:3487-3496.
Not in our library10.1021/jacs.1c11985
156.
Thalalla Gamage S, Sas-Chen A, Schwartz S, Meier JL. Quantitative nucleotide resolution profiling of RNA cytidine acetylation by ac4C-seq. Nat. Protoc. 2021;16:2286-2307.
Not in our library10.1038/s41596-021-00501-9
157.
Thomas JM, et al. A chemical signature for cytidine acetylation in RNA. J. Am. Chem. Soc. 2018;140:12667-12670.
Not in our library10.1021/jacs.8b06636
158.
Arango D, et al. Acetylation of cytidine in mRNA promotes translation efficiency. Cell. 2018;175:1872-1886.e1824.
Not in our library10.1016/j.cell.2018.10.030
159.
The Processing, Gene Regulation, Biological Functions, and Clinical Relevance of N4-Acetylcytidine on RNA: A Systematic Review · 2020
No notice
160.
Sharma S, et al. Yeast Kre33 and human NAT10 are conserved 18S rRNA cytosine acetyltransferases that modify tRNAs assisted by the adaptor Tan1/THUMPD1. Nucleic Acids Res. 2015;43:2242-2258.
Not in our library10.1093/nar/gkv075
161.
Sas-Chen A, et al. Dynamic RNA acetylation revealed by quantitative cross-evolutionary mapping. Nature. 2020;583:638-643.
Not in our library10.1038/s41586-020-2418-2
162.
Broly M, et al. THUMPD1 bi-allelic variants cause loss of tRNA acetylation and a syndromic neurodevelopmental disorder. Am. J. Hum. Genet. 2022;109:587-600.
Not in our library10.1016/j.ajhg.2022.02.001
163.
Bortolin-Cavaille ML, et al. Probing small ribosomal subunit RNA helix 45 acetylation across eukaryotic evolution. Nucleic Acids Res. 2022;50:6284-6299.
Not in our library10.1093/nar/gkac404
164.
Ito S, et al. Human NAT10 is an ATP-dependent RNA acetyltransferase responsible for N4-acetylcytidine formation in 18 S ribosomal RNA (rRNA). J. Biol. Chem. 2014;289:35724-35730.
Not in our library10.1074/jbc.c114.602698
165.
Wang K, et al. PIWI-interacting RNA HAAPIR regulates cardiomyocyte death after myocardial infarction by promoting NAT10-mediated ac(4) C acetylation of Tfec mRNA. Adv. Sci. (Weinh.). 2022;9:e2106058.
Not in our library10.1002/advs.202106058
166.
Dewe JM, Whipple JM, Chernyakov I, Jaramillo LN, Phizicky EM. The yeast rapid tRNA decay pathway competes with elongation factor 1A for substrate tRNAs and acts on tRNAs lacking one or more of several modifications. RNA. 2012;18:1886-1896.
Not in our library10.1261/rna.033654.112
167.
Whipple JM, Lane EA, Chernyakov I, D’Silva S, Phizicky EM. The yeast rapid tRNA decay pathway primarily monitors the structural integrity of the acceptor and T-stems of mature tRNA. Genes Dev. 2011;25:1173-1184.
Not in our library10.1101/gad.2050711
168.
Dominissini D, Rechavi G. N(4)-acetylation of cytidine in mRNA by NAT10 regulates stability and translation. Cell. 2018;175:1725-1727.
Not in our library10.1016/j.cell.2018.11.037
169.
Tsai K, et al. Acetylation of cytidine residues boosts HIV-1 gene expression by increasing viral RNA stability. Cell Host Microbe. 2020;28:306-312.e306.
Not in our library10.1016/j.chom.2020.05.011
170.
Arango D, et al. Direct epitranscriptomic regulation of mammalian translation initiation through N4-acetylcytidine. Mol. Cell. 2022;82:2797-2814.e2711.
Not in our library10.1016/j.molcel.2022.05.016
171.
Zhao BS, He C. Pseudouridine in a new era of RNA modifications. Cell Res. 2015;25:153-154.
Not in our library10.1038/cr.2014.143
172.
Borchardt EK, Martinez NM, Gilbert WV. Regulation and function of RNA pseudouridylation in human cells. Annu Rev. Genet. 2020;54:309-336.
Not in our library10.1146/annurev-genet-112618-043830
173.
Ge J, Yu YT. RNA pseudouridylation: new insights into an old modification. Trends Biochem Sci. 2013;38:210-218.
Not in our library10.1016/j.tibs.2013.01.002
174.
Karijolich J, Yi C, Yu YT. Transcriptome-wide dynamics of RNA pseudouridylation. Nat. Rev. Mol. Cell Biol. 2015;16:581-585.
Not in our library10.1038/nrm4040
175.
Role of main RNA modifications in cancer: N6-methyladenosine, 5-methylcytosine, and pseudouridine · 2022
No notice
176.
Cerneckis J, Cui Q, He C, Yi C, Shi Y. Decoding pseudouridine: an emerging target for therapeutic development. Trends Pharm. Sci. 2022;43:522-535.
Not in our library10.1016/j.tips.2022.03.008
177.
Jobert L, et al. The human base excision repair enzyme SMUG1 directly interacts with DKC1 and contributes to RNA quality control. Mol. Cell. 2013;49:339-345.
Not in our library10.1016/j.molcel.2012.11.010
178.
Penzo M, Guerrieri AN, Zacchini F, Trere D, Montanaro L. RNA pseudouridylation in physiology and medicine: for better and for worse. Genes (Basel). 2017;8:301.
Not in our library10.3390/genes8110301
179.
Song J, et al. Differential roles of human PUS10 in miRNA processing and tRNA pseudouridylation. Nat. Chem. Biol. 2020;16:160-169.
Not in our library10.1038/s41589-019-0420-5
180.
De Zoysa MD, Yu YT. Posttranscriptional RNA pseudouridylation. Enzymes. 2017;41:151-167.
Not in our library10.1016/bs.enz.2017.02.001
181.
Purchal MK, et al. Pseudouridine synthase 7 is an opportunistic enzyme that binds and modifies substrates with diverse sequences and structures. Proc. Natl. Acad. Sci. USA. 2022;119:e2109708119.
Not in our library10.1073/pnas.2109708119
182.
tRNA Modifications: Impact on Structure and Thermal Adaptation · 2017
No notice
183.
Guzzi N, et al. Pseudouridylation of tRNA-derived fragments steers translational control in stem cells. Cell. 2018;173:1204-1216.e1226.
Not in our library10.1016/j.cell.2018.03.008
184.
Guegueniat J, et al. The human pseudouridine synthase PUS7 recognizes RNA with an extended multi-domain binding surface. Nucleic Acids Res. 2021;49:11810-11822.
Not in our library10.1093/nar/gkab934
185.
Pseudouridine-modified tRNA fragments repress aberrant protein synthesis and predict leukaemic progression in myelodysplastic syndrome · 2022
No notice
186.
McCown PJ, et al. Naturally occurring modified ribonucleosides. Wiley Interdiscip. Rev. RNA. 2020;11:e1595.
Not in our library10.1002/wrna.1595
187.
Leppik M, Liiv A, Remme J. Random pseuoduridylation in vivo reveals critical region of Escherichia coli 23S rRNA for ribosome assembly. Nucleic Acids Res. 2017;45:6098-6108.
Not in our library10.1093/nar/gkx160
188.
Antonicka H, et al. A pseudouridine synthase module is essential for mitochondrial protein synthesis and cell viability. EMBO Rep. 2017;18:28-38.
Not in our library10.15252/embr.201643391
189.
Penzo M, Montanaro L. Turning uridines around: Role of rRNA pseudouridylation in ribosome biogenesis and ribosomal function. Biomolecules. 2018;8:38.
Not in our library10.3390/biom8020038
190.
Rajan KS, et al. Pseudouridines on Trypanosoma brucei spliceosomal small nuclear RNAs and their implication for RNA and protein interactions. Nucleic Acids Res. 2019;47:7633-7647.
Not in our library10.1093/nar/gkz477
191.
Wu G, et al. Pseudouridines in U2 snRNA stimulate the ATPase activity of Prp5 during spliceosome assembly. EMBO J. 2016;35:654-667.
Not in our library10.15252/embj.201593113
192.
Wang Q, et al. The PSI-U1 snRNP interaction regulates male mating behavior in Drosophila. Proc. Natl. Acad. Sci. USA. 2016;113:5269-5274.
Not in our library10.1073/pnas.1600936113
193.
Kariko K, et al. Incorporation of pseudouridine into mRNA yields superior nonimmunogenic vector with increased translational capacity and biological stability. Mol. Ther. 2008;16:1833-1840.
Not in our library10.1038/mt.2008.200
194.
Carlile TM, et al. Pseudouridine profiling reveals regulated mRNA pseudouridylation in yeast and human cells. Nature. 2014;515:143-146.
Not in our library10.1038/nature13802
195.
Martinez NM, et al. Pseudouridine synthases modify human pre-mRNA co-transcriptionally and affect pre-mRNA processing. Mol. Cell. 2022;82:645-659.e649.
Not in our library10.1016/j.molcel.2021.12.023
196.
Kohama Y, et al. Studies on thermophile products. V. Immunosuppressive profile in vitro of Bacillus stearothermophilus component, Fr.5-B. Chem. Pharm. Bull. (Tokyo). 1992;40:3017-3020.
Not in our library10.1248/cpb.40.3017
197.
The Critical Contribution of Pseudouridine to mRNA COVID-19 Vaccines · 2021
No notice
198.
Lee M, Kim B, Kim VN. Emerging roles of RNA modification: m(6)A and U-tail. Cell. 2014;158:980-987.
Not in our library10.1016/j.cell.2014.08.005
199.
Song J, Song J, Mo B, Chen X. Uridylation and adenylation of RNAs. Sci. China Life Sci. 2015;58:1057-1066.
Not in our library10.1007/s11427-015-4954-9
200.
Clamer M, Hofler L, Mikhailova E, Viero G, Bayley H. Detection of 3’-end RNA uridylation with a protein nanopore. ACS Nano. 2014;8:1364-1374.
Not in our library10.1021/nn4050479
201.
Wang J, Yang YN, Piao WL, Jin H. Uridylation: a vital way for cellular RNA surveillance. Yi Chuan. 2022;44:449-465.
Not in our library10.16288/j.yczz.22-094
202.
Zigackova D, Vanacova S. The role of 3’ end uridylation in RNA metabolism and cellular physiology. Philos. Trans. R. Soc. Lond. B Biol. Sci. 2018;373:20180171.
Not in our library10.1098/rstb.2018.0171
203.
Warkocki Z, Liudkovska V, Gewartowska O, Mroczek S, Dziembowski A. Terminal nucleotidyl transferases (TENTs) in mammalian RNA metabolism. Philos. Trans. R. Soc. Lond. B Biol. Sci. 2018;373:20180162.
Not in our library10.1098/rstb.2018.0162
204.
Aphasizhev R, Suematsu T, Zhang L, Aphasizheva I. Constructive edge of uridylation-induced RNA degradation. RNA Biol. 2016;13:1078-1083.
Not in our library10.1080/15476286.2016.1229736
205.
Yu S, Kim VN. A tale of non-canonical tails: gene regulation by post-transcriptional RNA tailing. Nat. Rev. Mol. Cell Biol. 2020;21:542-556.
Not in our library10.1038/s41580-020-0246-8
206.
Yamashita S, Takagi Y, Nagaike T, Tomita K. Crystal structures of U6 snRNA-specific terminal uridylyltransferase. Nat. Commun. 2017;8:15788.
Not in our library10.1038/ncomms15788
207.
Lim J, et al. Uridylation by TUT4 and TUT7 marks mRNA for degradation. Cell. 2014;159:1365-1376.
Not in our library10.1016/j.cell.2014.10.055
208.
Morgan M, et al. mRNA 3’ uridylation and poly(A) tail length sculpt the mammalian maternal transcriptome. Nature. 2017;548:347-351.
Not in our library10.1038/nature23318
209.
Warkocki Z, et al. Uridylation by TUT4/7 Restricts Retrotransposition of Human LINE-1s. Cell. 2018;174:1537-1548.e1529.
Not in our library10.1016/j.cell.2018.07.022
210.
Thornton JE, et al. Selective microRNA uridylation by Zcchc6 (TUT7) and Zcchc11 (TUT4). Nucleic Acids Res. 2014;42:11777-11791.
Not in our library10.1093/nar/gku805
211.
Hoefig KP, Heissmeyer V. Degradation of oligouridylated histone mRNAs: see UUUUU and goodbye. Wiley Interdiscip. Rev. RNA. 2014;5:577-589.
Not in our library10.1002/wrna.1232
212.
Chung CZ, et al. RNA surveillance by uridylation-dependent RNA decay in Schizosaccharomyces pombe. Nucleic Acids Res. 2019;47:3045-3057.
Not in our library10.1093/nar/gkz043
213.
Wolin SL, Cedervall T. The La protein. Annu Rev. Biochem. 2002;71:375-403.
Not in our library10.1146/annurev.biochem.71.090501.150003
214.
Rissland OS, Norbury CJ. Decapping is preceded by 3’ uridylation in a novel pathway of bulk mRNA turnover. Nat. Struct. Mol. Biol. 2009;16:616-623.
Not in our library10.1038/nsmb.1601
215.
Faehnle CR, Walleshauser J, Joshua-Tor L. Mechanism of Dis3l2 substrate recognition in the Lin28-let-7 pathway. Nature. 2014;514:252-256.
Not in our library10.1038/nature13553
216.
Ustianenko D, et al. TUT-DIS3L2 is a mammalian surveillance pathway for aberrant structured non-coding RNAs. EMBO J. 2016;35:2179-2191.
Not in our library10.15252/embj.201694857
217.
De Almeida, C., Scheer, H., Zuber, H. & Gagliardi, D. RNA uridylation: a key posttranscriptional modification shaping the coding and noncoding transcriptome. Wiley Interdiscip Rev RNA. 9, (2018).
Not in our library10.1002/wrna.1440
218.
Yashiro Y, Tomita K. Function and regulation of human terminal uridylyltransferases. Front Genet. 2018;9:538.
Not in our library10.3389/fgene.2018.00538
219.
Menezes MR, Balzeau J, Hagan JP. 3’ RNA uridylation in epitranscriptomics, gene regulation, and disease. Front Mol. Biosci. 2018;5:61.
Not in our library10.3389/fmolb.2018.00061
220.
Kim B, et al. TUT7 controls the fate of precursor microRNAs by using three different uridylation mechanisms. EMBO J. 2015;34:1801-1815.
Not in our library10.15252/embj.201590931
221.
Kim H, et al. A mechanism for microRNA arm switching regulated by uridylation. Mol. Cell. 2020;78:1224-1236.e1225.
Not in our library10.1016/j.molcel.2020.04.030
222.
Heo I, et al. Mono-uridylation of pre-microRNA as a key step in the biogenesis of group II let-7 microRNAs. Cell. 2012;151:521-532.
Not in our library10.1016/j.cell.2012.09.022
223.
Yang A, et al. 3’ Uridylation Confers miRNAs with non-canonical target repertoires. Mol. Cell. 2019;75:511-522.e514.
Not in our library10.1016/j.molcel.2019.05.014
224.
Jones MR, et al. Zcchc11-dependent uridylation of microRNA directs cytokine expression. Nat. Cell Biol. 2009;11:1157-1163.
Not in our library10.1038/ncb1931
225.
Ji L, Chen X. Regulation of small RNA stability: methylation and beyond. Cell Res. 2012;22:624-636.
Not in our library10.1038/cr.2012.36
226.
Gutierrez-Vazquez C, et al. 3’ Uridylation controls mature microRNA turnover during CD4 T-cell activation. RNA. 2017;23:882-891.
Not in our library10.1261/rna.060095.116
227.
Lin CC, et al. Terminal uridyltransferase 7 regulates TLR4-triggered inflammation by controlling Regnase-1 mRNA uridylation and degradation. Nat. Commun. 2021;12:3878.
Not in our library10.1038/s41467-021-24177-7
228.
The TUTase URT1 connects decapping activators and prevents the accumulation of excessively deadenylated mRNAs to avoid siRNA biogenesis · 2021
Not checked
229.
Eberhardt W, Doller A, Akool el S, Pfeilschifter J. Modulation of mRNA stability as a novel therapeutic approach. Pharm. Ther. 2007;114:56-73.
Not in our library10.1016/j.pharmthera.2007.01.002
230.
Le Pen J, et al. Terminal uridylyltransferases target RNA viruses as part of the innate immune system. Nat. Struct. Mol. Biol. 2018;25:778-786.
Not in our library10.1038/s41594-018-0106-9
231.
Felix MA, Wang D. Natural viruses of caenorhabditis nematodes. Annu Rev. Genet. 2019;53:313-326.
Not in our library10.1146/annurev-genet-112618-043756
232.
Frazier MN, et al. Characterization of SARS2 Nsp15 nuclease activity reveals it’s mad about U. Nucleic Acids Res. 2021;49:10136-10149.
Not in our library10.1093/nar/gkab719
233.
Koppers-Lalic D, et al. Nontemplated nucleotide additions distinguish the small RNA composition in cells from exosomes. Cell Rep. 2014;8:1649-1658.
Not in our library10.1016/j.celrep.2014.08.027
234.
Wulff BE, Sakurai M, Nishikura K. Elucidating the inosinome: global approaches to adenosine-to-inosine RNA editing. Nat. Rev. Genet. 2011;12:81-85.
Not in our library10.1038/nrg2915
235.
Li JB, Church GM. Deciphering the functions and regulation of brain-enriched A-to-I RNA editing. Nat. Neurosci. 2013;16:1518-1522.
Not in our library10.1038/nn.3539
236.
Quin J, et al. ADAR RNA Modifications, the Epitranscriptome and Innate Immunity. Trends Biochem Sci. 2021;46:758-771.
Not in our library10.1016/j.tibs.2021.02.002
237.
Ganem NS, Ben-Asher N, Lamm AT. In cancer, A-to-I RNA editing can be the driver, the passenger, or the mechanic. Drug Resist Updat. 2017;32:16-22.
Not in our library10.1016/j.drup.2017.09.001
238.
Liao Y, Jung SH, Kim T. A-to-I RNA editing as a tuner of noncoding RNAs in cancer. Cancer Lett. 2020;494:88-93.
Not in our library10.1016/j.canlet.2020.08.004
239.
Macbeth MR, et al. Inositol hexakisphosphate is bound in the ADAR2 core and required for RNA editing. Science. 2005;309:1534-1539.
Not in our library10.1126/science.1113150
240.
Vlachogiannis NI, Verrou KM, Stellos K, Sfikakis PP, Paraskevis D. The role of A-to-I RNA editing in infections by RNA viruses: Possible implications for SARS-CoV-2 infection. Clin. Immunol. 2021;226:108699.
Not in our library10.1016/j.clim.2021.108699
241.
Nishikura K. A-to-I editing of coding and non-coding RNAs by ADARs. Nat. Rev. Mol. Cell Biol. 2016;17:83-96.
Not in our library10.1038/nrm.2015.4
242.
Baker AR, Slack FJ. ADAR1 and its implications in cancer development and treatment. Trends Genet. 2022;38:821-830.
Not in our library10.1016/j.tig.2022.03.013
243.
Rewriting the transcriptome: adenosine-to-inosine RNA editing by ADARs · 2017
No notice
244.
Maas S, Kim YG, Rich A. Sequence, genomic organization and functional expression of the murine tRNA-specific adenosine deaminase ADAT1. Gene. 2000;243:59-66.
Not in our library10.1016/s0378-1119(99)00562-4
245.
Bertotti S, et al. Characterization of ADAT2/3 molecules in Trypanosoma cruzi and regulation of mucin gene expression by tRNA editing. Biochem J. 2022;479:561-580.
Not in our library10.1042/bcj20210850
246.
Liu X, et al. Crystal structure of the yeast heterodimeric ADAT2/3 deaminase. BMC Biol. 2020;18:189.
Not in our library10.1186/s12915-020-00920-2
247.
Genome-wide A-to-I RNA editing in fungi independent of ADAR enzymes · 2016
No notice
248.
Keegan LP, et al. The properties of a tRNA-specific adenosine deaminase from Drosophila melanogaster support an evolutionary link between pre-mRNA editing and tRNA modification. Mol. Cell Biol. 2000;20:825-833.
Not in our library10.1128/mcb.20.3.825-833.2000
249.
Elbarbary RA, Lucas BA, Maquat LE. Retrotransposons as regulators of gene expression. Science. 2016;351:aac7247.
Not in our library10.1126/science.aac7247
250.
Werry TD, Loiacono R, Sexton PM, Christopoulos A. RNA editing of the serotonin 5HT2C receptor and its effects on cell signalling, pharmacology and brain function. Pharm. Ther. 2008;119:7-23.
Not in our library10.1016/j.pharmthera.2008.03.012
251.
Jain M, Jantsch MF, Licht K. The Editor’s I on disease development. Trends Genet. 2019;35:903-913.
Not in our library10.1016/j.tig.2019.09.004
252.
Gagnidze K, Rayon-Estrada V, Harroch S, Bulloch K, Papavasiliou FN. A new chapter in genetic medicine: RNA editing and its role in disease pathogenesis. Trends Mol. Med. 2018;24:294-303.
Not in our library10.1016/j.molmed.2018.01.002
253.
Zipeto MA, Jiang Q, Melese E, Jamieson CH. RNA rewriting, recoding, and rewiring in human disease. Trends Mol. Med. 2015;21:549-559.
Not in our library10.1016/j.molmed.2015.07.001
254.
Farajollahi S, Maas S. Molecular diversity through RNA editing: a balancing act. Trends Genet. 2010;26:221-230.
Not in our library10.1016/j.tig.2010.02.001
255.
Savva YA, Rieder LE, Reenan RA. The ADAR protein family. Genome Biol. 2012;13:252.
Not in our library10.1186/gb-2012-13-12-252
256.
Tan MH, et al. Dynamic landscape and regulation of RNA editing in mammals. Nature. 2017;550:249-254.
Not in our library10.1038/nature24041
257.
Oakes E, Anderson A, Cohen-Gadol A, Hundley HA. Adenosine deaminase that acts on RNA 3 (ADAR3) binding to glutamate receptor subunit B Pre-mRNA inhibits RNA editing in glioblastoma. J. Biol. Chem. 2017;292:4326-4335.
Not in our library10.1074/jbc.m117.779868
258.
Raghava Kurup R, et al. RNA binding by ADAR3 inhibits adenosine-to-inosine editing and promotes expression of immune response protein MAVS. J. Biol. Chem. 2022;298:102267.
Not in our library10.1016/j.jbc.2022.102267
259.
Teoh PJ, Koh MY, Chng WJ. ADARs, RNA editing and more in hematological malignancies. Leukemia. 2021;35:346-359.
Not in our library10.1038/s41375-020-01076-2
260.
Aquino-Jarquin G. Novel engineered programmable systems for ADAR-mediated RNA editing. Mol. Ther. Nucleic Acids. 2020;19:1065-1072.
Not in our library10.1016/j.omtn.2019.12.042
261.
Yablonovitch AL, Deng P, Jacobson D, Li JB. The evolution and adaptation of A-to-I RNA editing. PLoS Genet. 2017;13:e1007064.
Not in our library10.1371/journal.pgen.1007064
262.
Xu X, Wang Y, Liang H. The role of A-to-I RNA editing in cancer development. Curr. Opin. Genet Dev. 2018;48:51-56.
Not in our library10.1016/j.gde.2017.10.009
263.
Ganem NS, Lamm AT. A-to-I RNA editing - thinking beyond the single nucleotide. RNA Biol. 2017;14:1690-1694.
Not in our library10.1080/15476286.2017.1364830
264.
Han SW, et al. RNA editing in RHOQ promotes invasion potential in colorectal cancer. J. Exp. Med. 2014;211:613-621.
Not in our library10.1084/jem.20132209
265.
Daniel C, Wahlstedt H, Ohlson J, Bjork P, Ohman M. Adenosine-to-inosine RNA editing affects trafficking of the gamma-aminobutyric acid type A (GABA(A)) receptor. J. Biol. Chem. 2011;286:2031-2040.
Not in our library10.1074/jbc.m110.130096
266.
Garrett S, Rosenthal JJ. RNA editing underlies temperature adaptation in K+ channels from polar octopuses. Science. 2012;335:848-851.
Not in our library10.1126/science.1212795
267.
Chen L, et al. Recoding RNA editing of AZIN1 predisposes to hepatocellular carcinoma. Nat. Med. 2013;19:209-216.
Not in our library10.1038/nm.3043
268.
Nakano M, Nakajima M. Significance of A-to-I RNA editing of transcripts modulating pharmacokinetics and pharmacodynamics. Pharm. Ther. 2018;181:13-21.
Not in our library10.1016/j.pharmthera.2017.07.003
269.
Slotkin W, Nishikura K. Adenosine-to-inosine RNA editing and human disease. Genome Med. 2013;5:105.
Not in our library10.1186/gm508
270.
Vlachogiannis NI, et al. Adenosine-to-inosine RNA editing contributes to type I interferon responses in systemic sclerosis. J. Autoimmun. 2021;125:102755.
Not in our library10.1016/j.jaut.2021.102755
271.
Jiang L, et al. ADAR1-mediated RNA editing links ganglioside catabolism to glioblastoma stem cell maintenance. J. Clin. Invest. 2022;132:e143397.
Not in our library10.1172/jci143397
272.
Yang CC, et al. ADAR1-mediated 3’ UTR editing and expression control of antiapoptosis genes fine-tunes cellular apoptosis response. Cell Death Dis. 2017;8:e2833.
Not in our library10.1038/cddis.2017.12
273.
Stellos K, et al. Adenosine-to-inosine RNA editing controls cathepsin S expression in atherosclerosis by enabling HuR-mediated post-transcriptional regulation. Nat. Med. 2016;22:1140-1150.
Not in our library10.1038/nm.4172
274.
Liang H, Landweber LF. Hypothesis: RNA editing of microRNA target sites in humans? RNA. 2007;13:463-467.
Not in our library10.1261/rna.296407
275.
Banerjee A, Vest KE, Pavlath GK, Corbett AH. Nuclear poly(A) binding protein 1 (PABPN1) and Matrin3 interact in muscle cells and regulate RNA processing. Nucleic Acids Res. 2017;45:10706-10725.
Not in our library10.1093/nar/gkx786
276.
Omata Y, et al. RNA editing enzyme ADAR1 governs the circadian expression of P-glycoprotein in human renal cells by regulating alternative splicing of the ABCB1 gene. J. Biol. Chem. 2021;296:100601.
Not in our library10.1016/j.jbc.2021.100601
277.
Cho CJ, Myung SJ, Chang S. ADAR1 and MicroRNA; a hidden crosstalk in cancer. Int. J. Mol. Sci. 2017;18:799.
Not in our library10.3390/ijms18040799
278.
Marceca GP, et al. Detecting and characterizing A-To-I microRNA editing in cancer. Cancers (Basel). 2021;13:1699.
Not in our library10.3390/cancers13071699
279.
Kokot KE, et al. Reduction of A-to-I RNA editing in the failing human heart regulates formation of circular RNAs. Basic Res. Cardiol. 2022;117:32.
Not in our library10.1007/s00395-022-00940-9
280.
Omata Y, et al. RNA editing enzyme ADAR1 controls miR-381-3p-mediated expression of multidrug resistance protein MRP4 via regulation of circRNA in human renal cells. J. Biol. Chem. 2022;298:102184.
Not in our library10.1016/j.jbc.2022.102184
281.
ADARs act as potent regulators of circular transcriptome in cancer · 2022
Not checked
282.
Yang W, et al. Modulation of microRNA processing and expression through RNA editing by ADAR deaminases. Nat. Struct. Mol. Biol. 2006;13:13-21.
Not in our library10.1038/nsmb1041
283.
Kawahara Y, et al. Frequency and fate of microRNA editing in human brain. Nucleic Acids Res. 2008;36:5270-5280.
Not in our library10.1093/nar/gkn479
284.
Zipeto MA, et al. ADAR1 activation drives leukemia stem cell self-renewal by impairing let-7 biogenesis. Cell Stem Cell. 2016;19:177-191.
Not in our library10.1016/j.stem.2016.05.004
285.
Kawahara Y, Zinshteyn B, Chendrimada TP, Shiekhattar R, Nishikura K. RNA editing of the microRNA-151 precursor blocks cleavage by the Dicer-TRBP complex. EMBO Rep. 2007;8:763-769.
Not in our library10.1038/sj.embor.7401011
286.
Kawahara Y, et al. Redirection of silencing targets by adenosine-to-inosine editing of miRNAs. Science. 2007;315:1137-1140.
Not in our library10.1126/science.1138050
287.
Vesely C, et al. ADAR2 induces reproducible changes in sequence and abundance of mature microRNAs in the mouse brain. Nucleic Acids Res. 2014;42:12155-12168.
Not in our library10.1093/nar/gku844
288.
Chen T, et al. ADAR1 is required for differentiation and neural induction by regulating microRNA processing in a catalytically independent manner. Cell Res. 2015;25:459-476.
Not in our library10.1038/cr.2015.24
289.
Ota H, et al. ADAR1 forms a complex with Dicer to promote microRNA processing and RNA-induced gene silencing. Cell. 2013;153:575-589.
Not in our library10.1016/j.cell.2013.03.024
290.
Shoshan E, et al. Reduced adenosine-to-inosine miR-455-5p editing promotes melanoma growth and metastasis. Nat. Cell Biol. 2015;17:311-321.
Not in our library10.1038/ncb3110
291.
Magnaye KM, et al. A-to-I editing of miR-200b-3p in airway cells is associated with moderate-to-severe asthma. Eur. Respir. J. 2021;58:2003862.
Not in our library10.1183/13993003.03862-2020
292.
van der Kwast R, et al. Adenosine-to-inosine editing of MicroRNA-487b alters target gene selection after ischemia and promotes neovascularization. Circ. Res. 2018;122:444-456.
Not in our library10.1161/circresaha.117.312345
293.
Li L, et al. The landscape of miRNA editing in animals and its impact on miRNA biogenesis and targeting. Genome Res. 2018;28:132-143.
Not in our library10.1101/gr.224386.117
294.
Kume H, Hino K, Galipon J, Ui-Tei K. A-to-I editing in the miRNA seed region regulates target mRNA selection and silencing efficiency. Nucleic Acids Res. 2014;42:10050-10060.
Not in our library10.1093/nar/gku662
295.
Mallela A, Nishikura K. A-to-I editing of protein coding and noncoding RNAs. Crit. Rev. Biochem Mol. Biol. 2012;47:493-501.
Not in our library10.3109/10409238.2012.714350
296.
Pasquinelli AE. A rADAR defense against RNAi. Genes Dev. 2018;32:199-201.
Not in our library10.1101/gad.313049.118
297.
Reich DP, Tyc KM, Bass BL. C. elegans ADARs antagonize silencing of cellular dsRNAs by the antiviral RNAi pathway. Genes Dev. 2018;32:271-282.
Not in our library10.1101/gad.310672.117
298.
Vlachogiannis NI, et al. Adenosine-to-inosine Alu RNA editing controls the stability of the pro-inflammatory long noncoding RNA NEAT1 in atherosclerotic cardiovascular disease. J. Mol. Cell Cardiol. 2021;160:111-120.
Not in our library10.1016/j.yjmcc.2021.07.005
299.
Silvestris DA, Scopa C, Hanchi S, Locatelli F, Gallo A. De novo A-to-I RNA editing discovery in lncRNA. Cancers (Basel). 2020;12:2959.
Not in our library10.3390/cancers12102959
300.
Gong J, et al. LNCediting: a database for functional effects of RNA editing in lncRNAs. Nucleic Acids Res. 2017;45:D79-D84.
Not in our library10.1093/nar/gkw835
301.
Di Giorgio S, Martignano F, Torcia MG, Mattiuz G, Conticello SG. Evidence for host-dependent RNA editing in the transcriptome of SARS-CoV-2. Sci. Adv. 2020;6:eabb5813.
Not in our library10.1126/sciadv.abb5813
302.
Gonzales-van Horn SR, Sarnow P. Making the mark: the role of adenosine modifications in the life cycle of RNA viruses. Cell Host Microbe. 2017;21:661-669.
Not in our library10.1016/j.chom.2017.05.008
303.
Wulff BE, Nishikura K. Substitutional A-to-I RNA editing. Wiley Interdiscip. Rev. RNA. 2010;1:90-101.
Not in our library10.1002/wrna.10
304.
Kumar BV, Connors TJ, Farber DL. Human T cell development, localization, and function throughout Life. Immunity. 2018;48:202-213.
Not in our library10.1016/j.immuni.2018.01.007
305.
Gaber T, Chen Y, Krauss PL, Buttgereit F. Metabolism of T lymphocytes in health and disease. Int Rev. Cell Mol. Biol. 2019;342:95-148.
Not in our library10.1016/bs.ircmb.2018.06.002
306.
Wang N, Tang H, Wang X, Wang W, Feng J. Homocysteine upregulates interleukin-17A expression via NSun2-mediated RNA methylation in T lymphocytes. Biochem Biophys. Res Commun. 2017;493:94-99.
Not in our library10.1016/j.bbrc.2017.09.069
307.
Nakahama T, et al. ADAR1-mediated RNA editing is required for thymic self-tolerance and inhibition of autoimmunity. EMBO Rep. 2018;19:e46303.
Not in our library10.15252/embr.201846303
308.
Chung H, Rice CM. T time for ADAR: ADAR1 is required for T cell self-tolerance. EMBO Rep. 2018;19:e47237.
Not in our library10.15252/embr.201847237
309.
Udhayakumar, V. K. et al. Arginine-rich peptide-based mRNA nanocomplexes efficiently instigate cytotoxic T cell immunity dependent on the amphipathic organization of the peptide. Adv Healthc Mater. 6, (2017).
Not in our library10.1002/adhm.201601412
310.
Zhou L, Chong MM, Littman DR. Plasticity of CD4+ T cell lineage differentiation. Immunity. 2009;30:646-655.
Not in our library10.1016/j.immuni.2009.05.001
311.
Zhu J, Paul WE. CD4 T cells: fates, functions, and faults. Blood. 2008;112:1557-1569.
Not in our library10.1182/blood-2008-05-078154
312.
Taniuchi I. CD4 helper and CD8 cytotoxic T cell differentiation. Annu Rev. Immunol. 2018;36:579-601.
Not in our library10.1146/annurev-immunol-042617-053411
313.
Zhu, J., Yamane, H. & Paul, W. E. Differentiation of effector CD4 T cellpopulations (*). Annu Rev. Immunol. 28, 445–489 (2010).
Not in our library10.1146/annurev-immunol-030409-101212
314.
Saravia J, Chapman NM, Chi H. Helper T cell differentiation. Cell Mol. Immunol. 2019;16:634-643.
Not in our library10.1038/s41423-019-0220-6
315.
Zhou J, et al. m(6)A demethylase ALKBH5 controls CD4(+) T cell pathogenicity and promotes autoimmunity. Sci. Adv. 2021;7:eabg0470.
Not in our library10.1126/sciadv.abg0470
316.
Lichinchi G, et al. Dynamics of the human and viral m(6)A RNA methylomes during HIV-1 infection of T cells. Nat. Microbiol. 2016;1:16011.
Not in our library10.1038/nmicrobiol.2016.11
317.
Kong W, et al. Nucleolar protein NOP2/NSUN1 suppresses HIV-1 transcription and promotes viral latency by competing with Tat for TAR binding and methylation. PLoS Pathog. 2020;16:e1008430.
Not in our library10.1371/journal.ppat.1008430
318.
Guo G, et al. Disease activity-associated alteration of mRNA m(5) C methylation in CD4(+) T cells of systemic lupus erythematosus. Front Cell Dev. Biol. 2020;8:430.
Not in our library10.3389/fcell.2020.00430
319.
Guo G, et al. Epitranscriptomic N4-acetylcytidine profiling in CD4(+) T cells of systemic lupus erythematosus. Front Cell Dev. Biol. 2020;8:842.
Not in our library10.3389/fcell.2020.00842
320.
Ruterbusch M, Pruner KB, Shehata L, Pepper M. In vivo CD4(+) T cell differentiation and function: revisiting the Th1/Th2 paradigm. Annu Rev. Immunol. 2020;38:705-725.
Not in our library10.1146/annurev-immunol-103019-085803
321.
Romagnani S. Th1/Th2 cells. Inflamm. Bowel Dis. 1999;5:285-294.
Not in our library10.1097/00054725-199911000-00009
322.
Romagnani S. T-cell subsets (Th1 versus Th2). Ann. Allergy Asthma Immunol. 2000;85:9-18.
Not in our library10.1016/s1081-1206(10)62426-x
323.
Dai B, et al. Significance of RNA N6-Methyladenosine Regulators in the Diagnosis and Subtype Classification of Childhood Asthma Using the Gene Expression Omnibus Database. Front Genet. 2021;12:634162.
Not in our library10.3389/fgene.2021.634162
324.
Yasuda K, Takeuchi Y, Hirota K. The pathogenicity of Th17 cells in autoimmune diseases. Semin Immunopathol. 2019;41:283-297.
Not in our library10.1007/s00281-019-00733-8
325.
Korn T, Bettelli E, Oukka M, Kuchroo VK. IL-17 and Th17 Cells. Annu Rev. Immunol. 2009;27:485-517.
Not in our library10.1146/annurev.immunol.021908.132710
326.
Knochelmann HM, et al. When worlds collide: Th17 and Treg cells in cancer and autoimmunity. Cell Mol. Immunol. 2018;15:458-469.
Not in our library10.1038/s41423-018-0004-4
327.
Cao Y, et al. Enterotoxigenic bacteroidesfragilis promotes intestinal inflammation and malignancy by inhibiting exosome-packaged miR-149-3p. Gastroenterology. 2021;161:1552-1566.e1512.
Not in our library10.1053/j.gastro.2021.08.003
328.
Crotty ST. Follicular helper cell biology: a decade of discovery and diseases. Immunity. 2019;50:1132-1148.
Not in our library10.1016/j.immuni.2019.04.011
329.
Varricchi G, et al. T follicular helper (Tfh) cells in normal immune responses and in allergic disorders. Allergy. 2016;71:1086-1094.
Not in our library10.1111/all.12878
330.
Crotty S. T follicular helper cell differentiation, function, and roles in disease. Immunity. 2014;41:529-542.
Not in our library10.1016/j.immuni.2014.10.004
331.
Zhu Y, et al. The E3 ligase VHL promotes follicular helper T cell differentiation via glycolytic-epigenetic control. J. Exp. Med. 2019;216:1664-1681.
Not in our library10.1084/jem.20190337
332.
METTL3-dependent m6A modification programs T follicular helper cell differentiation · 2021
No notice
333.
Transcriptional and epigenetic basis of Treg cell development and function: its genetic anomalies or variations in autoimmune diseases · 2020
No notice
334.
Goschl L, Scheinecker C, Bonelli M. Treg cells in autoimmunity: from identification to Treg-based therapies. Semin Immunopathol. 2019;41:301-314.
Not in our library10.1007/s00281-019-00741-8
335.
Scheinecker C, Goschl L, Bonelli M. Treg cells in health and autoimmune diseases: New insights from single cell analysis. J. Autoimmun. 2020;110:102376.
Not in our library10.1016/j.jaut.2019.102376
336.
A New Model of Spontaneous Colitis in Mice Induced by Deletion of an RNA m6A Methyltransferase Component METTL14 in T Cells · 2020
No notice
337.
Tong J, et al. m(6)A mRNA methylation sustains Treg suppressive functions. Cell Res. 2018;28:253-256.
Not in our library10.1038/cr.2018.7
338.
Henning AN, Roychoudhuri R, Restifo NP. Epigenetic control of CD8(+) T cell differentiation. Nat. Rev. Immunol. 2018;18:340-356.
Not in our library10.1038/nri.2017.146
339.
Cytotoxic CD8+ T cells in cancer and cancer immunotherapy · 2020
No notice
340.
Reading JL, et al. The function and dysfunction of memory CD8(+) T cells in tumor immunity. Immunol. Rev. 2018;283:194-212.
Not in our library10.1111/imr.12657
341.
Zhang N, Bevan MJ. CD8(+) T cells: foot soldiers of the immune system. Immunity. 2011;35:161-168.
Not in our library10.1016/j.immuni.2011.07.010
342.
Tsuchiya K, et al. YTHDF1 and YTHDF2 are associated with better patient survival and an inflamed tumor-immune microenvironment in non-small-cell lung cancer. Oncoimmunology. 2021;10:1962656.
Not in our library10.1080/2162402x.2021.1962656
343.
He X, Tan L, Ni J, Shen G. Expression pattern of m(6)A regulators is significantly correlated with malignancy and antitumor immune response of breast cancer. Cancer Gene Ther. 2021;28:188-196.
Not in our library10.1038/s41417-020-00208-1
344.
Wang L, et al. m(6) A RNA methyltransferases METTL3/14 regulate immune responses to anti-PD-1 therapy. EMBO J. 2020;39:e104514.
Not in our library10.15252/embj.2020104514
345.
N6-methyladenosine-modified circIGF2BP3 inhibits CD8+ T-cell responses to facilitate tumor immune evasion by promoting the deubiquitination of PD-L1 in non-small cell lung cancer · 2021
No notice
346.
Han D, et al. Anti-tumour immunity controlled through mRNA m(6)A methylation and YTHDF1 in dendritic cells. Nature. 2019;566:270-274.
Not in our library10.1038/s41586-019-0916-x
347.
Liu Y, et al. Tumors exploit FTO-mediated regulation of glycolytic metabolism to evade immune surveillance. Cell Metab. 2021;33:1221-1233.e1211.
Not in our library10.1016/j.cmet.2021.04.001
348.
Integrated analyses of m1A regulator-mediated modification patterns in tumor microenvironment-infiltrating immune cells in colon cancer · 2021
Not checked
349.
Adamo L, Rocha-Resende C, Mann DL. The emerging role of B lymphocytes in cardiovascular disease. Annu Rev. Immunol. 2020;38:99-121.
Not in our library10.1146/annurev-immunol-042617-053104
350.
LeBien TW, Tedder TF. B lymphocytes: how they develop and function. Blood. 2008;112:1570-1580.
Not in our library10.1182/blood-2008-02-078071
351.
Viau M, Zouali M. B-lymphocytes, innate immunity, and autoimmunity. Clin. Immunol. 2005;114:17-26.
Not in our library10.1016/j.clim.2004.08.019
352.
Lee DSW, Rojas OL, Gommerman JL. B cell depletion therapies in autoimmune disease: advances and mechanistic insights. Nat. Rev. Drug Disco. 2021;20:179-199.
Not in our library10.1038/s41573-020-00092-2
353.
Cancro MP, Tomayko MM. Memory B cells and plasma cells: The differentiative continuum of humoral immunity. Immunol. Rev. 2021;303:72-82.
Not in our library10.1111/imr.13016
354.
Ripperger TJ, Bhattacharya D. Transcriptional and metabolic control of memory b cells and plasma cells. Annu Rev. Immunol. 2021;39:345-368.
Not in our library10.1146/annurev-immunol-093019-125603
355.
Zheng Z, et al. Control of early B cell development by the RNA N(6)-methyladenosine methylation. Cell Rep. 2020;31:107819.
Not in our library10.1016/j.celrep.2020.107819
356.
Nair L, et al. Mechanism of noncoding RNA-associated N(6)-methyladenosine recognition by an RNA processing complex during IgH DNA recombination. Mol. Cell. 2021;81:3949-3964.e3947.
Not in our library10.1016/j.molcel.2021.07.037
357.
Xu A, et al. FTO promotes multiple myeloma progression by posttranscriptional activation of HSF1 in an m(6)A-YTHDF2-dependent manner. Mol. Ther. 2022;30:1104-1118.
Not in our library10.1016/j.ymthe.2021.12.012
358.
Marcu-Malina V, et al. ADAR1 is vital for B cell lineage development in the mouse bone marrow. Oncotarget. 2016;7:54370-54379.
Not in our library10.18632/oncotarget.11029
359.
Nutt SL, Chopin M. Transcriptional Networks Driving Dendritic Cell Differentiation and Function. Immunity. 2020;52:942-956.
Not in our library10.1016/j.immuni.2020.05.005
360.
Eisenbarth SC. Dendritic cell subsets in T cell programming: location dictates function. Nat. Rev. Immunol. 2019;19:89-103.
Not in our library10.1038/s41577-018-0088-1
361.
Dendritic Cells and Their Role in Immunotherapy · 2020
No notice
362.
Gardner A, Ruffell B. Dendritic cells and cancer immunity. Trends Immunol. 2016;37:855-865.
Not in our library10.1016/j.it.2016.09.006
363.
Shen S, et al. N6-methyladenosine (m6A)-mediated messenger RNA signatures and the tumor immune microenvironment can predict the prognosis of hepatocellular carcinoma. Ann. Transl. Med. 2021;9:59.
Not in our library10.21037/atm-20-7396
364.
Chen Y, Lei J, He S. m(6)A modification mediates mucosal immune microenvironment and therapeutic response in inflammatory bowel disease. Front Cell Dev. Biol. 2021;9:692160.
Not in our library10.3389/fcell.2021.692160
365.
Mettl3-mediated mRNA m6A methylation promotes dendritic cell activation · 2019
No notice
366.
Baal N, et al. ADAR1 is required for dendritic cell subset homeostasis and alveolar macrophage function. J. Immunol. 2019;202:1099-1111.
Not in our library10.4049/jimmunol.1800269
367.
Myers JA, Miller JS. Exploring the NK cell platform for cancer immunotherapy. Nat. Rev. Clin. Oncol. 2021;18:85-100.
Not in our library10.1038/s41571-020-0426-7
368.
Bjorkstrom NK, Strunz B, Ljunggren HG. Natural killer cells in antiviral immunity. Nat. Rev. Immunol. 2022;22:112-123.
Not in our library10.1038/s41577-021-00558-3
369.
Natural killer cells in cancer biology and therapy · 2020
No notice
370.
Caligiuri MA. Human natural killer cells. Blood. 2008;112:461-469.
Not in our library10.1182/blood-2007-09-077438
371.
METTL3-mediated m6A RNA methylation promotes the anti-tumour immunity of natural killer cells · 2021
No notice
372.
Ma S, et al. The RNA m6A reader YTHDF2 controls NK cell antitumor and antiviral immunity. J. Exp. Med. 2021;218:e20210279.
Not in our library10.1084/jem.20210279
373.
Germic N, Frangez Z, Yousefi S, Simon HU. Regulation of the innate immune system by autophagy: monocytes, macrophages, dendritic cells and antigen presentation. Cell Death Differ. 2019;26:715-727.
Not in our library10.1038/s41418-019-0297-6
374.
Chen S, et al. N6-methyladenosine modification of HIV-1 RNA suppresses type-I interferon induction in differentiated monocytic cells and primary macrophages. PLoS Pathog. 2021;17:e1009421.
Not in our library10.1371/journal.ppat.1009421
375.
Hume DA, Irvine KM, Pridans C. The mononuclear phagocyte system: the relationship between monocytes and macrophages. Trends Immunol. 2019;40:98-112.
Not in our library10.1016/j.it.2018.11.007
376.
Merad M, Martin JC. Pathological inflammation in patients with COVID-19: a key role for monocytes and macrophages. Nat. Rev. Immunol. 2020;20:355-362.
Not in our library10.1038/s41577-020-0331-4
377.
Chanput W, Mes JJ, Wichers HJ. THP-1 cell line: an in vitro cell model for immune modulation approach. Int Immunopharmacol. 2014;23:37-45.
Not in our library10.1016/j.intimp.2014.08.002
378.
Khatua S, Simal-Gandara J, Acharya K. Understanding immune-modulatory efficacy in vitro. Chem. Biol. Interact. 2022;352:109776.
Not in our library10.1016/j.cbi.2021.109776
379.
N6-methyladenosine RNA modification suppresses antiviral innate sensing pathways via reshaping double-stranded RNA · 2021
No notice
380.
Liu Y, et al. N (6)-methyladenosine RNA modification-mediated cellular metabolism rewiring inhibits viral replication. Science. 2019;365:1171-1176.
Not in our library10.1126/science.aax4468
381.
Zhang Y, et al. RNA-binding protein YTHDF3 suppresses interferon-dependent antiviral responses by promoting FOXO3 translation. Proc. Natl. Acad. Sci. USA. 2019;116:976-981.
Not in our library10.1073/pnas.1812536116
382.
Zheng Q, Hou J, Zhou Y, Li Z, Cao X. The RNA helicase DDX46 inhibits innate immunity by entrapping m(6)A-demethylated antiviral transcripts in the nucleus. Nat. Immunol. 2017;18:1094-1103.
Not in our library10.1038/ni.3830
383.
Bannister S, et al. Neonatal BCG vaccination is associated with a long-term DNA methylation signature in circulating monocytes. Sci. Adv. 2022;8:eabn4002.
Not in our library10.1126/sciadv.abn4002
384.
Zhang X, Li X, Jia H, An G, Ni J. The m(6)A methyltransferase METTL3 modifies PGC-1alpha mRNA promoting mitochondrial dysfunction and oxLDL-induced inflammation in monocytes. J. Biol. Chem. 2021;297:101058.
Not in our library10.1016/j.jbc.2021.101058
385.
Xie J, et al. Elevated N6-methyladenosine RNA levels in peripheral blood immune cells: a novel predictive biomarker and therapeutic target for colorectal cancer. Front Immunol. 2021;12:760747.
Not in our library10.3389/fimmu.2021.760747
386.
Tong J, et al. Pooled CRISPR screening identifies m(6)A as a positive regulator of macrophage activation. Sci. Adv. 2021;7:eabd4742.
Not in our library10.1126/sciadv.abd4742
387.
Du J, et al. N(6)-adenosine methylation of Socs1 mRNA is required to sustain the negative feedback control of macrophage activation. Dev. Cell. 2020;55:737-753.
Not in our library10.1016/j.devcel.2020.10.023
388.
m6A Reader YTHDF2 Regulates LPS-Induced Inflammatory Response · 2019
No notice
389.
The METTL3/MALAT1/PTBP1/USP8/TAK1 axis promotes pyroptosis and M1 polarization of macrophages and contributes to liver fibrosis · 2021
No notice
390.
Li J, et al. ADAR1 attenuates allogeneic graft rejection by suppressing miR-21 biogenesis in macrophages and promoting M2 polarization. FASEB J. 2018;32:5162-5173.
Not in our library10.1096/fj.201701449r
391.
Geering B, Stoeckle C, Conus S, Simon HU. Living and dying for inflammation: neutrophils, eosinophils, basophils. Trends Immunol. 2013;34:398-409.
Not in our library10.1016/j.it.2013.04.002
392.
Duffin R, Leitch AE, Fox S, Haslett C, Rossi AG. Targeting granulocyte apoptosis: mechanisms, models, and therapies. Immunol. Rev. 2010;236:28-40.
Not in our library10.1111/j.1600-065x.2010.00922.x
393.
Zeng H, et al. Construction and analysis of a colorectal cancer prognostic model based on N6-methyladenosine-related lncRNAs. Front Cell Dev. Biol. 2021;9:698388.
Not in our library10.3389/fcell.2021.698388
394.
Gong PJ, et al. Analysis of N6-methyladenosine methyltransferase reveals METTL14 and ZC3H13 as tumor suppressor genes in breast cancer. Front Oncol. 2020;10:578963.
Not in our library10.3389/fonc.2020.578963
395.
He Z, et al. PSMC5 promotes proliferation and metastasis of colorectal cancer by activating epithelial-mesenchymal transition signaling and modulating immune infiltrating cells. Front Cell Dev. Biol. 2021;9:657917.
Not in our library10.3389/fcell.2021.657917
396.
Zhernakova A, van Diemen CC, Wijmenga C. Detecting shared pathogenesis from the shared genetics of immune-related diseases. Nat. Rev. Genet. 2009;10:43-55.
Not in our library10.1038/nrg2489
397.
A physical wiring diagram for the human immune system · 2022
Corrected
398.
Mapping the developing human immune system across organs · 2022
No notice
399.
Roy P, Orecchioni M, Ley K. How the immune system shapes atherosclerosis: roles of innate and adaptive immunity. Nat. Rev. Immunol. 2022;22:251-265.
Not in our library10.1038/s41577-021-00584-1
400.
Jacquelot N, Seillet C, Vivier E, Belz GT. Innate lymphoid cells and cancer. Nat. Immunol. 2022;23:371-379.
Not in our library10.1038/s41590-022-01127-z
401.
Blander JM, Longman RS, Iliev ID, Sonnenberg GF, Artis D. Regulation of inflammation by microbiota interactions with the host. Nat. Immunol. 2017;18:851-860.
Not in our library10.1038/ni.3780
402.
Sogkas G, et al. Cellular and molecular mechanisms breaking immune tolerance in inborn errors of immunity. Cell Mol. Immunol. 2021;18:1122-1140.
Not in our library10.1038/s41423-020-00626-z
403.
Kalaora S, Nagler A, Wargo JA, Samuels Y. Mechanisms of immune activation and regulation: lessons from melanoma. Nat. Rev. Cancer. 2022;22:195-207.
Not in our library10.1038/s41568-022-00442-9
404.
Johnson DB, Nebhan CA, Moslehi JJ, Balko JM. Immune-checkpoint inhibitors: long-term implications of toxicity. Nat. Rev. Clin. Oncol. 2022;19:254-267.
Not in our library10.1038/s41571-022-00600-w
405.
Sullivan RJ, Weber JS. Immune-related toxicities of checkpoint inhibitors: mechanisms and mitigation strategies. Nat. Rev. Drug Disco. 2022;21:495-508.
Not in our library10.1038/s41573-021-00259-5
406.
Immunosuppressive cells in cancer: mechanisms and potential therapeutic targets · 2022
No notice
407.
Liu J, Peng Y, Wei W. Cell cycle on the crossroad of tumorigenesis and cancer therapy. Trends Cell Biol. 2022;32:30-44.
Not in our library10.1016/j.tcb.2021.07.001
408.
Gu Y, et al. The evolving landscape of N(6)-methyladenosine modification in the tumor microenvironment. Mol. Ther. 2021;29:1703-1715.
Not in our library10.1016/j.ymthe.2021.04.009
409.
Targeting the RNA m6A modification for cancer immunotherapy · 2022
No notice
410.
Natua S, Dhamdhere SG, Mutnuru SA, Shukla S. Interplay within tumor microenvironment orchestrates neoplastic RNA metabolism and transcriptome diversity. Wiley Interdiscip. Rev. RNA. 2022;13:e1676.
Not in our library10.1002/wrna.1676
411.
Li M, Zha X, Wang S. The role of N6-methyladenosine mRNA in the tumor microenvironment. Biochim Biophys. Acta Rev. Cancer. 2021;1875:188522.
Not in our library10.1016/j.bbcan.2021.188522
412.
The m6A/m5C/m1A Regulated Gene Signature Predicts the Prognosis and Correlates With the Immune Status of Hepatocellular Carcinoma · 2022
Not checked
413.
Yu G, et al. Comprehensive analysis of m5C methylation regulatory genes and tumor microenvironment in prostate cancer. Front Immunol. 2022;13:914577.
Not in our library10.3389/fimmu.2022.914577
414.
Liu J, et al. Comprehensive of N1-methyladenosine modifications patterns and immunological characteristics in ovarian cancer. Front Immunol. 2021;12:746647.
Not in our library10.3389/fimmu.2021.746647
415.
Dong K, et al. Identification and verification of m(7)G modification patterns and characterization of tumor microenvironment infiltration via multi-omics analysis in clear cell renal cell carcinoma. Front Immunol. 2022;13:874792.
Not in our library10.3389/fimmu.2022.874792
416.
Prognostic and Immunological Role of mRNA ac4C Regulator NAT10 in Pan-Cancer: New Territory for Cancer Research? · 2021
Not checked
417.
Zhang M, et al. H/ACA snoRNP gene family as diagnostic and prognostic biomarkers for hepatocellular carcinoma. Pharmgenomics Pers. Med. 2021;14:1331-1345.
Not in our library10.2147/pgpm.s333838
418.
Li B, et al. Surmounting cancer drug resistance: New insights from the perspective of N(6)-methyladenosine RNA modification. Drug Resist Updat. 2020;53:100720.
Not in our library10.1016/j.drup.2020.100720
419.
Zhang F, et al. Crosstalk among m(6)A RNA methylation, hypoxia and metabolic reprogramming in TME: from immunosuppressive microenvironment to clinical application. J. Hematol. Oncol. 2022;15:84.
Not in our library10.1186/s13045-022-01304-5
420.
Jia J, et al. Novel insights into m(6)A modification of coding and non-coding RNAs in tumor biology: From molecular mechanisms to therapeutic significance. Int J. Biol. Sci. 2022;18:4432-4451.
Not in our library10.7150/ijbs.73093
421.
RNA m6A methylation orchestrates cancer growth and metastasis via macrophage reprogramming · 2021
No notice
422.
LncRNA-PACERR induces pro-tumour macrophages via interacting with miR-671-3p and m6A-reader IGF2BP2 in pancreatic ductal adenocarcinoma · 2022
No notice
423.
Dong L, et al. The loss of RNA N(6)-adenosine methyltransferase Mettl14 in tumor-associated macrophages promotes CD8(+) T cell dysfunction and tumor growth. Cancer Cell. 2021;39:945-957.e910.
Not in our library10.1016/j.ccell.2021.04.016
424.
Wykes MN, Lewin SR. Immune checkpoint blockade in infectious diseases. Nat. Rev. Immunol. 2018;18:91-104.
Not in our library10.1038/nri.2017.112
425.
Galluzzi L, Buque A, Kepp O, Zitvogel L, Kroemer G. Immunogenic cell death in cancer and infectious disease. Nat. Rev. Immunol. 2017;17:97-111.
Not in our library10.1038/nri.2016.107
426.
McBride AA. Human papillomaviruses: diversity, infection and host interactions. Nat. Rev. Microbiol. 2022;20:95-108.
Not in our library10.1038/s41579-021-00617-5
427.
Mohammadi M, Akhoundi M, Malih S, Mohammadi A, Sheykhhasan M. Therapeutic roles of CAR T cells in infectious diseases: Clinical lessons learnt from cancer. Rev. Med Virol. 2022;32:e2325.
Not in our library10.1002/rmv.2325
428.
Tan, B. & Gao, S. J. RNA epitranscriptomics: Regulation of infectionof RNA and DNA viruses by N(6) -methyladenosine (m(6) A. Rev. Med. Virol28, e1983 (2018).
Not in our library10.1002/rmv.1983
429.
Yu PL, Cao SJ, Wu R, Zhao Q, Yan QG. Regulatory effect of m(6) A modification on different viruses. J. Med. Virol. 2021;93:6100-6115.
Not in our library10.1002/jmv.27246
430.
McFadden MJ, Horner SM. N(6)-methyladenosine regulates host responses to viral infection. Trends Biochem Sci. 2021;46:366-377.
Not in our library10.1016/j.tibs.2020.11.008
431.
Thompson MG, Sacco MT, Horner SM. How RNA modifications regulate the antiviral response. Immunol. Rev. 2021;304:169-180.
Not in our library10.1111/imr.13020
432.
Williams GD, Gokhale NS, Horner SM. Regulation of viral infection by the RNA modification N6-methyladenosine. Annu Rev. Virol. 2019;6:235-253.
Not in our library10.1146/annurev-virology-092818-015559
433.
Kostyusheva A, Brezgin S, Glebe D, Kostyushev D, Chulanov V. Host-cell interactions in HBV infection and pathogenesis: the emerging role of m6A modification. Emerg. Microbes Infect. 2021;10:2264-2275.
Not in our library10.1080/22221751.2021.2006580
434.
Wang L, Wen M, Cao X. Nuclear hnRNPA2B1 initiates and amplifies the innate immune response to DNA viruses. Science. 2019;365:eaav0758.
Not in our library10.1126/science.aav0758
435.
Crooke PS, Tossberg JT, Porter KP, Aune TM. Reduced A-to-I editing of endogenous Alu RNAs in lung after SARS-CoV-2 infection. Curr. Res Immunol. 2021;2:52-59.
Not in our library10.1016/j.crimmu.2021.04.001
436.
Extensive editing of cellular and viral double-stranded RNA structures accounts for innate immunity suppression and the proviral activity of ADAR1p150. · 2018
Not checked
437.
Yuan Y, et al. Therapeutic potential of interleukin-2 in autoimmune diseases. Trends Mol. Med. 2022;28:596-612.
Not in our library10.1016/j.molmed.2022.04.010
438.
Krovi SH, Kuchroo VK. Activation pathways that drive CD4(+) T cells to break tolerance in autoimmune diseases(). Immunol. Rev. 2022;307:161-190.
Not in our library10.1111/imr.13071
439.
Brannon, E. R. et al. Polymeric particle-based therapies for acute inflammatory diseases. Nat Rev Mater. 1–18 (2022).
Not in our library10.1038/s41578-022-00458-5
440.
Efferth T, Oesch F. The immunosuppressive activity of artemisinin-type drugs towards inflammatory and autoimmune diseases. Med. Res. Rev. 2021;41:3023-3061.
Not in our library10.1002/med.21842
441.
Damsky W, et al. The emerging role of Janus kinase inhibitors in the treatment of autoimmune and inflammatory diseases. J. Allergy Clin. Immunol. 2021;147:814-826.
Not in our library10.1016/j.jaci.2020.10.022
442.
Papotto PH, Reinhardt A, Prinz I, Silva-Santos B. Innately versatile: gammadelta17 T cells in inflammatory and autoimmune diseases. J. Autoimmun. 2018;87:26-37.
Not in our library10.1016/j.jaut.2017.11.006
443.
The m6A Reader IGF2BP2 Regulates Macrophage Phenotypic Activation and Inflammatory Diseases by Stabilizing TSC1 and PPAR γ · 2021
No notice
444.
Laxminarayana D, Khan IU, Kammer G. Transcript mutations of the alpha regulatory subunit of protein kinase A and up-regulation of the RNA-editing gene transcript in lupus T lymphocytes. Lancet. 2002;360:842-849.
Not in our library10.1016/s0140-6736(02)09966-x
445.
Increased RNA Editing May Provide a Source for Autoantigens in Systemic Lupus Erythematosus · 2018
Not checked
446.
Li Q, et al. RNA editing underlies genetic risk of common inflammatory diseases. Nature. 2022;608:569-577.
Not in our library10.1038/s41586-022-05052-x
447.
Liu J, et al. CCR7 chemokine receptor-inducible lnc-Dpf3 restrains dendritic cell migration by inhibiting HIF-1alpha-mediated glycolysis. Immunity. 2019;50:600-615.e615.
Not in our library10.1016/j.immuni.2019.01.021
448.
Kaul A, et al. Systemic lupus erythematosus. Nat. Rev. Dis. Prim. 2016;2:16039.
Not in our library10.1038/nrdp.2016.39
449.
Attfield, K. E., Jensen, L. T., Kaufmann, M., Friese, M. A. & Fugger, L. The immunology of multiple sclerosis. Nat Rev Immunol. (2022).
Not in our library10.1038/s41577-022-00718-z
450.
Van der Jeught K, et al. Dendritic cell targeting mRNA lipopolyplexes combine strong antitumor T-cell immunity with improved inflammatory safety. ACS Nano. 2018;12:9815-9829.
Not in our library10.1021/acsnano.8b00966
451.
Krienke C, et al. A noninflammatory mRNA vaccine for treatment of experimental autoimmune encephalomyelitis. Science. 2021;371:145-153.
Not in our library10.1126/science.aay3638
452.
Lee JH, et al. Enhancer RNA m6A methylation facilitates transcriptional condensate formation and gene activation. Mol. Cell. 2021;81:3368-3385.e3369.
Not in our library10.1016/j.molcel.2021.07.024
453.
The RNA Methyltransferase NSUN2 and Its Potential Roles in Cancer · 2020
No notice
454.
Aberrant NSUN2-mediated m5C modification of H19 lncRNA is associated with poor differentiation of hepatocellular carcinoma · 2020
No notice
455.
Letoquart J, et al. Structural and functional studies of Bud23-Trm112 reveal 18S rRNA N7-G1575 methylation occurs on late 40S precursor ribosomes. Proc. Natl. Acad. Sci. USA. 2014;111:E5518-E5526.
Not in our library10.1073/pnas.1413089111
456.
Boon KL, Pearson MD, Kos M. Self-association of Trimethylguanosine Synthase Tgs1 is required for efficient snRNA/snoRNA trimethylation and pre-rRNA processing. Sci. Rep. 2015;5:11282.
Not in our library10.1038/srep11282
457.
Peculis BA, Reynolds K, Cleland M. Metal determines efficiency and substrate specificity of the nuclear NUDIX decapping proteins X29 and H29K (Nudt16). J. Biol. Chem. 2007;282:24792-24805.
Not in our library10.1074/jbc.m704179200
458.
Aphasizhev R, Aphasizheva I, Simpson L. A tale of two TUTases. Proc. Natl. Acad. Sci. USA. 2003;100:10617-10622.
Not in our library10.1073/pnas.1833120100
459.
Pfaller CK, George CX, Samuel CE. Adenosine deaminases acting on RNA (ADARs) and viral infections. Annu Rev. Virol. 2021;8:239-264.
Not in our library10.1146/annurev-virology-091919-065320
460.
Cesarini V, et al. ADAR2/miR-589-3p axis controls glioblastoma cell migration/invasion. Nucleic Acids Res. 2018;46:2045-2059.
Not in our library10.1093/nar/gkx1257
461.
Figueroa T, Boumart I, Coupeau D, Rasschaert D. Hyperediting by ADAR1 of a new herpesvirus lncRNA during the lytic phase of the oncogenic Marek’s disease virus. J. Gen. Virol. 2016;97:2973-2988.
Not in our library10.1099/jgv.0.000606
462.
Song C, Sakurai M, Shiromoto Y, Nishikura K. Functions of the RNA editing enzyme ADAR1 and their relevance to human diseases. Genes (Basel). 2016;7:129.
Not in our library10.3390/genes7120129
463.
Ringlander J, et al. Impact of ADAR-induced editing of minor viral RNA populations on replication and transmission of SARS-CoV-2. Proc. Natl. Acad. Sci. USA. 2022;119:e2112663119.
Not in our library10.1073/pnas.2112663119
464.
He J, et al. METTL3 restrains papillary thyroid cancer progression via m(6)A/c-Rel/IL-8-mediated neutrophil infiltration. Mol. Ther. 2021;29:1821-1837.
Not in our library10.1016/j.ymthe.2021.01.019

Cited by papers we hold 2

The role of RNA methylation in tumor immunity and its potential in immunotherapy · 2024
No notice
RNA modifications in cellular metabolism: implications for metabolism-targeted therapy and immunotherapy · 2024
No notice

Reads

Read by people on this page

None yet.

Checked or read by AI through naulon

None yet.

A person counts once a day per paper. We keep no cookie and no address: a reader is a hash that changes every day. Any month under five reads shows no number.

Are you an author?

Is this your paper?

Claim it to add your note and be paid when agents cite it. Free.