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The KCTD family of proteins: structure, function, disease relevance

Zhepeng Liu, Yaqian Xiang, Guihong Sun

Cell & Bioscience · 2013 · Review

doi:10.1186/2045-3701-3-45

Abstract

The family of potassium channel tetramerizationdomain (KCTD) proteins consists of 26 members with mostly unknown functions. The name of the protein family is due to the sequence similarity between the conserved N-terminal region of KCTD proteins and the tetramerization domain in some voltage-gated potassium channels. Dozens of publications suggest that KCTD proteins have roles in various biological processes and diseases. In this review, we summarize the character of Bric-a-brack,Tram-track, Broad complex(BTB) of KCTD proteins, their roles in the ubiquitination pathway, and the roles of KCTD mutants in diseases. Furthermore, we review potential downstream signaling pathways and discuss future studies that should be performed.

Full text

From PubMed Central, U.S. National Library of Medicine, as current on Oct 26, 2026. Paragraph numbers are ours, so an answer can point at one.

Introduction

1The human potassium (K+) channel tetramerization domain (KCTD)family of proteins consists of 26 members that share sequence similarity with the cytoplasmic domain of voltage-gated K+ channels(Kv channels). The KCTD proteins have relatively conserved N-terminal domains and variable C-termini. Comparative analyses of the conserved N-terminal sequence suggest the presence of a common Bric-a-brack,Tram-track, Broad complex (BTB) domain, which is also known as the POZ domain. The BTB domain is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. A variety of functions have been identified for the BTB domain-containing KCTD proteins. These functions include transcriptional repression, cytoskeleton regulation, tetramerization and gating of ion channels, and interaction with the cullin E3 (Cul3) ubiquitin ligase complex. In this review, we will summarize the homology between KCTD family members and some of the key features of KCTD proteins. We will also discuss the roles of mutant KCTDs in disease.

BTB domain and homology between KCTD family members

2The human genome includes approximately 400 BTB domain-containing proteins. The BTB domain is a highly conserved motif of about 100 amino acids and can be found at the N-terminusof C2H2-type zinc-finger transcription factors and in some actin-binding proteins. BTB domain-containing proteins include transcription factors, oncogenic proteins, ion channel proteins, and KCTD proteins. Many BTB domain-containing proteins contain one or two additional domains, such as kelch repeats, zinc-finger domains, FYVE (Fab1, YOTB, Vac1, and EEA1) fingers which is a novel zinc finger-like domain found in several proteins involved in membrane trafficking, or ankyrin repeats. These special domains provide unique characteristics and functions to the BTB proteins. The BTB domain facilitates protein-protein interactions between KCTD proteins to allow self-assembly or with non-BTB-domain-containing proteins to promote oligomerization. The X-ray crystal structure of KCTD5 also revealed assemblies of five subunits while tetramers were anticipated. A variety of functional roles of KCTD proteins have been identified by different signal pathways, including sonic hedgehog (Shh), Wnt/beta-catenin, FGF, and GABA signaling. Alignment of the amino acids in the potassium tetramerization domains of all known KCTD proteins demonstrates that most KCTD proteins can be divided into seven groups by amino acid sequences. The A-group contains KCTD9, KCTD17, KCTD 5, and KCTD 2. The B-group contains KCTD10, KCTD13, and TNFAIP1. The C-group contains KCTD7 and KCTD14. The d-group contains KCTD8, KCTD12, and KCTD16. The E-group contains KCTD11, KCTD21, and KCTD6. Members of the F-group include KCTD1 and KCTD15. And the final group is the G-group, which contains KCTD3 and SHKBP1 and BTB10. KCTD20, KCTD18, KCTD19, and KCTD4 do not belong to these seven groups (Figure 1). The evolutionary tree of the KCTD family proteins is similar to the group that Skoblov M et al. built. We also suggest that homologous KCTD members may share similar functional roles in proliferation, transcription, protein degradation, regulation of G-protein coupled receptors and other molecular or biological processes.

KCTD proteins as adaptor molecules

3BTB-domain-containing KCTD proteins may act as adaptors for interactions between the Cul3 ubiquitin ligase and its substrates. Thus, BTB KCTD proteins may facilitate successful ubiquitination of substrate proteins. Cul3 is one of seven human cullin proteins (Cul1,Cul2,Cul3,Cul4A,Cul4B,Cul5, and Cul7). Most cullins form complexes with substrate proteins by interacting with the BTB domains of adaptor proteins. Thus, the BTB domain is important for the process of ubiquitination and protein degradation. Ubiquitination involves a three-step enzymatic cascade, which is initially activated by ubiquitin-activating enzyme(E1). The substrate is then transferred to ubiquitin-conjugating enzyme(E2) and is finally linked with ubiquitin ligase(E3). Various cellular functions, including cell proliferation, differentiation, apoptosis, and protein transport, involve protein ubiquitination and de-ubiquitination. Bioinformatics and mutagenesis analyses have demonstrated that the best-characterized member of the KCTD family, KCTD11/REN, is expressed as two alternative variants, sKCTD11 and lKCTD11. Despite the fact that both variants possess a BTB domain in the N-terminus, only the lKCTD11 form has a complete BTB domain. Intriguingly, this has not disturbed the cul3-binding activity of sKCTD11. KCTD11/REN also mediates histone deacetylase (HDAC1) ubiquitination and degradation via cullin binding, resulting in reduced Hh/Gli signaling. The KCTD21 and KCTD6 have also been found to have the same features as KCTD11. Thus, KCTD21 and KCTD6 may also facilitate protein degradation and reduced cellular signaling due to associations with ubiquitin ligases. KCTD5 and KCTD7 have also been shown to function as substrate-specific adaptors for cullin3-based E3 ligases. In addition, KCTD7 has been shown to increase potassium conductance due to increased proteasome degradation of an unidentified substrate. Thus, several members of the KCTD family function as critical adaptor molecules for ubiquitin-mediated protein degradation. This function ultimately results in the modulation of important downstream signaling pathways and biological processes. As can be seen from Figure 1, cullin is fairly widely interaction with the family of KCTD proteins. In the future, this novel substrate of KCTD will help to understand the function of the complex of CUL3 –BTB.

KCTDs and disease

4KCTD proteins have essential roles in proliferation, differentiation, apoptosis, and metabolism. Improper regulation of KCTD genes has been associated with various diseases, including medulloblastoma, breast carcinoma, obesity, and pulmonary inflammation. Many studies show associations between mutations in individual KCTD genes or allelic loss of KCTDs with specific diseases. For example, a homozygous mutation (R99X) in exon 2 of KCTD7 has been described in progressive myoclonic epilepsy (PME). A second homozygous missense mutation (R94W) in exon 2 of KCTD7 has also been found in PME. In addition, a heterozygous missense mutation (R84W) and a large heterozygous deletion of exons 3 and 4 of KCTD7 have also been reported in patients with PME. Allelic deletion of human KCTD11at chromosomal location 17p13.2 has been found in medulloblastoma. In addition, gene copy number variants (CNVs) of KCTD13 mapping to chromosomal location 16p11.2 are considered to be major genetic causes of macrocephaly and microcephaly. Overexpression of KCTD13 induces microcephaly, whereas suppression of the same locus results in a macrocephalic phenotype. Missense mutations in KCTD1occur in Scalp-ear-nipple (SEN) syndrome. Single nucleotide polymorphisms(SNPs) of KCTD10 (i5642G- > C and V206VT- > C) are associated with altered concentrations of HDL cholesterol, particularly in subjects with high levels of carbohydrate intake. KCTD mutants affect proliferation, differentiation, apoptosis, and metabolism in different tissues. For example, the CNVs of KCTD13 affect the balance of proliferation and apoptosis in neuronal progenitor cells. In addition, deletions in KCTD11 abrogateinhibition of Shh signaling at the outer to inner external granule layer-granule cell progenitor (EGL GCP) transitions by affecting expression of Gli1 and Gli2. Deletions in KCASH, KCTD21, or KCTD6 block interactions with ubiquitination enzymes, preventing degradation of HDAC1. This leads to increased acetylation of Gli1 and increased Hh/Gli signaling, which drives uncontrolled proliferation and development and progression of medulloblastoma. Not only mutant KCTD could cause diseases, but also the change of KCTD expression involved in different diseases. All of the diseases related with KCTD proteins have been list in a Table 1 to make the family more convenient for further study.

Conclusion

5There are some features of KCTDs that have not been reviewed in this article. For example, KCTD8, -12, -12b, and-16 form functional oligomers with the GABAB receptor, resulting in the modulation of important signaling pathways. In addition, the PDIP1 family members (KCTD10, KCTD13, and TNFAIP1) are tumor necrosis factor-a-inducible proteins that can stimulate the activity of DNA polymerase in DNA replication and repair pathways. Furthermore, interactions between KCTD1, KCTD15, and AP-2 represses the transcriptional activity of AP-2a, Finally, KCTD1 has been shown to interact with PrPC. In the review, we summarize the BTB characteristics of the KCTD proteins, their roles in the ubiquitination pathway, and the relevance of KCTD mutations in various diseases. The review highlight the extraordinary possibility of the interaction of cullin-KCTDs to target substrates for ubiquitin-dependent degradation. If BTB-containing KCTD proteins can assemble into Cul3-based complexes, we estimate KCTD proteins can recruit substrates into ubiquitin system. We specifically discuss the role of KCTD1 in the ubiquitination pathway via interaction with cul3. We also hypothesize that KCTD1 mediate prion protein into ubiquitination signal pathway, and deregulation of the KCTD1 mediated prion protein ubiquitination might be both a cause and result of prion disease. Furthermore, we speculate that members of the same sub-groups may have similar roles in biological processes or molecular signaling pathways. We believe that further investigations into the functions of individual KCTD family members are warranted, particularly within the context of specific diseases as described here.

Abbreviations

6KCTD: Potassium channel tetramerization domain; BTB: Bric-a-brack,Tram-track, Broad complex; Cul3: Cullin E3 ubiquitin ligase; Shh: Sonic hedgehog; E1: Ubiquitin-activating enzyme; E2: Ubiquitin-conjugating enzyme; E3: Ubiquitin ligase; HDAC: Histone deacetylase; PME: Progressive myoclonic epilepsy; CNV: Copy number variant; SEN: Scalp-ear-nipplesyndrome; SNP: Single nucleotide polymorphism; EGL GCP: External granule layer-granule cell progenitor; KCASH: KCTD containing, Cullin3 adaptor, suppressor of Hedgehog; TNFAIP1: Tumor necrosis factor, alpha-induced protein 1.

Competing interests

7The authors declare that they have no competing interests.

Authors’ contributions

8ZP, YX, and GS co-wrote this review. All authors read and approved the final manuscript.

References 49

1.
Takahashi C Suzuki T Nishida E Kusakabe M Identification and characterization of Xenopus kctd15, an ectodermal gene repressed by the FGF pathwayInt J Dev Biol2012 35393402
Not in our library10.1387/ijdb.113333ct
2.
Mei F Xiang J Han S He Y Lu Y Xu J Guo D Xiao G Tien P Sun G Expression, purification, and secondary structure characterization of recombinant KCTD1Biochemistry (Mosc)2012 38941945
Not in our library10.1134/s0006297912080160
3.
Bayon Y Trinidad AG De la Puerta ML Del Carmen RM Bogetz J Rojas A De Pereda JM Rahmouni S Williams S Matsuzawa S KCTD5, a putative substrate adaptor for cullin3 ubiquitin ligasesFEBS J2008 31539003910
Not in our library10.1111/j.1742-4658.2008.06537.x
4.
Melnick A Ahmad KF Arai S Polinger A Ball H Borden KL Carlile GW Prive GG Licht JD In-depth mutational analysis of the promyelocytic leukemia zinc finger BTB/POZ domain reveals motifs and residues required for biological and transcriptional functionsMol Cell Biol2000 31765506567
Not in our library10.1128/mcb.20.17.6550-6567.2000
5.
Ahmad KF Melnick A Lax S Bouchard D Liu J Kiang CL Mayer S Takahashi S Licht JD Prive GG Mechanism of SMRT corepressor recruitment by the BCL6 BTB domainMol Cell2003 3615511564
Not in our library10.1016/s1097-2765(03)00454-4
6.
Kang MIKA Wakabayashi N Kim SG Yamamoto M Scaffolding of Keap1 to the actin cytoskeleton controls the function of Nrf2 as key regulator of cytoprotective phase 2 genesProc Natl Acad Sci U S A2004 320462051
Not in our library10.1073/pnas.0308347100
7.
Kreusch A Pfaffinger PJ Stevens CF Choe S Crystal structure of the tetramerization domain of the Shaker potassium channelNature1998 36679945948
Not in our library10.1038/31978
8.
Minor DL Lin YF Mobley BC Avelar A Jan YN Jan LY Berger JM The polar T1 interface is linked to conformational changes that open the voltage-gated potassium channelCell2000 35657670
Not in our library10.1016/s0092-8674(00)00088-x
9.
Pintard L Willems A Peter M Cullin-based ubiquitin ligases: Cul3-BTB complexes join the familyEMBO J2004 3816811687
Not in our library10.1038/sj.emboj.7600186
10.
Krek W BTB proteins as henchmen of Cul3-based ubiquitin ligasesNat Cell Biol2003 311950951
Not in our library10.1038/ncb1103-950
11.
Bardwell VJ Treisman R The POZ domain: a conserved protein-protein interaction motifGenes Dev1994 31416641677
Not in our library10.1101/gad.8.14.1664
12.
Correale S Pirone L Di Marcotullio L De Smaele E Greco A Mazza D Moretti M Alterio V Vitagliano L Di Gaetano S Molecular organization of the cullin E3 ligase adaptor KCTD11Biochimie2011 34715724
Not in our library10.1016/j.biochi.2010.12.014
13.
Ding X Luo C Zhou J Zhong Y Hu X Zhou F Ren K Gan L He A Zhu J The interaction of KCTD1 with transcription factor AP-2alpha inhibits its transactivationJ Cell Biochem2009 32285295
Not in our library10.1002/jcb.22002
14.
Ding XF Luo C Ren KQ Zhang J Zhou JL Hu X Liu RS Wang Y Gao X Characterization and expression of a human KCTD1 gene containing the BTB domain, which mediates transcriptional repression and homomeric interactionsDNA Cell Biol2008 35257265
Not in our library10.1089/dna.2007.0662
15.
Sequence and structural analysis of BTB domain proteins · 2005
No notice
16.
Dementieva IS Tereshko V McCrossan ZA Solomaha E Araki D Xu C Grigorieff N Goldstein SA Pentameric assembly of potassium channel tetramerization domain-containing protein 5J Mol Biol2009 31175191
Not in our library10.1016/j.jmb.2009.01.030
17.
De Smaele E Di Marcotullio L Moretti M Pelloni M Occhione MA Infante P Cucchi D Greco A Pietrosanti L Todorovic J Identification and characterization of KCASH2 and KCASH3, 2 novel Cullin3 adaptors suppressing histone deacetylase and Hedgehog activity in medulloblastomaNeoplasia2011 34374385
Not in our library10.1593/neo.101630
18.
Canettieri LDM G Greco A Coni S Antonucci L Infante P Pietrosanti EDS L Ferretti E Miele E Pelloni M De Simone G Pedone PG EM Giorgi A Steinkühler C Vitagliano L Pedone C Schinin IS ME Gulino A Histone deacetylase and Cullin3-REN(KCTD11) ubiquitin ligase interplay regulates hedgehog signalling through Gli acetylationNat Cell Biol2010 3132142
Not in our library10.1038/ncb2013
19.
De Smaele E Di Marcotullio L Ferretti E Screpanti I Alesse E Gulino A Chromosome 17p deletion in human medulloblastoma: a missing checkpoint in the Hedgehog pathwayCell Cycle2004 31012631266
Not in our library10.4161/cc.3.10.1200
20.
Dutta S Dawid IB Kctd15 inhibits neural crest formation by attenuating Wnt/beta-catenin signaling outputDevelopment2010 31830133018
Not in our library10.1242/dev.047548
21.
Seddik R Jungblut SP Silander OK Rajalu M Fritzius T Besseyrias V Jacquier V Fakler B Gassmann M Bettler B Opposite effects of KCTD subunit domains on GABA(B) receptor-mediated desensitizationJ Biol Chem2012 3473986939877
Not in our library10.1074/jbc.m112.412767
22.
Sand PG Langguth B Itzhacki J Bauer A Geis S Cardenas-Conejo ZE Pimentel V Kleinjung T Resequencing of the auxiliary GABA(B) receptor subunit gene KCTD12 in chronic tinnitusFront Syst Neurosci2012 341
Not in our library10.3389/fnsys.2012.00041
23.
Metz M Gassmann M Fakler B Schaeren-Wiemers N Bettler B Distribution of the auxiliary GABAB receptor subunits KCTD8, 12, 12b, and 16 in the mouse brainJ Comp Neurol2011 3814351454
Not in our library10.1002/cne.22610
24.
Schwenk J Metz M Zolles G Turecek R Fritzius T Bildl W Tarusawa E Kulik A Unger A Ivankova K Native GABA(B) receptors are heteromultimers with a family of auxiliary subunitsNature2010 37295231235
Not in our library10.1038/nature08964
25.
Skoblov M Marakhonov A Marakasova E Guskova A Chandhoke V Birerdinc A Baranova A Protein partners of KCTD proteins provide insights about their functional roles in cell differentiation and vertebrate developmentBioessays2013 37586596
Not in our library10.1002/bies.201300002
26.
Furukawa YJH M Borchers C Xiong Y Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligasesNat Cell Biol2005 310011007
Not in our library10.1038/ncb1056
27.
Hochstrasser M Ubiquitin-dependent protein degradationAnnu Rev Genet1996 3405439
Not in our library10.1146/annurev.genet.30.1.405
28.
Hershko A Ciechanover A The ubiquitin systemAnnu Rev Biochem1998 3425479
Not in our library10.1146/annurev.biochem.67.1.425
29.
De Smaele LDM E Moretti M Pelloni M Occhione MA Infante P Cucchi D Greco A Pietrosanti L Todorovic J Coni S Canettieri G Ferretti E Bei R Maroder M Screpanti I Gulino A Identification and characterization of KCASH2 and KCASH3, 2 novel Cullin3 adaptors suppressing histone deacetylase and Hedgehog activity in medulloblastomaNeoplasia2010 3374385
Not in our library10.1593/neo.101630
30.
Azizieh R Orduz D Van Bogaert P Bouschet T Rodriguez W Schiffmann SN Pirson I Abramowicz MJ Progressive myoclonic epilepsy-associated gene KCTD7 is a regulator of potassium conductance in neuronsMol Neurobiol2011 31111121
Not in our library10.1007/s12035-011-8194-0
31.
Staropoli JF Karaa A Lim ET Kirby A Elbalalesy N Romansky SG Leydiker KB Coppel SH Barone R Xin W A homozygous mutation in KCTD7 links neuronal ceroid lipofuscinosis to the ubiquitin-proteasome systemAm J Hum Genet2012 31202208
Not in our library10.1016/j.ajhg.2012.05.023
32.
Mancarelli MM Zazzeroni F Ciccocioppo L Capece D Po A Murgo S Di Camillo R Rinaldi C Ferretti E Gulino A The tumor suppressor gene KCTD11REN is regulated by Sp1 and methylation and its expression is reduced in tumorsMol Cancer2010 3172
Not in our library10.1186/1476-4598-9-172
33.
Faryna MF Konermann C Aulmann S Bermejo JL Brugger M Diederichs S Rom J Weichenhan D Claus R Rehli M Schirmacher P Sinn HP Plass C Gerhauser C Genome-wide methylation screen in low-grade breast cancer identifies novel epigenetically altered genes as potential biomarkers for tumor diagnosisFASEB J2012 349374950
Not in our library10.1096/fj.12-209502
34.
Yoganathan P Karunakaran S Ho MM Clee SM Nutritional regulation of genome-wide association obesity genes in a tissue-dependent mannerNutr Metab (Lond)2012 3165
Not in our library10.1186/1743-7075-9-65
35.
Paternoster L Evans DM Nohr EA Holst C Gaborieau V Brennan P Gjesing AP Grarup N Witte DR Jorgensen T Genome-wide population-based association study of extremely overweight young adults–the GOYA studyPLoS One2011 39e24303
Not in our library10.1371/journal.pone.0024303
36.
Koehler GPD DR Sweezey NB Tanswell AK Hu J Lung inflammation as a therapeutic target in cystic fibrosisCell Mol Biol2004 3377381
Not in our library10.1165/rcmb.2004-0124tr
37.
Van Bogaert P Azizieh R Desir J Aeby A De Meirleir L Laes JF Christiaens F Abramowicz MJ Mutation of a potassium channel-related gene in progressive myoclonic epilepsyAnn Neurol2007 36579586
Not in our library10.1002/ana.21121
38.
Kousi M Anttila V Schulz A Calafato S Jakkula E Riesch E Myllykangas L Kalimo H Topcu M Gokben S Novel mutations consolidate KCTD7 as a progressive myoclonus epilepsy geneJ Med Genet2012 36391399
Not in our library10.1136/jmedgenet-2012-100859
39.
Di Marcotullio L Ferretti E De Smaele E Argenti B Mincione C Zazzeroni F Gallo R Masuelli L Napolitano M Maroder M REN(KCTD11) is a suppressor of Hedgehog signaling and is deleted in human medulloblastomaProc Natl Acad Sci U S A2004 3291083310838
Not in our library10.1073/pnas.0400690101
40.
Golzio C Willer J Talkowski ME Oh EC Taniguchi Y Jacquemont S Reymond A Sun M Sawa A Gusella JF KCTD13 is a major driver of mirrored neuroanatomical phenotypes of the 16p11.2 copy number variantNature2012 37398363367
Not in our library10.1038/nature11091
41.
Marneros AG Beck AE Turner EH McMillin MJ Edwards MJ Field M De Macena Sobreira NL Perez AB Fortes JA Lampe AK Mutations in KCTD1 cause scalp-ear-nipple syndromeAm J Hum Genet2013 34621626
Not in our library10.1016/j.ajhg.2013.03.002
42.
Junyent M Parnell LD Lai CQ Lee YC Smith CE Arnett DK Tsai MY Kabagambe EK Straka RJ Province M Novel variants at KCTD10, MVK, and MMAB genes interact with dietary carbohydrates to modulate HDL-cholesterol concentrations in the genetics of lipid lowering drugs and diet network studyAm J Clin Nutr2009 33686694
Not in our library10.3945/ajcn.2009.27738
43.
Hasegawa T Asanuma H Ogino J Hirohashi Y Shinomura Y Iwaki H Kikuchi H Kondo T Use of potassium channel tetramerization domain-containing 12 as a biomarker for diagnosis and prognosis of gastrointestinal stromal tumorHum Pathol2013 3712711277
Not in our library10.1016/j.humpath.2012.10.013
44.
Lwa TR Tan CH Lew QJ Chu KL Tan J Lee YY Chao SH Identification of cellular genes critical to recombinant protein production using a Gaussia luciferase-based siRNA screening systemJ Biotechnol2010 34160168
Not in our library10.1016/j.jbiotec.2010.02.016
45.
Chen T Zhu L Zhou Y Pi B Liu X Deng G Zhang R Wang Y Wu Z Han M KCTD9 contributes to liver injury through NK cell activation during hepatitis B virus-induced acute-on-chronic liver failureClin Immunol2013 33207216
Not in our library10.1016/j.clim.2012.12.013
46.
Zhou YY Zou Y Chen T Wang HW Han MF Pi B Yan WM Xi D Huang JQ Luo XP KCTD9, a novel potassium channel related gene, was highly expressed in hepatic NK cells and T cells of fulminant hepatitis mice induced by MHV-3Zhonghua Gan Zang Bing Za Zhi2011 311833837
Not in our library10.3760/cma.j.issn.1007-3418.2011.11.010
47.
Hayasaki H Sohma Y Kanbara K Otsuki Y Heterogenous GABA(B) receptor-mediated pathways are involved in the local GABAergic system of the rat trigeminal ganglion: possible involvement of KCTD proteinsNeuroscience2012 3344358
Not in our library10.1016/j.neuroscience.2012.05.038
48.
Zhou J Ren K Liu X Xiong X Hu X Zhang J A novel PDIP1-related protein, KCTD10, that interacts with proliferating cell nuclear antigen and DNA polymerase deltaBiochim Biophys Acta2005 33200203
Not in our library10.1016/j.bbaexp.2005.05.005
49.
Huang T Xu J Xiang J Lu Y Chen R Huang L Xiao G Sun G PrPC interacts with potassium channel tetramerization domain containing 1 (KCTD1) protein through the PrP(51–136) region containing octapeptide repeatsBiochem Biophys Res Commun2012 31182186
Not in our library10.1016/j.bbrc.2011.11.081

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