Dynamic Regulation of the 26S Proteasome: From Synthesis to Degradation

Abstract

All eukaryotes rely on selective proteolysis to control the abundance of key regulatory proteins and maintain a healthy and properly functioning proteome. Most of this turnover is catalyzed by the 26S proteasome, an intricate, multi-subunit proteolytic machine. Proteasomes recognize and degrade proteins first marked with one or more chains of poly-ubiquitin, the addition of which is actuated by hundreds of ligases that individually identify appropriate substrates for ubiquitylation. Subsequent proteasomal digestion is essential and influences a myriad of cellular processes in species as diverse as plants, fungi and humans. Importantly, dysfunction of 26S proteasomes is associated with numerous human pathologies and profoundly impacts crop performance, thus making an understanding of proteasome dynamics critically relevant to almost all facets of human health and nutrition. Given this widespread significance, it is not surprising that sophisticated mechanisms have evolved to tightly regulate 26S proteasome assembly, abundance and activity in response to demand, organismal development and stress. These include controls on transcription and chaperone-mediated assembly, influences on proteasome localization and activity by an assortment of binding proteins and post-translational modifications, and ultimately the removal of excess or damaged particles via autophagy. Intriguingly, the autophagic clearance of damaged 26S proteasomes first involves their modification with ubiquitin, thus connecting ubiquitylation and autophagy as key regulatory events in proteasome quality control. This turnover is also influenced by two distinct biomolecular condensates that coalesce in the cytoplasm, one attracting damaged proteasomes for autophagy, and the other reversibly storing proteasomes during carbon starvation to protect them from autophagic clearance. In this review, we describe the current state of knowledge regarding the dynamic regulation of 26S proteasomes at all stages of their life cycle, illustrating how protein degradation through this proteolytic machine is tightly controlled to ensure optimal growth, development and longevity.

References 397

1. 1.

   Adachi A. Koizumi M. Ohsumi Y. (2017 ). Autophagy induction under carbon starvation conditions is negatively regulated by carbon catabolite repression. J. Biol. Chem. 292, 19905–19918.

   Not in our library10.1074/jbc.m117.817510 (opens in a new tab)

2. 2.

   Adrain C. Creagh E. M. Cullen S. P. Martin S. J. (2004 ). Caspase-dependent inactivation of proteasome function during programmed cell death in Drosophila and man. J. Biol. Chem. 279, 36923–36930.

   Not in our library10.1074/jbc.m402638200 (opens in a new tab)

3. 3.

   Albert S. Schaffer M. Beck F. Mosalaganti S. Asano S. Thomas H. F.. (2017 ). Proteasomes tether to two distinct sites at the nuclear pore complex. Proc. Natl. Acad. Sci. U.S.A. 114, 13726–13731.

   Not in our library10.1073/pnas.1716305114 (opens in a new tab)

4. 4.

   Alberti S. Gladfelter A. Mittag T. (2019 ). Considerations and challenges in studying liquid-liquid phase separation and biomolecular condensates. Cell 176, 419–434.

   Not in our library10.1016/j.cell.2018.12.035 (opens in a new tab)

5. 5.

   Arendt C. S. Hochstrasser M. (1997 ). Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active site formation. Proc. Natl. Acad. Sci. U.S.A. 94, 7156–7161.

   Not in our library10.1073/pnas.94.14.7156 (opens in a new tab)

6. 6.

   Armon T. Ganoth D. Hershko A. (1990 ). Assembly of the 26S complex that degrades proteins ligated to ubiquitin is accompanied by the formation of ATPase activity. J. Biol. Chem. 265, 20723–20726.

   Not in our library

7. 7.

   Asai M. Tsukamoto O. Minamino T. Asanuma H. Fujita M. Asano Y.. (2009 ). PKA rapidly enhances proteasome assembly and activity in in vivo canine hearts. J. Mol. Cell. Cardiol. 46, 452–462.

   Not in our library10.1016/j.yjmcc.2008.11.001 (opens in a new tab)

8. 8.

   Asano S. Fukuda Y. Beck F. Aufderheide A. Förster F. Danev R.. (2015 ). A molecular census of 26S proteasomes in intact neurons. Science 347, 439–442.

   Not in our library10.1126/science.1261197 (opens in a new tab)

9. 9.

   Aufderheide A. Beck F. Stenge F. Hartwig M. Schweitzer A. Pfeifer G.. (2015a ). Structural characterization of the interaction of Ubp6 with the 26S proteasome. Proc. Natl. Acad. Sci. U.S.A. 112, 8626–8631.

   Not in our library10.1073/pnas.1510449112 (opens in a new tab)

10. 10.

    Aufderheide A. Unverdorben P. Baumeister W. Förster F. (2015b ). Structural disorder and its role in proteasomal degradation. FEBS Lett. 589, 2552–2560.

    Not in our library10.1016/j.febslet.2015.07.034 (opens in a new tab)

11. 11.

    Bader M. Benjamin S. Wapinski O. L. Smith D. M. Goldberg A. L. Steller H. (2011 ). A conserved F-box regulatory complex controls proteasome activity in Drosophila. Cell 145, 371–382.

    Not in our library10.1016/j.cell.2011.03.021 (opens in a new tab)

12. 12.

    Bai M. Zhao X. Sahara K. Ohte Y. Hirano Y. Kaneko T.. (2014 ). Assembly mechanisms of specialized core particles of the proteasome. Biomolecules 4, 662–677.

    Not in our library10.3390/biom4030662 (opens in a new tab)

13. 13.

    Baird L. Tsujita T. Kobayashi E. H. Funayama R. Nagashima T. Nakayama K.. (2017 ). A homeostatic shift facilitates endoplasmic reticulum proteostasis through transcriptional integration of proteostatic stress response pathways. Mol. Cell. Biol. 37:00439.

    Not in our library10.1128/mcb.00439-16 (opens in a new tab)

14. 14.

    Bajorek M. Finley D. Glickman M. H. (2003 ). Proteasome disassembly and down-regulation is correlated with viability during stationary phase. Curr. Biol. 13, 1140–1144.

    Not in our library10.1016/s0960-9822(03)00417-2 (opens in a new tab)

15. 15.

    Barrault M. B. Richet N. Godard C. Murciano B. Le Tallec B. Rousseau E.. (2012 ). Dual functions of the Hsm3 protein in chaperoning and scaffolding regulatory particle subunits during the proteasome assembly. Proc. Natl. Acad. Sci. U.S.A. 109, 1001–1010.

    Not in our library10.1073/pnas.1116538109 (opens in a new tab)

16. 16.

    Barthelme D. Sauer R. T. (2012 ). Identification of the Cdc48-20S proteasome as an ancient AAA proteolytic machine. Science 337, 843–846.

    Not in our library10.1126/science.1224352 (opens in a new tab)

17. 17.

    Bashore C. Dambacher C. M. Goodall E. A. Matyskiela M. E. Lander G. C. Martin A. (2015 ). Ubp6 deubiquitinase controls conformational dynamics and substrate degradation of the 26S proteasome. Nat. Struct. Mol. Biol. 22, 712–719.

    Not in our library10.1038/nsmb.3075 (opens in a new tab)

18. 18.

    Baumeister W. Dahlmann B. Hegerl R. Kopp F. Keuhn L. Pfeifer G. (1994 ). Electron microscopy and image analysis of the multi-catalytic proteinase. FEBS Lett. 241, 239–245.

    Not in our library10.1016/0014-5793(88)81069-x (opens in a new tab)

19. 19.

    Beck F. Unverdorben P. Bohn S. Schweitzer A. Pfeifer G. Sakata E.. (2012 ). Near-atomic resolution structural model of the yeast 26S proteasome. Proc. Natl. Acad. Sci. U.S.A. 109, 14870–14875.

    Not in our library10.1073/pnas.1213333109 (opens in a new tab)

20. 20.

    Beck M. Hurt E. (2017 ). The nuclear pore complex: understanding its function through structural insight. Nat. Rev. Mol. Cell Biol. 18, 73–89.

    Not in our library10.1038/nrm.2016.147 (opens in a new tab)

21. 21.

    Beckwith R. Estrin E. Worden E. J. Martin A. (2013 ). Reconstitution of the 26S proteasome reveals functional asymmetries in its AAA unfoldase. Nat. Struct. Mol. Biol. 20, 1164–1172.

    Not in our library10.1038/nsmb.2659 (opens in a new tab)

22. 22.

    Besche H. C. Sha Z. Kukushkin N. V. Peth A. Hock E. M. Kim W. (2014 ). Auto-ubiquitination of the 26S proteasome on Rpn13 regulates breakdown of ubiquitin conjugates. EMBO J. 33, 1159–1176.

    Not in our library10.1002/embj.201386906 (opens in a new tab)

23. 23.

    Bhattacharyya S. Yu H. Mim C. Matouschek A. (2014 ). Regulated protein turnover: snapshots of the proteasome in action. Nat. Rev. Mol. Cell Biol. 15, 122–133.

    Not in our library10.1038/nrm3741 (opens in a new tab)

24. 24.

    Bingol B. Schuman E. M. (2006 ). Activity-dependent dynamics and sequestration of proteasomes in dendritic spines. Nature 441, 1144–1148.

    Not in our library10.1038/nature04769 (opens in a new tab)

25. 25.

    Biswas M. Phan D. Watanabe M. Chan J. Y. (2011 ). The Fbw7 tumor suppressor regulates nuclear factor E2-related factor 1 transcription factor turnover through proteasome-mediated proteolysis. J. Biol. Chem. 286, 39282–39289.

    Not in our library10.1074/jbc.m111.253807 (opens in a new tab)

26. 26.

    Book A. J. Gladman N. P. Lee S. S. Scalf M. Smith L. M. Vierstra R. D. (2010 ). Affinity purification of the Arabidopsis 26S proteasome reveals a diverse array of plant proteolytic complexes. J. Biol. Chem. 285, 25554–25569.

    Not in our library10.1074/jbc.m110.136622 (opens in a new tab)

27. 27.

    Brooks P. Fuertes G. Murray R. Z. Bose S. Knecht E. Rechsteiner M.. (2000 ). Subcellular localization of proteasomes and their regulatory complexes in mammalian cells. Biochem. J. 346, 155–161.

    Not in our library10.1042/bj3460155 (opens in a new tab)

28. 28.

    Buetow L. Huang D. T. (2016 ). Structural insights into the catalysis and regulation of E3 ubiquitin ligases. Nat. Rev. Mol. Cell Biol. 17, 626–642.

    Not in our library10.1038/nrm.2016.91 (opens in a new tab)

29. 29.

    Burcoglu J. Zhao L. Enenkel C. (2015 ). Nuclear import of yeast proteasomes. Cells 4, 387–405.

    Not in our library10.3390/cells4030387 (opens in a new tab)

30. 30.

    Burri L. Höckendorff J. Boehm U. Klamp T. Dohmen R. J. Lévy F. (2000 ). Identification and characterization of a mammalian protein interacting with 20S proteasome precursors. Proc. Natl. Acad. Sci. U.S.A. 97, 10348–10353.

    Not in our library10.1073/pnas.190268597 (opens in a new tab)

31. 31.

    Chen L. Madura K. (2014 ). Yeast importin-α (Srp1) performs distinct roles in the import of nuclear proteins and in targeting proteasomes to the nucleus. J. Biol. Chem. 289, 32339–32352.

    Not in our library10.1074/jbc.m114.582023 (opens in a new tab)

32. 32.

    Chen L. Romero L. Chuang S. M. Tournier V. Joshi K. K. Lee J. A.. (2011 ). Sts1 plays a key role in targeting proteasomes to the nucleus. J. Biol. Chem. 286, 3104–3118.

    Not in our library10.1074/jbc.m110.135863 (opens in a new tab)

33. 33.

    Chen P. Hochstrasser M. (1996 ). Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly. Cell 86, 961–972.

    Not in our library10.1016/s0092-8674(00)80171-3 (opens in a new tab)

34. 34.

    Chen S. Wu J. Lu Y. Ma Y. B. Lee B. H. Yu Z.. (2016 ). Structural basis for dynamic regulation of the human 26S proteasome. Proc. Natl. Acad. Sci. U.S.A. 113, 12991–12996.

    Not in our library10.1073/pnas.1614614113 (opens in a new tab)

35. 35.

    Chen X. Ebelle D. L. Wright B. J. Sridharan V. Hooper E. Walters K. J. (2019 ). Structure of RPN10 bound to UBQLN2 UBL illustrates the basis for complementarity between shuttle factors and substrates at the proteasome. J. Mol. Biol. 431, 939–955.

    Not in our library10.1016/j.jmb.2019.01.021 (opens in a new tab)

36. 36.

    Cho-Park P. F. Steller H. (2013 ). Proteasome regulation by ADP-ribosylation. Cell 153, 614–627.

    Not in our library10.1016/j.cell.2013.03.040 (opens in a new tab)

37. 37.

    Chu-Ping M. Slaughter C. A. DeMartino G. N. (1992 ). Purification and characterization of a protein inhibitor of the 20S proteasome (macropain). Biochim. Biophys. Acta 1119, 303–311.

    Not in our library10.1016/0167-4838(92)90218-3 (opens in a new tab)

38. 38.

    Ciechanover A. Finley D. Varshavsky A. (1984 ). Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85. Cell 37, 57–66.

    Not in our library10.1016/0092-8674(84)90300-3 (opens in a new tab)

39. 39.

    Ciechanover A. Heller H. Elias S. Haas A. L. Hershko A. (1980 ). ATP-dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation. Proc. Natl. Acad. Sci. U.S.A. 77, 1365–1368.

    Not in our library10.1073/pnas.77.3.1365 (opens in a new tab)

40. 40.

    Clague M. J. Urbé S. Komander D. (2019 ). Breaking the chains: deubiquitylating enzyme specificity begets function. Nat. Rev. Mol. Cell Biol. 20, 338–352.

    Not in our library10.1038/s41580-019-0099-1 (opens in a new tab)

41. 41.

    Cohen-Kaplan V. Livneh I. Avni N. Fabre B. Ziv T. Kwon Y. T.. (2016 ). p62- and ubiquitin-dependent stress-induced autophagy of the mammalian 26S proteasome. Proc. Natl. Acad. Sci. U.S.A. 113, 7490–7499.

    Not in our library10.1073/pnas.1615455113 (opens in a new tab)

42. 42.

    Collins G. A. Goldberg A. L. (2017 ). The logic of the 26S proteasome. Cell 169, 792–806.

    Not in our library10.1016/j.cell.2017.04.023 (opens in a new tab)

43. 43.
    The Proteasome in Modern Drug Discovery: Second Life of a Highly Valuable Drug Target · 2017

    Not checked
44. 44.

    Crosas B. Hanna J. Kirkpatrick D. S. Zhang D. P. Tone Y. Hathaway N. A. (2006 ). Ubiquitin chains are re-modelled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities. Cell 127, 1401–1413.

    Not in our library10.1016/j.cell.2006.09.051 (opens in a new tab)

45. 45.

    Cuervo A. M. Palmer A. Rivett A. J. Knecht E. (1995 ). Degradation of proteasomes by lysosomes in rat liver. Eur. J. Biochem. 227, 792–800.

    Not in our library10.1111/j.1432-1033.1995.tb20203.x (opens in a new tab)

46. 46.

    Cui Z. Scruggs S. B. Gilda J. E. Ping P. Gomes A. V. (2014 ). Regulation of cardiac proteasomes by ubiquitination, SUMOylation, and beyond. J. Mol. Cell. Cardiol. 71, 32–42.

    Not in our library10.1016/j.yjmcc.2013.10.008 (opens in a new tab)

47. 47.

    da Fonseca P. C. Morris E. P. (2008 ). Structure of the human 26S proteasome: subunit radial displacements open the gate into the proteolytic core. J. Biol. Chem. 283, 23305–23314.

    Not in our library10.1074/jbc.m802716200 (opens in a new tab)

48. 48.
    Atomic structure of the 26S proteasome lid reveals the mechanism of deubiquitinase inhibition · 2016

    Not checked
49. 49.

    Dang F. W. Chen L. Madura K. (2016 ). Catalytically active proteasomes function predominantly in the cytosol. J. Biol. Chem. 291, 18765–18777.

    Not in our library10.1074/jbc.m115.712406 (opens in a new tab)

50. 50.

    Dange T. Smith D. M. Noy T. Rommel P. C. Jurzitza L. Cordero R. J.. (2011 ). Blm10 protein promotes proteasomal substrate turnover by an active gating mechanism. J. Biol. Chem. 286, 42830–42839.

    Not in our library10.1074/jbc.m111.300178 (opens in a new tab)

51. 51.

    De La Mota-Peynado A. Lee S. Y. Pierce B. M. Wani P. Singh C. R. Roelofs J. (2013 ). The proteasome-associated protein Ecm29 inhibits proteasomal ATPase activity and in vivo protein degradation by the proteasome. J. Biol. Chem. 288, 29467–29481.

    Not in our library10.1074/jbc.m113.491662 (opens in a new tab)

52. 52.

    de la Peña A. H. Goodall E. A. Gates S. N. Lander G. C. Martin A. (2018 ). Substrate-engaged 26S proteasome structures reveal mechanisms for ATP hydrolysis-driven translocation. Science 362:0725.

    Not in our library10.1126/science.aav0725 (opens in a new tab)

53. 53.

    de Poot S. A. H. Tian G. Finley D. (2017 ). Meddling with fate: the proteasomal deubiquitylating enzymes. J. Mol. Biol. 429, 3525–3545.

    Not in our library10.1016/j.jmb.2017.09.015 (opens in a new tab)

54. 54.

    Demasi M. Silva G. M. Netto L. E. (2003 ). The 20S proteasome from Saccharomyces cerevisiae is responsive to redox modifications and is S-glutathionylated. J. Biol. Chem. 278, 679–685.

    Not in our library10.1074/jbc.m209282200 (opens in a new tab)

55. 55.

    Dengjel J. Høyer-Hansen M. Nielsen M. O. Eisenberg T. Harder L. M. Schandorff S.. (2012 ). Identification of autophagosome-associated proteins and regulators by quantitative proteomic analysis and genetic screens. Mol. Cell. Proteomics 11, M111.014035.

    Not in our library10.1074/mcp.m111.014035 (opens in a new tab)

56. 56.

    Dick T. P. Nussbaum A. K. Deeg M. Heinemeyer W. Groll M. Schirle M.. (1998 ). Contribution of proteasomal β-subunits to the cleavage of peptide substrates analyzed with yeast mutants. J. Biol. Chem. 273, 25637–25646.

    Not in our library10.1074/jbc.273.40.25637 (opens in a new tab)

57. 57.

    Dikic I. Elazar Z. (2018 ). Mechanism and medical implications of mammalian autophagy. Nat. Rev. Mol. Cell Biol. 19, 349–364.

    Not in our library10.1038/s41580-018-0003-4 (opens in a new tab)

58. 58.

    Dong Y. Zhang S. Wu Z. Li X. Wang W. L. Zhu Y. (2019 ). Cryo-EM structures and dynamics of substrate-engaged human 26S proteasomes. Nature 565, 49–55.

    Not in our library10.1038/s41586-018-0736-4 (opens in a new tab)

59. 59.

    Dou Z. Xu C. Donahue G. Shimi T. Pan J. A. Zhu J.. (2015 ). Autophagy mediates degradation of nuclear lamina. Nature 527, 105–109.

    Not in our library10.1038/nature15548 (opens in a new tab)

60. 60.

    Driscoll J. Brown M. G. Finley D. Monaco J. J. (1993 ). MHC-linked LMP gene products specifically alter peptidase activities of the proteasome. Nature 365, 262–264.

    Not in our library10.1038/365262a0 (opens in a new tab)

61. 61.

    Dubiel W. Pratt G. Ferrell K. Rechsteiner M. (1992 ). Purification of an 11S regulator of the multi-catalytic protease. J. Biol. Chem. 267, 22369–22377.

    Not in our library

62. 62.

    Eisele M. R. Reed R. G. Rudack T. Schweitzer A. Beck F. Nagy I. (2018 ). Expanded coverage of the 26S proteasome conformational landscape reveals mechanisms of peptide gating. Cell Rep. 24, 1301–1315.

    Not in our library10.1016/j.celrep.2018.07.004 (opens in a new tab)

63. 63.

    Elbaz-Alon Y. Eisenberg-Bord M. Shinder V. Stiller S. B. Shimoni E. Wiedemann N.. (2015 ). Lam6 regulates the extent of contacts between organelles. Cell Rep. 12, 7–14.

    Not in our library10.1016/j.celrep.2015.06.022 (opens in a new tab)

64. 64.

    Elsasser S. Chandler-Militello D. Müller B. Hanna J. Finley D. (2004 ). Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome. J. Biol. Chem. 279, 26817–26822.

    Not in our library10.1074/jbc.m404020200 (opens in a new tab)

65. 65.

    Elsasser S. Gali R. R. Schwickart M. Larsen C. N. Leggett D. S. Müller B.. (2002 ). Proteasome subunit Rpn1 binds ubiquitin-like protein domains. Nat. Cell Biol. 4, 725–730.

    Not in our library10.1038/ncb845 (opens in a new tab)

66. 66.

    Elsasser S. Schmidt M. Finley D. (2005 ). Characterization of the proteasome using native gel electrophoresis. Methods Enzymol. 398, 353–363.

    Not in our library10.1016/s0076-6879(05)98029-4 (opens in a new tab)

67. 67.

    Enenkel C. Blobel G. Rexach M. (1995 ). Identification of a yeast karyopherin heterodimer that targets import substrate to mammalian nuclear pore complexes. J. Biol. Chem. 270, 16499–16502.

    Not in our library10.1074/jbc.270.28.16499 (opens in a new tab)

68. 68.

    Enenkel C. Lehmann A. Kloetzel P. M. (1998 ). Subcellular distribution of proteasomes implicates a major location of protein degradation in the nuclear envelope-ER network in yeast. EMBO J. 17, 6144–6154.

    Not in our library10.1093/emboj/17.21.6144 (opens in a new tab)

69. 69.

    Esaki M. Johjima-Murata A. Islam M. T. Ogura T. (2018 ). Biological and pathological implications of an alternative ATP-powered proteasome assembly with Cdc48 and the 20 peptidase. Front. Mol. Biosci. 5:56

    Not in our library10.3389/fmolb.2018.00056 (opens in a new tab)

70. 70.

    Estrin E. Lopez-Blanco J. R. Chacón P. Martin A. (2013 ). Formation of an intricate helical bundle dictates the assembly of the 26S proteasome lid. Structure 21, 1624–1635.

    Not in our library10.1016/j.str.2013.06.023 (opens in a new tab)

71. 71.

    Eytan E. Ganoth D. Armon T. Hershko A. (1989 ). ATP-dependent incorporation of the 20S protease into the 26S complex that degrades proteins conjugated to ubiquitin. Proc. Natl. Acad. Sci. U.S.A. 86, 7751–7755.

    Not in our library10.1073/pnas.86.20.7751 (opens in a new tab)

72. 72.

    Farmer L. M. Book A. J. Lee K. H. Lin Y. L. Fu H. Vierstra R. D. (2010 ). The RAD23 family provides an essential connection between the 26S proteasome and ubiquitylated proteins in Arabidopsis. Plant Cell 22, 124–142.

    Not in our library10.1105/tpc.109.072660 (opens in a new tab)

73. 73.

    Farré J. C. Subramani S. (2016 ). Mechanistic insights into selective autophagy pathways: lessons from yeast. Nat. Rev. Mol. Cell Biol. 17, 537–552.

    Not in our library10.1038/nrm.2016.74 (opens in a new tab)

74. 74.

    Fatimababy A. S. Lin Y. L. Usharani R. Radjacommare R. Wang H. T. Tsai H. L.. (2010 ). Cross-species divergence of the major recognition pathways of ubiquitylated substrates for ubiquitin/26S proteasome-mediated proteolysis. FEBS J. 277, 796–816.

    Not in our library10.1111/j.1742-4658.2009.07531.x (opens in a new tab)

75. 75.

    Finley D. (2009 ). Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu. Rev. Biochem. 78, 477–513.

    Not in our library10.1146/annurev.biochem.78.081507.101607 (opens in a new tab)

76. 76.

    Finley D. Prado M. A. (2019 ). The proteasome and its network: engineering for adaptability. Cold Spring Harb. Perspect. Biol.

    Not in our library10.1101/cshperspect.a033985 (opens in a new tab)

77. 77.

    Finley D. Ulrich H. D. Sommer T. Kaiser P. (2012 ). The ubiquitin-proteasome system of Saccharomyces cerevisiae. Genetics 192, 319–360.

    Not in our library10.1534/genetics.112.140467 (opens in a new tab)

78. 78.

    Fishbain S. Prakash S. Herrig A. Elsasser S. Matouschek A. (2011 ). Rad23 escapes degradation because it lacks a proteasome initiation region. Nat. Commun. 2:192.

    Not in our library10.1038/ncomms1194 (opens in a new tab)

79. 79.

    Frentzel S. Pesold-Hurt B. Seelig A. Kloetzel P. M. (1994 ). 20S proteasomes are assembled via distinct precursor complexes: processing of LMP2 and LMP7 proproteins takes place in 13-16 S pre-proteasome complexes. J. Mol. Biol. 236, 975–981.

    Not in our library10.1016/0022-2836(94)90003-5 (opens in a new tab)

80. 80.

    Fu H. Doelling J. H. Arendt C. S. Hochstrasser M. Vierstra R. D. (1998a ). Molecular organization of the 20S proteasome gene family from Arabidopsis thaliana. Genetics 149, 677–692.

    Not in our library10.1093/genetics/149.2.677 (opens in a new tab)

81. 81.

    Fu H. Doelling J. H. Rubin D. M. Vierstra R. D. (1999 ). Structural and functional analysis of the six regulatory particle AAA-ATPase subunits from the Arabidopsis 26S proteasome. Plant J. 18, 529–539.

    Not in our library10.1046/j.1365-313x.1999.00479.x (opens in a new tab)

82. 82.

    Fu H. Sadis S. Rubin D. M. Glickman M. H. van Nocker S. Finley D. (1998b ). Multi-ubiquitin chain binding and protein degradation are mediated by distinct domains within the 26S proteasome subunit Mcb1. J. Biol. Chem. 273, 1970–1981.

    Not in our library10.1074/jbc.273.4.1970 (opens in a new tab)

83. 83.

    Fu X. Sokolova V. Webb K. J. Old W. Park S. (2018 ). Ubiquitin-dependent switch during assembly of the proteasomal ATPases mediated by Not4 ubiquitin ligase. Proc. Natl. Acad. Sci. U.S.A. 115, 13246–13251.

    Not in our library10.1073/pnas.1805353115 (opens in a new tab)

84. 84.

    Fukunaga K. Kudo T. Toh-e A. Tanaka K. Saeki Y. (2010 ). Dissection of the assembly pathway of the proteasome lid in Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 396, 1048–1053.

    Not in our library10.1016/j.bbrc.2010.05.061 (opens in a new tab)

85. 85.

    Funakoshi M. Tomko R. J. Kobayashi H. Hochstrasser M. (2009 ). Multiple assembly chaperones govern biogenesis of the proteasome regulatory particle base. Cell 137, 887–899.

    Not in our library10.1016/j.cell.2009.04.061 (opens in a new tab)

86. 86.

    Gaczynska M. Rock K. L. Goldberg A. L. (1993 ). Interferon-γ and expression of MHC genes regulate peptide hydrolysis by proteasomes. Nature 365, 264–267.

    Not in our library10.1038/365264a0 (opens in a new tab)

87. 87.

    Gao W. Kang J. H. Liao Y. Ding W. X. Gambotto A. A. Watkins S. C.. (2010 ). Biochemical isolation and characterization of the tubulovesicular LC3-positive autophagosomal compartment. J. Biol. Chem. 285, 1371–1383.

    Not in our library10.1074/jbc.m109.054197 (opens in a new tab)

88. 88.

    Gardner R. G. Nelson Z. W. Gottschling D. E. (2005 ). Degradation-mediated protein quality control in the nucleus. Cell 120, 803–815.

    Not in our library10.1016/j.cell.2005.01.016 (opens in a new tab)

89. 89.

    Gatica D. Lahiri V. Klionsky D. J. (2018 ). Cargo recognition and degradation by selective autophagy. Nat. Cell Biol. 20, 233–242.

    Not in our library10.1038/s41556-018-0037-z (opens in a new tab)

90. 90.

    Gerards W. L. de Jong W. W. Bloemendal H. Boelens W. (1998 ). The human proteasome subunit HsC8 induces ring formation of other α-type subunits. J. Mol. Biol. 275, 113–121.

    Not in our library10.1006/jmbi.1997.1429 (opens in a new tab)

91. 91.

    Gerards W. L. Enzlin J. Häner M. Hendriks I. L. Aebi U. Bloemendal H.. (1997 ). The human α-type proteasomal subunit HsC8 forms a double ring-like structure, but does not assemble into proteasome-like particles with the β-type subunits HsDelta or HsBPROS26. J. Biol. Chem. 272, 10080–10086.

    Not in our library10.1074/jbc.272.15.10080 (opens in a new tab)

92. 92.

    Gille C. Goede A. Schlöetelburg C. Preissner R. Kloetzel P. M. Göbel U. B.. (2003 ). A comprehensive view on proteasomal sequences: implications for the evolution of the proteasome. J. Mol. Biol. 326, 1437–1448.

    Not in our library10.1016/s0022-2836(02)01470-5 (opens in a new tab)

93. 93.

    Gladman N. P. Marshall R. S. Lee K. H. Vierstra R. D. (2016 ). The proteasome stress regulon is controlled by a pair of NAC transcription factors in Arabidopsis. Plant Cell 28, 1279–1296.

    Not in our library10.1105/tpc.15.01022 (opens in a new tab)

94. 94.

    Glickman M. H. Rubin D. M. Coux O. Wefes I. Pfeifer G. Cjeka Z. (1998 ). A sub-complex of the proteasome regulatory particle required for ubiquitin conjugate degradation and related to the COP9 signalosome and eIF3. Cell 94, 615–623.

    Not in our library10.1016/s0092-8674(00)81603-7 (opens in a new tab)

95. 95.

    Goebl M. G. Yochem J. Jentsch S. McGrath J. P. Varshavsky A. Byers B. (1988 ). The yeast cell cycle gene CDC34 encodes a ubiquitin conjugating enzyme. Science 241, 1331–1335.

    Not in our library10.1126/science.2842867 (opens in a new tab)

96. 96.

    Gomes A. V. Zong C. Edmondson R. D. Li X. Stefani E. Zhang J.. (2006 ). Mapping the murine cardiac 26S proteasome complexes. Circ. Res. 99, 362–371.

    Not in our library10.1161/01.res.0000237386.98506.f7 (opens in a new tab)

97. 97.

    Griffin T. A. Nandi D. Cruz M. Fehling H. J. Kaer L. Monaco J. J. (1998 ). Immunoproteasome assembly: co-operative incorporation of interferon-γ-inducible subunits. J. Exp. Med. 187, 97–104.

    Not in our library10.1084/jem.187.1.97 (opens in a new tab)

98. 98.

    Griffin T. A. Slack J. P. McCluskey T. S. Monaco J. J. Colbert R. A. (2000 ). Identification of proteassemblin, a mammalian homologue of the yeast protein, Ump1p, that is required for normal proteasome assembly. Mol. Cell Biol. Res. Commun. 3, 212–217.

    Not in our library10.1006/mcbr.2000.0213 (opens in a new tab)

99. 99.

    Groettrup M. Standera S. Stohwasser R. Kloetzel P. M. (1997 ). The subunits MECL1 and LMP2 are mutually required for incorporation into the 20S proteasome. Proc. Natl. Acad. Sci. U.S.A. 94, 8970–8975.

    Not in our library10.1073/pnas.94.17.8970 (opens in a new tab)

100. 100.

     Groll M. Bajorek M. Köhler A. Moroder L. Rubin D. M. Huber R.. (2000 ). A gated channel into the proteasome core particle. Nat. Struct. Biol. 7, 1062–1067.

     Not in our library10.1038/80992 (opens in a new tab)

101. 101.

     Groll M. Ditzel L. Löwe J. Stock D. Bochtler M. Bartunik H. D. (1997 ). Structure of the 20S proteasome from yeast at 2.4Å resolution. Nature 386, 463–471.

     Not in our library10.1038/386463a0 (opens in a new tab)

102. 102.

     Groll M. Heinemeyer W. Jäger S. Ullrich T. Bochtler M. Wolf D. H. (1999 ). The catalytic site of 20S proteasomes and their role in subunit maturation: a mutational and crystallographic study. Proc. Natl. Acad. Sci. U.S.A. 96, 10976–10983.

     Not in our library10.1073/pnas.96.20.10976 (opens in a new tab)

103. 103.

     Gu Z. C. Wu E. Sailer C. Jando J. Styles E. Eisenkolb I.. (2017 ). Ubiquitin orchestrates proteasome dynamics between proliferation and quiescence in yeast. Mol. Biol. Cell 28, 2479–2491.

     Not in our library10.1091/mbc.e17-03-0162 (opens in a new tab)

104. 104.

     Guo X. Engel J. L. Xiao J. Tagliabracci V. S. Wang X. Huang L.. (2011 ). UBLCP1 is a 26S proteasome phosphatase that regulates nuclear proteasome activity. Proc. Natl. Acad. Sci. U.S.A. 108, 18649–18654.

     Not in our library10.1073/pnas.1113170108 (opens in a new tab)

105. 105.

     Ha S. W. Ju D. Xie Y. (2012 ). The N-terminal domain of Rpn4 serves as a portable ubiquitin-independent degron and is recognized by specific 19S RP subunits. Biochem. Biophys. Res. Commun. 419, 226–231.

     Not in our library10.1016/j.bbrc.2012.01.152 (opens in a new tab)

106. 106.

     Hahn J. S. Neef D. W. Thiele D. J. (2006 ). A stress regulatory network for co-ordinated activation of proteasome expression mediated by yeast heat shock transcription factor. Mol. Microbiol. 60, 240–251.

     Not in our library10.1111/j.1365-2958.2006.05097.x (opens in a new tab)

107. 107.

     Hamazaki J. Iemura S. Natsume T. Yashiroda H. Tanaka K. Murata S. (2006 ). A novel proteasome-interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes. EMBO J. 25, 4524–4536.

     Not in our library10.1038/sj.emboj.7601338 (opens in a new tab)

108. 108.

     Hanna J. Hathaway N. A. Tone Y. Crosas B. Elsasser S. Kirkpatrick D. S. (2006 ). The deubiquitinating enzyme Ubp6 functions non-catalytically to delay proteasomal degradation. Cell 127, 99–111.

     Not in our library10.1016/j.cell.2006.07.038 (opens in a new tab)

109. 109.

     Hanna J. Meides A. Zhang D. P. Finley D. (2007 ). A ubiquitin stress response induces altered proteasome composition. Cell 129, 747–759.

     Not in our library10.1016/j.cell.2007.03.042 (opens in a new tab)

110. 110.

     Hanna J. Waterman D. Boselli M. Finley D. (2012 ). Spg5 protein regulates the proteasome in quiescence. J. Biol. Chem. 287, 34400–34409.

     Not in our library10.1074/jbc.m112.390294 (opens in a new tab)

111. 111.

     Hanssum A. Zhong Z. Rousseau A. Krzyzosiak A. Sigurdardottir A. Bertolotti A. (2014 ). An inducible chaperone adapts proteasome assembly to stress. Mol. Cell 55, 566–577.

     Not in our library10.1016/j.molcel.2014.06.017 (opens in a new tab)

112. 112.

     Haracska L. Udvardy A. (1997 ). Mapping the ubiquitin-binding domains in the p54 regulatory complex subunit of the Drosophila 26S protease. FEBS Lett. 412, 331–336.

     Not in our library10.1016/s0014-5793(97)00808-9 (opens in a new tab)

113. 113.

     Haruki H. Nishikawa J. Laemmli U. K. (2008 ). The anchor-away technique: rapid, conditional establishment of yeast mutant phenotypes. Mol. Cell 31, 925–932.

     Not in our library10.1016/j.molcel.2008.07.020 (opens in a new tab)

114. 114.

     Hatanaka A. Chen B. Sun J. Q. Mano Y. Funakoshi M. Kobayashi H.. (2011 ). Fub1p, a novel protein isolated by boundary screening, binds the proteasome complex. Genes Genet. Syst. 86, 305–314.

     Not in our library10.1266/ggs.86.305 (opens in a new tab)

115. 115.

     Havé M. Marmagne A. Chardon F. Masclaux-Daubresse C. (2017 ). Nitrogen re-mobilization during leaf senescence: lessons from Arabidopsis to crops. J. Exp. Bot. 68, 2513–2529.

     Not in our library10.1093/jxb/erw365 (opens in a new tab)

116. 116.

     Heessen S. Masucci M. G. Dantuma N. P. (2005 ). The UBA2 domain functions as an intrinsic stabilization signal that protects Rad23 from proteasomal degradation. Mol. Cell 18, 225–235.

     Not in our library10.1016/j.molcel.2005.03.015 (opens in a new tab)

117. 117.

     Heinemeyer W. Fischer M. Krimmer T. Stachon U. Wolf D. H. (1997 ). The active sites of the eukaryotic 20S proteasome and their involvement in subunit precursor processing. J. Biol. Chem. 272, 25200–25209.

     Not in our library10.1074/jbc.272.40.25200 (opens in a new tab)

118. 118.

     Heinen C. Acs K. Hoogstraten D. Dantuma N. P. (2011 ). C-terminal UBA domains protect ubiquitin receptors by preventing initiation of protein degradation. Nat. Commun. 2, 191.

     Not in our library10.1038/ncomms1179 (opens in a new tab)

119. 119.

     Heink S. Ludwig D. Kloetzel P. M. Krüger E. (2005 ). IFNγ-induced immune adaptation of the proteasome system is an accelerated and transient response. Proc. Natl. Acad. Sci. U.S.A. 102, 9241–9246.

     Not in our library10.1073/pnas.0501711102 (opens in a new tab)

120. 120.

     Hershko A. Ciechanover A. Heller H. Haas A. L. Rose I. A. (1980 ). Proposed role of ATP in protein breakdown: conjugation of proteins with multiple chains of the polypeptide of ATP-dependent proteolysis. Proc. Natl. Acad. Sci. U.S.A. 77, 1783–1786.

     Not in our library10.1073/pnas.77.4.1783 (opens in a new tab)

121. 121.

     Hershko A. Heller H. Elias S. Ciechanover A. (1983 ). Components of a ubiquitin-protein ligase system: resolution, affinity purification, and roles in protein breakdown. J. Biol. Chem. 258, 8206–8214.

     Not in our library

122. 122.

     Hirano H. Kimura Y. Kimura A. (2016 ). Biological significance of co-and post-translational modifications of the yeast 26S proteasome. J. Proteomics 134, 37–46.

     Not in our library10.1016/j.jprot.2015.11.016 (opens in a new tab)

123. 123.

     Hirano Y. Hayashi H. Iemura S. Hendil K. B. Niwa S. Kishimoto T. (2006 ). Co-operation of multiple chaperones required for the assembly of mammalian 20S proteasomes. Mol. Cell 24, 977–984.

     Not in our library10.1016/j.molcel.2006.11.015 (opens in a new tab)

124. 124.

     Hirano Y. Hendil K. B. Yashiroda H. Iemura S. Nagane R. Hioki Y.. (2005 ). A heterodimeric complex that promotes the assembly of mammalian 20S proteasomes. Nature 437, 1381–1385.

     Not in our library10.1038/nature04106 (opens in a new tab)

125. 125.

     Hirano Y. Kaneko T. Okamoto K. Bai M. Yashiroda H. Furuyama K.. (2008 ). Dissecting the β-ring assembly pathway of the mammalian 20S proteasome. EMBO J. 27, 2204–2213.

     Not in our library10.1038/emboj.2008.148 (opens in a new tab)

126. 126.

     Hisamatsu H. Shimbara N. Saito Y. Kristensen P. Hendil K. B. Fujiwara T.. (1996 ). Newly identified pair of proteasomal subunits regulated reciprocally by interferon-γ. J. Exp. Med. 183, 1807–1816.

     Not in our library10.1084/jem.183.4.1807 (opens in a new tab)

127. 127.
     UBQLN2 Mediates Autophagy-Independent Protein Aggregate Clearance by the Proteasome · 2016

     No notice
128. 128.

     Hofmann K. Bucher P. (1996 ). The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway. Trends Biochem. Sci. 21, 172–173.

     Not in our library10.1016/s0968-0004(96)30015-7 (opens in a new tab)

129. 129.

     Hofmann K. Falquet L. (2001 ). A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systems. Trends Biochem. Sci. 26, 347–350.

     Not in our library10.1016/s0968-0004(01)01835-7 (opens in a new tab)

130. 130.

     Howell L. A. Tomko R. J. Kusmierczyk A. R. (2017 ). Putting it all together: intrinsic and extrinsic mechanisms governing proteasome biogenesis. Front. Biol. 12, 19–48.

     Not in our library10.1007/s11515-017-1439-1 (opens in a new tab)

131. 131.

     Hua Z. Vierstra R. D. (2011 ). The cullin-RING ubiquitin-protein ligases. Annu. Rev. Plant Biol. 62, 299–334.

     Not in our library10.1146/annurev-arplant-042809-112256 (opens in a new tab)

132. 132.

     Huber E. M. Basler M. Schwab R. Heinemeyer W. Kirk C. J. Groettrup M.. (2012 ). Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity. Cell 148, 727–738.

     Not in our library10.1016/j.cell.2011.12.030 (opens in a new tab)

133. 133.

     Huber E. M. Heinemeyer W. Li X. Arendt C. S. Hochstrasser M. Groll M. (2016 ). A unified mechanism for proteolysis and autocatalytic activation in the 20S proteasome. Nat. Commun. 7, 10900.

     Not in our library10.1038/ncomms10900 (opens in a new tab)

134. 134.

     Husnjak K. Dikic I. (2012 ). Ubiquitin-binding proteins: decoders of ubiquitin-mediated cellular function. Annu. Rev. Biochem. 81, 291–322.

     Not in our library10.1146/annurev-biochem-051810-094654 (opens in a new tab)

135. 135.

     Husnjak K. Elsasser S. Zhang N. Chen X. Randles L. Shi Y.. (2008 ). Proteasome subunit Rpn13 is a novel ubiquitin receptor. Nature 453, 481–488.

     Not in our library10.1038/nature06926 (opens in a new tab)

136. 136.

     Hutten S. Kehlenbach R. H. (2007 ). CRM1-mediated nuclear export: to the pore and beyond. Trends Cell Biol. 17, 193–201.

     Not in our library10.1016/j.tcb.2007.02.003 (opens in a new tab)

137. 137.

     Imai J. Maruya M. Yashiroda H. Yahara I. Tanaka K. (2003 ). The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome EMBO J. 22, 3557–3567.

     Not in our library10.1093/emboj/cdg349 (opens in a new tab)

138. 138.

     Isasa M. Katz E. J. Kim W. Yugo V. González S. Kirkpatrick D. S. (2010 ). Mono-ubiquitination of RPN10 regulates substrate recruitment to the proteasome. Mol. Cell 38, 733–745.

     Not in our library10.1016/j.molcel.2010.05.001 (opens in a new tab)

139. 139.

     Ishii K. Noda M. Yagi H. Thammaporn R. Seetaha S. Satoh T.. (2015 ). Disassembly of the self-assembled, double-ring structure of proteasome α7 homo-tetradecamer by α6. Sci. Rep. 5, 18167.

     Not in our library10.1038/srep18167 (opens in a new tab)

140. 140.

     Isono E. Nishihara K. Saeki Y. Yashiroda H. Kamata N. Ge L.. (2007 ). The assembly pathway of the 19S regulatory particle of the yeast 26S proteasome. Mol. Biol. Cell 569–580.

     Not in our library10.1091/mbc.e06-07-0635 (opens in a new tab)

141. 141.

     Iwafune Y. Kawasaki H. Hirano H. (2002 ). Electrophoretic analysis of phosphorylation of the yeast 20S proteasome. Electrophoresis 23, 329–338.

     Not in our library10.1002/1522-2683(200202)23:2<329::aid-elps329>3.0.co;2-1 (opens in a new tab)

142. 142.

     Jacobson A. D. MacFadden A. Wu Z. Peng J. Liu C. W. (2014 ). Auto-regulation of the 26S proteasome by in situ ubiquitination. Mol. Biol. Cell 25, 1824–1835.

     Not in our library10.1091/mbc.e13-10-0585 (opens in a new tab)

143. 143.

     Ju D. Xie Y. (2004 ). Proteasomal degradation of Rpn4 via two distinct mechanisms, ubiquitin-dependent and -independent. J. Biol. Chem. 279, 23851–23854.

     Not in our library10.1074/jbc.c400111200 (opens in a new tab)

144. 144.

     Ju D. Xie Y. (2006 ). Identification of the preferential ubiquitination site and ubiquitin-dependent degradation signal of Rpn4. J. Biol. Chem. 281, 10657–10662.

     Not in our library10.1074/jbc.m513790200 (opens in a new tab)

145. 145.

     Ju D. Xu H. Wang X. Xie Y. (2007 ). Ubiquitin-mediated degradation of Rpn4 is controlled by a phosphorylation-dependent ubiquitylation signal. Biochim. Biophys. Acta 1773, 1672–1680.

     Not in our library10.1016/j.bbamcr.2007.04.012 (opens in a new tab)

146. 146.

     Kaganovich D. Kopito R. Frydman J. (2008 ). Mis-folded proteins partition between two distinct quality control compartments. Nature 454, 1088–1095.

     Not in our library10.1038/nature07195 (opens in a new tab)

147. 147.

     Kaneko T. Hamazaki J. Iemura S. Sasaki K. Furuyama K. Natsume T. (2009 ). Assembly pathway of the mammalian proteasome base sub-complex is mediated by multiple specific chaperones. Cell 137, 914–925.

     Not in our library10.1016/j.cell.2009.05.008 (opens in a new tab)

148. 148.

     Kawamata T. Horie T. Matsunami M. Sasaki M. Ohsumi Y. (2017 ). Zinc starvation induces autophagy in yeast. J. Biol. Chem. 292, 8520–8530.

     Not in our library10.1074/jbc.m116.762948 (opens in a new tab)

149. 149.

     Khaminets A. Behl C. Dikic I. (2016 ). Ubiquitin-dependent and -independent signals in selective autophagy. Trends Cell Biol. 26, 6–16.

     Not in our library10.1016/j.tcb.2015.08.010 (opens in a new tab)

150. 150.

     Kikuchi J. Iwafune Y. Akiyama T. Okayama A. Nakamura H. Arakawa N.. (2010 ). Co- and post-translational modifications of the 26S proteasome in yeast. Proteomics 10, 2769–2779.

     Not in our library10.1002/pmic.200900283 (opens in a new tab)

151. 151.

     Kim D. Y. Scalf M. Smith L. M. Vierstra R. D. (2013 ). Advanced proteomic analyses yield a deep catalog of ubiquitylation targets in Arabidopsis. Plant Cell 25, 1523–1540.

     Not in our library10.1105/tpc.112.108613 (opens in a new tab)

152. 152.

     Kim S. Y. Kim S. G. Kim Y. S. Seo P. J. Bae M. Yoon H. K.. (2007 ). Exploring membrane-associated NAC transcription factors in Arabidopsis: implications for membrane biology in genome regulation. Nucleic Acids Res. 35, 203–213.

     Not in our library10.1093/nar/gkl1068 (opens in a new tab)

153. 153.

     Kimura A. Kato Y. Hirano H. (2012 ). N-myristoylation of the Rpt2 subunit regulates intracellular localization of the yeast 26S proteasome. Biochemistry 51, 8856–8866.

     Not in our library10.1021/bi3007862 (opens in a new tab)

154. 154.

     Kimura A. Kurata Y. Nakabayashi J. Kagawa H. Hirano H. (2016 ). N-myristoylation of the Rpt2 subunit of the yeast 26S proteasome is implicated in the subcellular compartment-specific protein quality control system. J. Proteomics 130, 33–41.

     Not in our library10.1016/j.jprot.2015.08.021 (opens in a new tab)

155. 155.

     Kimura Y. Kurata Y. Ishikawa A. Okayama A. Kamita M. Hirano H. (2013 ). N-terminal methylation of proteasome subunit Rpt1 in yeast. Proteomics 13, 3167–3174.

     Not in our library10.1002/pmic.201300207 (opens in a new tab)

156. 156.

     Kincaid E. Z. Che J. W. York I. Escobar H. Reyes-Vargas E. Delgado J. C.. (2011 ). Mice completely lacking immunoproteasomes show major changes in antigen presentation. Nat. Immunol. 13, 129–135.

     Not in our library10.1038/ni.2203 (opens in a new tab)

157. 157.

     Kingsbury D. J. Griffin T. A. Colbert R. A. (2000 ). Novel propeptide function in 20S proteasome assembly influences β-subunit composition. J. Biol. Chem. 275, 24156–24162.

     Not in our library10.1074/jbc.m001742200 (opens in a new tab)

158. 158.

     Kirisako T. Kamei K. Murata S. Kato M. Fukumoto H. Kanie M.. (2006 ). A ubiquitin ligase complex assembles linear poly-ubiquitin chains. EMBO J. 25, 4877–4887.

     Not in our library10.1038/sj.emboj.7601360 (opens in a new tab)

159. 159.

     Kisselev A. F. Akopian T. N. Castillo V. Goldberg A. L. (1999 ). Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown. Mol. Cell 4, 395–402.

     Not in our library10.1016/s1097-2765(00)80341-x (opens in a new tab)

160. 160.

     Kisselev A. F. Garcia-Calvo M. Overkleeft H. S. Peterson E. Pennington M. W. Ploegh H. L.. (2003 ). The caspase-like sites of proteasomes, their substrate specificity, new inhibitors and substrates, and allosteric interactions with the trypsin-like sites. J. Biol. Chem. 278, 35869–35877.

     Not in our library10.1074/jbc.m303725200 (opens in a new tab)

161. 161.

     Kleijnen M. F. Roelofs J. Park S. Hathaway N. A. Glickman M. H. King R. W.. (2007 ). Stability of the proteasome can be regulated allosterically through engagement of its proteolytic active sites. Nat. Struct. Mol. Biol. 14, 1180–1188.

     Not in our library10.1038/nsmb1335 (opens in a new tab)

162. 162.

     Klionsky D. J. Schulman B. A. (2014 ). Dynamic regulation of macroautophagy by distinctive ubiquitin-like proteins. Nat. Struct. Mol. Biol. 21, 336–345.

     Not in our library10.1038/nsmb.2787 (opens in a new tab)

163. 163.

     Kock M. Nunes M. M. Hemann M. Kube S. Dohmen R. J. Herzog F.. (2015 ). Proteasome assembly from 15S precursors involves major conformational changes and recycling of the Pba1-Pba2 chaperone. Nat. Commun. 6, 6123.

     Not in our library10.1038/ncomms7123 (opens in a new tab)

164. 164.

     Köhler A. Cascio P. Leggett D. S. Woo K. M. Goldberg A. L. Finley D. (2001 ). The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release. Mol. Cell 7, 1143–1152.

     Not in our library10.1016/s1097-2765(01)00274-x (opens in a new tab)

165. 165.

     Koizumi S. Hamazaki J. Murata S. (2018 ). Transcriptional regulation of the 26S proteasome by Nrf1. Proc. Jpn. Acad. Ser. B Phys. Biol. Sci. 94, 325–336.

     Not in our library10.2183/pjab.94.021 (opens in a new tab)

166. 166.
     The aspartyl protease DDI2 activates Nrf1 to compensate for proteasome dysfunction · 2016

     No notice
167. 167.

     Kraft C. Deplazes A. Sohrmann M. Peter M. (2008 ). Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease. Nat. Cell Biol. 10, 602–610.

     Not in our library10.1038/ncb1723 (opens in a new tab)

168. 168.

     Kragelund B. B. Schenstrøm S. M. Rebula C. A. Panse V. G. Hartmann-Petersen R. (2016 ). DSS1/Sem1, a multifunctional and intrinsically disordered protein. Trends Biochem. Sci. 41, 446–459.

     Not in our library10.1016/j.tibs.2016.02.004 (opens in a new tab)

169. 169.

     Kravtsova-Ivantsiv Y. Ciechanover A. (2012 ). Non-canonical ubiquitin-based signals for proteasomal degradation. J. Cell Sci. 125, 539–548.

     Not in our library10.1242/jcs.093567 (opens in a new tab)

170. 170.

     Krick R. Muehe Y. Prick T. Bremer S. Schlotterhose P. Eskelinen E. L.. (2008 ). Piecemeal microautophagy of the nucleus requires the core macroautophagy genes. Mol. Biol. Cell 19, 4492–4505.

     Not in our library10.1091/mbc.e08-04-0363 (opens in a new tab)

171. 171.

     Kriegenburg F. Seeger M. Saeki Y. Tanaka K. Lauridsen A. M. Hartmann-Petersen R.. (2008 ). Mammalian 26S proteasomes remain intact during protein degradation. Cell 135, 355–365.

     Not in our library10.1016/j.cell.2008.08.032 (opens in a new tab)

172. 172.

     Kusmierczyk A. R. Kunjappu M. J. Funakoshi M. Hochstrasser M. (2008 ). A multimeric assembly factor controls the formation of alternative 20S proteasomes. Nat. Struct. Mol. Biol. 15, 237–244.

     Not in our library10.1038/nsmb.1389 (opens in a new tab)

173. 173.

     Kusmierczyk A. R. Kunjappu M. J. Kim R. Y. Hochstrasser M. (2011 ). A conserved 20S proteasome assembly factor requires a C-terminal HbYX motif for proteasomal precursor binding. Nat. Struct. Mol. Biol. 18, 622–629.

     Not in our library10.1038/nsmb.2027 (opens in a new tab)

174. 174.

     Lander G. C. Estrin E. Matyskiela M. E. Bashore C. Nogales E. Martin A. (2012 ). Complete subunit architecture of the proteasome regulatory particle. Nature 482, 186–191.

     Not in our library10.1038/nature10774 (opens in a new tab)

175. 175.

     Laporte D. Salin B. Daignan-Fornier B. Sagot I. (2008 ). Reversible cytoplasmic localization of the proteasome in quiescent yeast cells. J. Cell Biol. 181, 737–745.

     Not in our library10.1083/jcb.200711154 (opens in a new tab)

176. 176.

     Lasker K. Förster F. Bohn S. Walzthoeni T. Villa E. Unverdorben P.. (2012 ). Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach. Proc. Natl. Acad. Sci. U.S.A. 109, 1380–1387.

     Not in our library10.1073/pnas.1120559109 (opens in a new tab)

177. 177.

     Le Guerroué F. Eck F. Jung J. Starzetz T. Mittelbronn M. Kaulich M. (2017 ). Autophagosomal content profiling reveals an LC3-dependent piecemeal mitophagy pathway. Mol. Cell 68, 786–796.

     Not in our library10.1016/j.molcel.2017.10.029 (opens in a new tab)

178. 178.

     Le Tallec B. Barrault M. B. Courbeyrette R. Guérois R. Marsolier-Kergoat M. C. Peyroche A. (2007 ). 20S proteasome assembly is orchestrated by two distinct pairs of chaperones in yeast and in mammals. Mol. Cell 27, 660–674.

     Not in our library10.1016/j.molcel.2007.06.025 (opens in a new tab)

179. 179.

     Le Tallec B. Barrault M. B. Guérois R. Carré T. Peyroche A. (2009 ). Hsm3/S5b participates in the assembly pathway of the 19S regulatory particle of the proteasome. Mol. Cell 33, 389–399.

     Not in our library10.1016/j.molcel.2009.01.010 (opens in a new tab)

180. 180.

     Lee B. H. Lu Y. Prado M. A. Shi Y. Tian G. Sun S.. (2016 ). USP14 deubiquitinates proteasome-bound substrates that are ubiquitinated at multiple sites. Nature 532, 398–401.

     Not in our library10.1038/nature17433 (opens in a new tab)

181. 181.

     Lee C. Schwartz M. P. Prakash S. Iwakura M. Matouschek A. (2001 ). ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal. Mol. Cell 7, 627–637.

     Not in our library10.1016/s1097-2765(01)00209-x (opens in a new tab)

182. 182.

     Lee C. S. Lee C. Hu T. Nguyen J. M. Zhang J. Martin M. V. (2011 ). Loss of nuclear factor E2-related factor 1 in the brain leads to mis-regulation of proteasome gene expression and neurodegeneration. Proc. Natl. Acad. Sci. U.S.A. 108, 8408–8413.

     Not in our library10.1073/pnas.1019209108 (opens in a new tab)

183. 183.

     Lee S. Y. De La Mota-Peynado A. Roelofs J. (2011 ). Loss of Rpt5 protein interactions with the core particle and Nas2 protein causes the formation of faulty proteasomes that are inhibited by Ecm29. J. Biol. Chem. 286, 36641–36651.

     Not in our library10.1074/jbc.m111.280875 (opens in a new tab)

184. 184.

     Leggett D. S. Glickman M. H. Finley D. (2005 ). Purification of proteasomes, proteasome sub-complexes and proteasome-associated proteins from budding yeast. Methods Mol. Biol. 301, 57–70.

     Not in our library10.1385/1-59259-895-1:057 (opens in a new tab)

185. 185.

     Leggett D. S. Hanna J. Borodovsky A. Crosas B. Schmidt M. Baker R. T.. (2002 ). Multiple associated proteins regulate proteasome structure and function. Mol. Cell 10, 495–507.

     Not in our library10.1016/s1097-2765(02)00638-x (opens in a new tab)

186. 186.

     Lehmann A. Janek K. Braun B. Kloetzel P. M. Enenkel C. (2002 ). 20S proteasomes are imported as precursor complexes into the nucleus of yeast. J. Mol. Biol. 317, 401–413.

     Not in our library10.1006/jmbi.2002.5443 (opens in a new tab)

187. 187.

     Lehmann A. Jechow K. Enenkel C. (2008 ). Blm10 binds to pre-activated proteasome core particles with open gate conformation. EMBO Rep. 9, 1237–1243.

     Not in our library10.1038/embor.2008.190 (opens in a new tab)

188. 188.

     Lehmann A. Niewienda A. Jechow K. Janek K. Enenkel C. (2010 ). Ecm29 fulfills quality control functions in proteasome assembly. Mol. Cell 38, 879–888.

     Not in our library10.1016/j.molcel.2010.06.016 (opens in a new tab)

189. 189.

     Lehrbach N. J. Breen P. C. Ruvkun G. (2019 ). Protein sequence editing of SKN-1A/Nrf1 by peptide:N-glycanase controls proteasome gene expression. Cell 177, 737–750.

     Not in our library10.1016/j.cell.2019.03.035 (opens in a new tab)

190. 190.
     Proteasome dysfunction triggers activation of SKN-1A/Nrf1 by the aspartic protease DDI-1 · 2016

     No notice
191. 191.

     Lehrbach N. J. Ruvkun G. (2019 ). Endoplasmic reticulum-associated SKN-1A/Nrf1 mediates a cytoplasmic unfolded protein response and promotes longevity. eLife 8:44425.

     Not in our library10.7554/elife.44425 (opens in a new tab)

192. 192.

     Levine B. Kroemer G. (2019 ). Biological functions of autophagy genes: a disease perspective. Cell 176, 11–42.

     Not in our library10.1016/j.cell.2018.09.048 (opens in a new tab)

193. 193.

     Li F. Chung T. Pennington J. G. Federico M. L. Kaeppler H. F. Kaeppler S. M. (2015 ). Autophagic recycling plays a central role in maize nitrogen re-mobilization. Plant Cell 27, 1389–1408.

     Not in our library10.1105/tpc.15.00158 (opens in a new tab)

194. 194.

     Li J. Rechsteiner M. (2001 ). Molecular dissection of the 11S REG (PA28) proteasome activators. Biochimie 83, 373–383.

     Not in our library10.1016/s0300-9084(01)01236-6 (opens in a new tab)

195. 195.

     Li N. Xu R. Li Y. (2019 ). Molecular networks of seed size control in plants. Annu. Rev. Plant Biol. 70, 435–463.

     Not in our library10.1146/annurev-arplant-050718-095851 (opens in a new tab)

196. 196.

     Li X. Kusmierczyk A. R. Wong P. Emili A. Hochstrasser M. (2007 ). β-subunit appendages promote 20S proteasome assembly by overcoming an Ump1-dependent checkpoint. EMBO J. 26, 2339–2349.

     Not in our library10.1038/sj.emboj.7601681 (opens in a new tab)

197. 197.

     Li X. Li Y. Arendt C. S. Hochstrasser M. (2016 ). Distinct elements in the proteasomal β5 subunit propeptide required for autocatalytic processing and proteasome assembly. J. Biol. Chem. 291, 1991–2003.

     Not in our library10.1074/jbc.m115.677047 (opens in a new tab)

198. 198.

     Li X. Thompson D. Kumar B. DeMartino G. M. (2014 ). Molecular and cellular roles of PI31 (PSMF1) protein in regulation of proteasome function. J. Biol. Chem. 289, 17392–17405.

     Not in our library10.1074/jbc.m114.561183 (opens in a new tab)

199. 199.

     Liang R. Y. Chen L. Ko B. T. Shen Y. H. Li Y. T. Chen B. R.. (2014 ). Rad23 interaction with the proteasome is regulated by phosphorylation of its ubiquitin-like domain. J. Mol. Biol. 426, 4049–4060.

     Not in our library10.1016/j.jmb.2014.10.004 (opens in a new tab)

200. 200.

     Lipinszki Z. Kovács L. Deák P. Udvardy A. (2012 ). Ubiquitylation of Drosophila p54/Rpn10/S5a regulates its interaction with the UBL-UBA poly-ubiquitin receptors. Biochemistry 51, 2461–2470.

     Not in our library10.1021/bi3001006 (opens in a new tab)

201. 201.

     Liu C. W. Li X. Thompson D. Wooding K. Chang T. L. Tang Z.. (2006 ). ATP binding and ATP hydrolysis play distinct roles in the function of the 26S proteasome. Mol. Cell 24, 39–50.

     Not in our library10.1016/j.molcel.2006.08.025 (opens in a new tab)

202. 202.

     Livnat-Levanon N. Kevel É. Kleifeld O. Krutauz D. Segref A. Rinaldi T.. (2014 ). Reversible 26S proteasome disassembly upon mitochondrial stress. Cell Rep. 7, 1371–1380.

     Not in our library10.1016/j.celrep.2014.04.030 (opens in a new tab)

203. 203.

     Lokireddy S. Kukushkin N. V. Goldberg A. L. (2015 ). cAMP-induced phosphorylation of 26S proteasomes on Rpn6/PSMD11 enhances their activity and the degradation of mis-folded proteins. Proc. Natl. Acad. Sci. U.S.A. 112, 7176–7185.

     Not in our library10.1073/pnas.1522332112 (opens in a new tab)

204. 204.

     Lu H. Zong C. Wang Y. Young G. W. Deng N. Souda P. (2008 ). Revealing the dynamics of the 20S proteasome phosphoproteome: a combined CID and electron transfer dissociation approach. Mol. Cell. Proteomics 7, 2073–2089.

     Not in our library10.1074/mcp.m800064-mcp200 (opens in a new tab)

205. 205.

     Lu K. Psakhye I. Jentsch S. (2014 ). Autophagic clearance of polyQ proteins mediated by ubiquitin-Atg8 adaptors of the conserved CUET protein family. Cell 158, 549–563.

     Not in our library10.1016/j.cell.2014.05.048 (opens in a new tab)

206. 206.

     Lu Y. Lee B. H. King R. W. Finley D. Kirschner M. W. (2015 ). Substrate degradation by the proteasome: a single molecule kinetic analysis. Science 348:1250834.

     Not in our library10.1126/science.1250834 (opens in a new tab)

207. 207.
     Comparative transcriptome profiling analyses during the lag phase uncover YAP1, PDR1, PDR3, RPN4, and HSF1 as key regulatory genes in genomic adaptation to the lignocellulose derived inhibitor HMF for Saccharomyces cerevisiae · 2010

     No notice
208. 208.

     Malinovska L. Kroschwald S. Munder M. C. Richter D. Alberti S. (2012 ). Molecular chaperones and stress-inducible protein sorting factors co-ordinate the spatiotemporal distribution of protein aggregates. Mol. Biol. Cell 23, 3041–3056.

     Not in our library10.1091/mbc.e12-03-0194 (opens in a new tab)

209. 209.

     Manasanch E. E. Orlowski R. Z. (2017 ). Proteasome inhibitors in cancer therapy. Nat. Rev. Clin. Oncol. 14, 417–433.

     Not in our library10.1038/nrclinonc.2016.206 (opens in a new tab)

210. 210.

     Mancias J. D. Wang X. Gygi S. P. Harper J. W. Kimmelman A. C. (2014 ). Quantitative proteomics identifies NCOA4 as the cargo receptor mediating ferritinophagy. Nature 509, 105–109.

     Not in our library10.1038/nature13148 (opens in a new tab)

211. 211.

     Mannhaupt G. Schnall R. Karpov V. Vetter I. Feldmann H. (1999 ). Rpn4p acts as a transcription factor by binding to PACE, a nonomer box found upstream of 26S proteasomal and other genes in yeast. FEBS Lett. 450, 27–34.

     Not in our library10.1016/s0014-5793(99)00467-6 (opens in a new tab)

212. 212.

     Maqbool A. Hughes R. K. Dagdas Y. F. Tregidgo N. Zess E. Belhaj K.. (2016 ). Structural basis of host ATG8 binding by the Irish potato famine pathogen effector protein PexRD54. J. Biol. Chem. 291, 20270–20282.

     Not in our library10.1074/jbc.m116.744995 (opens in a new tab)

213. 213.

     Marques A. J. Glanemann C. Ramos P. C. Dohmen R. J. (2007 ). The C-terminal extension of the β7 subunit and activator complexes stabilize nascent 20S proteasomes and promote their maturation. J. Biol. Chem. 282, 34869–34876.

     Not in our library10.1074/jbc.m705836200 (opens in a new tab)

214. 214.

     Marshall R. S. Gemperline D. C. Vierstra R. D. (2017 ). Purification of 26S proteasomes and their sub-complexes from plants. Methods Mol. Biol. 1511, 301–334.

     Not in our library10.1007/978-1-4939-6533-5_24 (opens in a new tab)

215. 215.

     Marshall R. S. Hua Z. Mali S. McLoughlin F. Vierstra R. D. (2019 ). ATG8-binding UIM proteins define a new class of autophagy adaptors and receptors. Cell 177, 766–781.

     Not in our library10.1016/j.cell.2019.02.009 (opens in a new tab)

216. 216.

     Marshall R. S. Li F. Gemperline D. C. Book A. J. Vierstra R. D. (2015 ). Autophagic degradation of the 26S proteasome is mediated by the dual ATG8/ubiquitin receptor RPN10 in Arabidopsis. Mol. Cell 58, 1053–1066.

     Not in our library10.1016/j.molcel.2015.04.023 (opens in a new tab)

217. 217.

     Marshall R. S. McLoughlin F. Vierstra R. D. (2016 ). Autophagic turnover of inactive 26S proteasomes in yeast is directed by the ubiquitin receptor Cue5 and the Hsp42 chaperone. Cell Rep. 16, 1717–1732.

     Not in our library10.1016/j.celrep.2016.07.015 (opens in a new tab)

218. 218.

     Marshall R. S. Vierstra R. D. (2015 ). Eat or be eaten: the autophagic plight of inactive 26S proteasomes. Autophagy 11, 1927–1928.

     Not in our library10.1080/15548627.2015.1078961 (opens in a new tab)

219. 219.

     Marshall R. S. Vierstra R. D. (2018a ). Autophagy: the master of bulk and selective recycling. Annu. Rev. Plant Biol. 69, 173–208.

     Not in our library10.1146/annurev-arplant-042817-040606 (opens in a new tab)

220. 220.

     Marshall R. S. Vierstra R. D. (2018b ). Proteasome storage granules protect proteasomes from autophagic degradation upon carbon starvation. eLife 7:34532.

     Not in our library10.7554/elife.34532 (opens in a new tab)

221. 221.

     McCutchen-Maloney S. L. Matsuda K. Shimbara N. Binns D. D. Tanaka K. Slaughter C. A.. (2000 ). cDNA cloning, expression, and functional characterization of PI31, a proline-rich inhibitor of the proteasome. J. Biol. Chem. 275, 18557–18565.

     Not in our library10.1074/jbc.m001697200 (opens in a new tab)

222. 222.

     McLoughlin F. Augustine R. C. Marshall R. S. Li F. Kirkpatrick L. D. Otegui M. S. (2018 ). Maize multi-omics reveal roles for autophagic recycling in proteome re-modelling and lipid turnover. Nat. Plants 4, 1056–1070.

     Not in our library10.1038/s41477-018-0299-2 (opens in a new tab)

223. 223.

     Meiners S. Heyken D. Weller A. Ludwig A. Stangl K. Kloetzel P. M.. (2003 ). Inhibition of proteasome activity induces concerted expression of proteasome genes and de novo formation of mammalian proteasomes. J. Biol. Chem. 278, 21517–21525.

     Not in our library10.1074/jbc.m301032200 (opens in a new tab)

224. 224.

     Mijaljica D. Prescott M. Devenish R. J. (2012 ). A late form of nucleophagy in Saccharomyces cerevisiae. PLoS ONE 7:e40013.

     Not in our library10.1371/journal.pone.0040013 (opens in a new tab)

225. 225.

     Miller S. B. Mogk A. Bukau B. (2015 ). Spatially organized aggregation of mis-folded proteins as a cellular stress defense strategy. J. Mol. Biol. 427, 1564–1574.

     Not in our library10.1016/j.jmb.2015.02.006 (opens in a new tab)

226. 226.

     Mochida K. Oikawa Y. Kimura Y. Kirisako H. Hirano H. Ohsumi Y.. (2015 ). Receptor-mediated selective autophagy degrades the endoplasmic reticulum and the nucleus. Nature 522, 359–362.

     Not in our library10.1038/nature14506 (opens in a new tab)

227. 227.

     Morishita T. Kojima Y. Maruta T. Nishizawa-Yokoi A. Yabuta Y. Shigeoka S. (2009 ). An Arabidopsis NAC transcription factor, ANAC078, regulates flavonoid biosynthesis under high light. Plant Cell Physiol. 50, 2210–2222.

     Not in our library10.1093/pcp/pcp159 (opens in a new tab)

228. 228.

     Murata S. Sasaki K. Kishimoto T. Niwa S. Hayashi H. Takahama Y.. (2007 ). Regulation of CD8+ T-cell development by thymus-specific proteasomes. Science 316, 1349–1353.

     Not in our library10.1126/science.1141915 (opens in a new tab)

229. 229.

     Murata S. Takahama Y. Kasahara M. Tanaka K. (2018 ). The immunoproteasome and thymoproteasome: functions, evolution and human disease. Nat. Immunol. 19, 923–931.

     Not in our library10.1038/s41590-018-0186-z (opens in a new tab)

230. 230.

     Nahar A. Fu X. Polovin G. Orth J. D. Park S. (2019 ). Two alternative mechanisms regulate the onset of chaperone-mediated assembly of the proteasomal ATPases. J. Biol. Chem. 294, 6562–6577.

     Not in our library10.1074/jbc.ra118.006298 (opens in a new tab)

231. 231.

     Nandi D. Woodward E. Ginsburg D. B. Monaco J. J. (1997 ). Intermediates in the formation of mouse 20S proteasomes: implications for the assembly of precursor β-subunits. EMBO J. 16, 5363–5375.

     Not in our library10.1093/emboj/16.17.5363 (opens in a new tab)

232. 232.

     Nederlof P. M. Wang H. R. Baumeister W. (1995 ). Nuclear localization signals of human and Thermoplasma proteasomal α-subunits are functional in vitro. Proc. Natl. Acad. Sci. U.S.A. 92, 12060–12064.

     Not in our library10.1073/pnas.92.26.12060 (opens in a new tab)

233. 233.

     Nemec A. A. Howell L. A. Peterson A. K. Murray M. A. Tomko R. J. (2017 ). Autophagic clearance of proteasomes in yeast requires the conserved sorting nexin Snx4. J. Biol. Chem. 292, 21466–21480.

     Not in our library10.1074/jbc.m117.817999 (opens in a new tab)

234. 234.

     Nemec A. A. Peterson A. K. Warnock J. L. Reed R. G. Tomko R. J. (2019 ). An allosteric interaction network promotes conformation state-dependent eviction of the Nas6 assembly chaperone from nascent 26S proteasomes. Cell Rep. 26, 483–495.

     Not in our library10.1016/j.celrep.2018.12.042 (opens in a new tab)

235. 235.

     Nguyen H. M. Schippers J. H. Gõni-Ramos O. Christoph M. P. Dortay H. van der Hoorn R. A.. (2013 ). An upstream regulator of the 26S proteasome modulates organ size in Arabidopsis thaliana. Plant J. 74, 25–36.

     Not in our library10.1111/tpj.12097 (opens in a new tab)

236. 236.

     Nice D. C. Sato T. K. Stromhaug P. E. Emr S. D. Klionsky D. J. (2002 ). Co-operative binding of the cytoplasm-to-vacuole targeting pathway proteins Cvt13 and Cvt20 to phosphatidylinositol-3-phosphate at the pre-autophagosomal structure is required for selective autophagy. J. Biol. Chem. 277, 30198–30207.

     Not in our library10.1074/jbc.m204736200 (opens in a new tab)

237. 237.

     Nickell S. Beck F. Scheres S. H. Korinke A. Förster F. Lasker K.. (2009 ). Insights into the molecular architecture of the 26S proteasome. Proc. Natl. Acad. Sci. U.S.A. 106, 11943–11947.

     Not in our library10.1073/pnas.0905081106 (opens in a new tab)

238. 238.

     Nishizawa A. Yabuta Y. Yoshida E. Maruta T. Yoshimura K. Shigeoka S. (2006 ). Arabidopsis heat shock transcription factor A2 as a key regulator in response to several types of environmental stress. Plant J. 48, 535–547.

     Not in our library10.1111/j.1365-313x.2006.02889.x (opens in a new tab)

239. 239.

     Noda N. N. Kumeta H. Nakatogawa H. Satoo K. Adachi W. Ishii J.. (2008 ). Structural basis of target recognition by Atg8/LC3 during selective autophagy. Genes Cells 13, 1211–1218.

     Not in our library10.1111/j.1365-2443.2008.01238.x (opens in a new tab)

240. 240.

     Noda N. N. Ohsumi Y. Inagaki F. (2010 ). An Atg8 family interacting motif crucial for selective autophagy. FEBS Lett. 584, 1379–1385.

     Not in our library10.1016/j.febslet.2010.01.018 (opens in a new tab)

241. 241.

     Nussbaum A. K. Dick T. P. Keilholz W. Schirle M. Stefanović S. Dietz K.. (1998 ). Cleavage motifs of the yeast 20S proteasome β-subunits deduced from digests of enolase 1. Proc. Natl. Acad. Sci. U.S.A. 95, 12504–12509.

     Not in our library10.1073/pnas.95.21.12504 (opens in a new tab)

242. 242.

     Oh E. Akopian D. Rape M. (2018 ). Principles of ubiquitin-dependent signaling. Annu. Rev. Cell Dev. Biol. 34, 137–162.

     Not in our library10.1146/annurev-cellbio-100617-062802 (opens in a new tab)

243. 243.

     Ohsumi Y. (2001 ). Molecular dissection of autophagy: two ubiquitin-like systems. Nat. Rev. Mol. Cell Biol. 2, 211–216.

     Not in our library10.1038/35056522 (opens in a new tab)

244. 244.
     The Cdc48 unfoldase prepares well-folded protein substrates for degradation by the 26S proteasome · 2019

     No notice
245. 245.

     Owsianik G. Balzi L. Ghislain M. (2002 ). Control of 26S proteasome expression by transcription factors regulating multi-drug resistance in Saccharomyces cerevisiae. Mol. Microbiol. 43, 1295–1308.

     Not in our library10.1046/j.1365-2958.2002.02823.x (opens in a new tab)

246. 246.

     Pack C. G. Yukii H. Toh-e A. Kudo T. Tsuchiya H. Kaiho A.. (2014 ). Quantitative live-cell imaging reveals spatio-temporal dynamics and cytoplasmic assembly of the 26S proteasome. Nat. Commun. 5:3396.

     Not in our library10.1038/ncomms4396 (opens in a new tab)

247. 247.

     Padmanabhan A. Vuong S. A. Hochstrasser M. (2016 ). Assembly of an evolutionarily conserved alternative proteasome isoform in human cells. Cell Rep. 14, 2962–2974.

     Not in our library10.1016/j.celrep.2016.02.068 (opens in a new tab)

248. 248.

     Panasenko O. O. Collart M. A. (2011 ). Not4 E3 ligase contributes to proteasome assembly and functional integrity in part through Ecm29. Mol. Cell. Biol. 31, 1610–1623.

     Not in our library10.1128/mcb.01210-10 (opens in a new tab)

249. 249.

     Panasenko O. O. Somasekharan S. P. Villanyi Z. Zagatti M. Bezrukov F. Rashpa R.. (2019 ). Co-translational assembly of proteasome subunits in NOT1-containing assemblysomes. Nat. Struct. Mol. Biol. 26, 110–120.

     Not in our library10.1038/s41594-018-0179-5 (opens in a new tab)

250. 250.

     Pante N. Kann M. (2002 ). The nuclear pore complex is able to transport macromolecules with diameters of about 39 nm. Mol. Biol. Cell 13, 425–434.

     Not in our library10.1091/mbc.01-06-0308 (opens in a new tab)

251. 251.

     Paraskevopoulos K. Kriegenburg F. Tatham M. H. Rösner H. I. Medina B. Larsen I. B.. (2014 ). Dss1 is a 26S proteasome ubiquitin receptor. Mol. Cell 56, 453–461.

     Not in our library10.1016/j.molcel.2014.09.008 (opens in a new tab)

252. 252.

     Park S. Kim W. Tian G. Gygi S. P. Finley D. (2011 ). Structural defects in the regulatory particle-core particle interface of the proteasome induce a novel proteasome stress response. J. Biol. Chem. 286, 36652–36666.

     Not in our library10.1074/jbc.m111.285924 (opens in a new tab)

253. 253.

     Park S. Li X. Kim H. M. Singh C. R. Tian G. Hoyt M. A. (2013 ). Re-configuration of the proteasome during chaperone-mediated assembly. Nature 497, 512–516.

     Not in our library10.1038/nature12123 (opens in a new tab)

254. 254.

     Park S. Roelofs J. Kim W. Robert J. Schmidt M. Gygi S. P.. (2009 ). Hexameric assembly of the proteasomal ATPases is templated through their C-termini. Nature 459, 866–870.

     Not in our library10.1038/nature08065 (opens in a new tab)

255. 255.

     Parzych K. R. Klionsky D. J. (2018 ). Vacuolar hydrolysis and efflux: current knowledge and unanswered questions. Autophagy 15, 212–227.

     Not in our library10.1080/15548627.2018.1545821 (opens in a new tab)

256. 256.

     Pathare G. R. Nagy I. Bohn S. Unverdorben P. Hubert A. Körner R. (2012 ). The proteasomal subunit Rpn6 is a molecular clamp holding the core and regulatory sub-complexes together. Proc. Natl. Acad. Sci. U.S.A. 109, 149–154.

     Not in our library10.1073/pnas.1117648108 (opens in a new tab)

257. 257.

     Pathare G. R. Nagy I. Sledz P. Anderson D. J. Zhou H. J. Pardon E.. (2014 ). Crystal structure of the proteasomal deubiquitylation module Rpn8-Rpn11. Proc. Natl. Acad. Sci. U.S.A. 111, 2984–2989.

     Not in our library10.1073/pnas.1400546111 (opens in a new tab)

258. 258.

     Peters L. Z. Hazan R. Breker M. Schuldiner M. Ben-Aroya S. (2013 ). Formation and dissociation of proteasome storage granules are regulated by cytosolic pH. J. Cell Biol. 201, 663–671.

     Not in our library10.1083/jcb.201211146 (opens in a new tab)

259. 259.

     Peters L. Z. Karmon O. David-Kadoch G. Hazan R. Yu T. Glickman M. H. (2015 ). The protein quality control machinery regulates mis-assembled proteasome subunits. PLoS Genet. 11, e1005178

     Not in our library10.1371/journal.pgen.1005178 (opens in a new tab)

260. 260.

     Peters L. Z. Karmon O. Miodownik S. Ben-Aroya S. (2016 ). Proteasome storage granules are transiently associated with the insoluble protein deposit in Saccharomyces cerevisiae. J. Cell Sci. 129, 1190–1197.

     Not in our library10.1242/jcs.179648 (opens in a new tab)

261. 261.

     Peth A. Kukushkin N. V. Bossé M. Goldberg A. L. (2013a ). Ubiquitinated proteins activate the proteasomal ATPases by binding to Usp14 or Uch37 homologs. J. Biol. Chem. 288, 7781–7790.

     Not in our library10.1074/jbc.m112.441907 (opens in a new tab)

262. 262.

     Peth A. Nathan J. A. Goldberg A. L. (2013b ). The ATP costs and time required to degrade ubiquitinated proteins by the 26S proteasome. J. Biol. Chem. 288, 29215–29222.

     Not in our library10.1074/jbc.m113.482570 (opens in a new tab)

263. 263.

     Peth A. Uchiki T. Goldberg A. L. (2010 ). ATP-dependent steps in the binding of ubiquitin conjugates to the 26S proteasome that commit to degradation. Mol. Cell 40, 671–681.

     Not in our library10.1016/j.molcel.2010.11.002 (opens in a new tab)

264. 264.

     Prakash S. Tian L. Ratliff K. S. Lehotzky R. E. Matouschek A. (2004 ). An unstructured initiation site is required for efficient proteasome-mediated degradation. Nat. Struct. Mol. Biol. 11, 830–837.

     Not in our library10.1038/nsmb814 (opens in a new tab)

265. 265.

     Rabl J. Smith D. M. Yu Y. Chang S. C. Goldberg A. L. Cheng Y. (2008 ). Mechanism of gate opening in the 20S proteasome by the proteasomal ATPases. Mol. Cell 30, 360–368.

     Not in our library10.1016/j.molcel.2008.03.004 (opens in a new tab)

266. 266.
     p97-dependent retrotranslocation and proteolytic processing govern formation of active Nrf1 upon proteasome inhibition · 2014

     No notice
267. 267.

     Radhakrishnan S. K. Lee C. S. Young P. Beskow A. Chan J. Y. Deshaies R. J. (2010 ). Transcription factor Nrf1 mediates the proteasome recovery pathway after proteasome inhibition in mammalian cells. Mol. Cell 38, 17–28.

     Not in our library10.1016/j.molcel.2010.02.029 (opens in a new tab)

268. 268.

     Ramachandran K. V. Fu J. M. Schaffer T. B. Na C. H. Delannoy M. Margolis S. S. (2018 ). Activity-dependent degradation of the nascentome by the neuronal membrane proteasome. Mol. Cell 71, 169–177.

     Not in our library10.1016/j.molcel.2018.06.013 (opens in a new tab)

269. 269.

     Ramachandran K. V. Margolis S. S. (2017 ). A mammalian nervous system-specific plasma membrane proteasome complex that moderates neuronal function. Nat. Struct. Mol. Biol. 24, 419–430.

     Not in our library10.1038/nsmb.3389 (opens in a new tab)

270. 270.

     Ramos P. C. Höckendorff J. Johnson E. S. Varshavsky A. Dohmen R. J. (1998 ). Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of assembly. Cell 92, 489–499.

     Not in our library10.1016/s0092-8674(00)80942-3 (opens in a new tab)

271. 271.

     Rape M. (2018 ). Ubiquitylation at the crossroads of development and disease. Nat. Rev. Mol. Cell Biol. 19, 59–70.

     Not in our library10.1038/nrm.2017.83 (opens in a new tab)

272. 272.

     Reggiori F. Klionsky D. J. (2013 ). Autophagic processes in yeast: mechanism, machinery and regulation. Genetics 194, 341–361.

     Not in our library10.1534/genetics.112.149013 (opens in a new tab)

273. 273.

     Reits E. A. Benham A. M. Plougastel B. Neefjes J. Trowsdale J. (1997 ). Dynamics of proteasome distribution in living cells. EMBO J. 16, 6087–6094.

     Not in our library10.1093/emboj/16.20.6087 (opens in a new tab)

274. 274.

     Roberts P. Moshitch-Moshkovitz S. Kvam E. O'Toole E. Winey M. Goldfarb D. S. (2003 ). Piecemeal microautophagy of the nucleus in Saccharomyces cerevisiae. Mol. Biol. Cell 14, 129–141.

     Not in our library10.1091/mbc.e02-08-0483 (opens in a new tab)

275. 275.

     Roelofs J. Park S. Haas W. Tian G. McAllister F. E. Huo Y.. (2009 ). Chaperone-mediated pathway of proteasome regulatory particle assembly. Nature 459, 861–865.

     Not in our library10.1038/nature08063 (opens in a new tab)

276. 276.

     Rogov V. V. Dötsch V. Johansen T. Kirkin V. (2014 ). Interactions between autophagy receptors and ubiquitin-like proteins form the molecular basis for selective autophagy. Mol. Cell 53, 167–178.

     Not in our library10.1016/j.molcel.2013.12.014 (opens in a new tab)

277. 277.

     Rogov V. V. Stolz A. Ravichandran A. C. Rios-Szwed D. O. Suzuki H. Kniss A. (2018 ). Structural and functional analysis of the GABARAP-interacting motif. EMBO Rep. 19, e47268

     Not in our library10.15252/embr.201847268 (opens in a new tab)

278. 278.

     Rousseau A. Bertolotti A. (2016 ). An evolutionarily conserved pathway controls proteasome homeostasis. Nature 536, 184–189.

     Not in our library10.1038/nature18943 (opens in a new tab)

279. 279.

     Rousseau A. Bertolotti A. (2018 ). Regulation of proteasome assembly and activity in health and disease. Nat. Rev. Mol. Cell Biol. 19, 697–712.

     Not in our library10.1038/s41580-018-0040-z (opens in a new tab)

280. 280.

     Ruschak A. M. Religa T. L. Breuer S. Witt S. Kay L. E. (2010 ). The proteasome antechamber maintains substrates in an unfolded state. Nature 467, 868–871.

     Not in our library10.1038/nature09444 (opens in a new tab)

281. 281.

     Russell J. D. Scalf M. Book A. J. Ladror D. T. Vierstra R. D. Smith L. M.. (2013 ). Characterization and quantification of intact 26S proteasome proteins by real-time measurement of intrinsic fluorescence prior to top-down mass spectrometry. PLoS One 8, 58157.

     Not in our library10.1371/journal.pone.0058157 (opens in a new tab)

282. 282.

     Russell S. J. Steger K. A. Johnston S. A. (1999 ). Subcellular localization, stoichiometry, and protein levels of 26S proteasome subunits in yeast. J. Biol. Chem. 274, 21943–21952.

     Not in our library10.1074/jbc.274.31.21943 (opens in a new tab)

283. 283.

     Sadre-Bazzaz K. Whitby F. G. Robinson H. Formosa T. Hill C. P. (2010 ). Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening. Mol. Cell 37, 728–735.

     Not in our library10.1016/j.molcel.2010.02.002 (opens in a new tab)

284. 284.

     Saeki Y. (2017 ). Ubiquitin recognition by the proteasome. J. Biochem. 161, 113–124.

     Not in our library10.1093/jb/mvw091 (opens in a new tab)

285. 285.

     Saeki Y. Toh-e A. Kudo T. Kawamura H. Tanaka K. (2009 ). Multiple proteasome-interacting proteins assist the assembly of the yeast 19S regulatory particle. Cell 137, 900–913.

     Not in our library10.1016/j.cell.2009.05.005 (opens in a new tab)

286. 286.

     Saez I. Vilchez D. (2014 ). The mechanistic links between proteasome activity, ageing, and age-related diseases. Curr. Genomics 15, 38–51.

     Not in our library10.2174/138920291501140306113344 (opens in a new tab)

287. 287.

     Sagot I. Laporte D. (2019 ). The cell biology of quiescent yeast: a diversity of individual scenarios. J. Cell Sci. 132, jcs213025.

     Not in our library10.1242/jcs.213025 (opens in a new tab)

288. 288.

     Saha S. Panigrahi D. P. Patil S. Bhutia S. K. (2018 ). Autophagy in health and disease: a comprehensive review. Biomed. Pharmacother. 104, 485–495.

     Not in our library10.1016/j.biopha.2018.05.007 (opens in a new tab)

289. 289.

     Sakata E. Bohn S. Mihalache O. Kiss P. Beck F. Nagy I. (2012 ). Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryo-microscopy. Proc. Natl. Acad. Sci. U.S.A. 109, 1479–1484.

     Not in our library10.1073/pnas.1119394109 (opens in a new tab)

290. 290.

     Samant R. S. Livingston C. M. Sontag E. M. Frydman J. (2018 ). Distinct proteostasis circuits co-operate in nuclear and cytoplasmic protein quality control. Nature 563, 407–411.

     Not in our library10.1038/s41586-018-0678-x (opens in a new tab)

291. 291.

     Sá-Moura B. Simões A. M. Fraga J. Fernandes H. Abreu I. A. Botelho H. M.. (2013 ). Biochemical and biophysical characterization of recombinant yeast proteasome maturation factor Ump1. Comput. Struct. Biotechnol. J. 7:201304006.

     Not in our library10.5936/csbj.201304006 (opens in a new tab)

292. 292.

     Satoh K. Sasajima H. Nyoumura K. I. Yokosawa H. Sawada H. (2001 ). Assembly of the 26S proteasome is regulated by phosphorylation of the p45/Rpt6 ATPase subunit. Biochemistry 40, 314–319.

     Not in our library10.1021/bi001815n (opens in a new tab)

293. 293.

     Satoh T. Saeki Y. Hiromoto T. Wang Y. H. Uekusa Y. Yagi H.. (2014 ). Structural basis for proteasome formation controlled by the assembly chaperone Nas2. Structure 22, 731–743.

     Not in our library10.1016/j.str.2014.02.014 (opens in a new tab)

294. 294.

     Saunier R. Esposito M. Dassa E. P. Delahodde A. (2013 ). Integrity of the Saccharomyces cerevisiae Rpn11 protein is critical for formation of proteasome storage granules and survival in stationary phase. PLoS One 8, 70357.

     Not in our library10.1371/journal.pone.0070357 (opens in a new tab)

295. 295.

     Savulescu A. F. Shorer H. Kleifeld O. Cohen I. Gruber R. Glickman M. H. (2011 ). Nuclear import of an intact pre-assembled proteasome particle. Mol. Biol. Cell 22, 880–891.

     Not in our library10.1091/mbc.e10-07-0595 (opens in a new tab)

296. 296.

     Schauber C. Chen L. Tongaonkar P. Vega I. Lambertson D. Potts W.. (1998 ). Rad23 links DNA repair to the ubiquitin-proteasome pathway. Nature 391, 715–718.

     Not in our library10.1038/35661 (opens in a new tab)

297. 297.

     Schmidt M. Haas W. Crosas B. Santamaria P. G. Gygi S. P. Walz T.. (2005 ). The HEAT repeat protein Blm10 regulates the yeast proteasome by capping the core particle. Nat. Struct. Mol. Biol. 12, 294–303.

     Not in our library10.1038/nsmb914 (opens in a new tab)

298. 298.

     Schmidtke G. Kraft R. Kostka S. Henklein P. Frömmel C. Löwe J.. (1996 ). Analysis of mammalian 20S proteasome biogenesis: the maturation of β-subunits is an ordered two-step mechanism involving autocatalysis. EMBO J. 15, 6887–6898.

     Not in our library10.1002/j.1460-2075.1996.tb01081.x (opens in a new tab)

299. 299.

     Schmidtke G. Schmidt M. Kloetzel P. M. (1997 ). Maturation of the mammalian 20S proteasome: purification and characterization of 13S and 16S proteasome precursor complexes. J. Mol. Biol. 268, 95–106.

     Not in our library10.1006/jmbi.1997.0947 (opens in a new tab)

300. 300.

     Schoebel S. Mi W. Stein A. Ovchinnikov S. Pavlovicz R. Di Maio F.. (2017 ). Cryo-EM structure of the protein-conducting ERAD channel Hrd1 in complex with Hrd3. Nature 548, 352–355.

     Not in our library10.1038/nature23314 (opens in a new tab)

301. 301.

     Schreiber A. Peter M. (2014 ). Substrate recognition in selective autophagy and the ubiquitin-proteasome system. Biochim. Biophys. Acta 1843, 163–181.

     Not in our library10.1016/j.bbamcr.2013.03.019 (opens in a new tab)

302. 302.

     Schreiner P. Chen X. Husnjak K. Randles L. Zhang N. Elsasser S.. (2008 ). Ubiquitin docking at the proteasome through a novel pleckstrin homology domain interaction. Nature 453, 548–552.

     Not in our library10.1038/nature06924 (opens in a new tab)

303. 303.

     Schubert U. Antón L. C. Gibbs J. Norbury C. C. Yewdell J. W. Bennink J. R. (2000 ). Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 404, 770–774.

     Not in our library10.1038/35008096 (opens in a new tab)

304. 304.

     Schweitzer A. Aufderheide A. Rudack T. Beck F. Pfeifer G. Plitzko J. M.. (2016 ). Structure of the human 26S proteasome at a resolution of 3.9 Å. Proc. Natl. Acad. Sci. U.S.A. 113, 7816–7821.

     Not in our library10.1073/pnas.1608050113 (opens in a new tab)

305. 305.

     Seemuller E. Lupas A. Baumeister W. (1996 ). Autocatalytic processing of the 20S proteasome. Nature 382, 468–471.

     Not in our library10.1038/382468a0 (opens in a new tab)

306. 306.

     Sha Z. Goldberg A. L. (2014 ). Proteasome-mediated processing of Nrf1 is essential for co-ordinate induction of all proteasome subunits and p97. Curr. Biol. 24, 1573–1583.

     Not in our library10.1016/j.cub.2014.06.004 (opens in a new tab)

307. 307.

     Sha Z. Goldberg A. L. (2016 ). Complete inhibition of the proteasome reduces new proteasome production by causing Nrf1 aggregation. Curr. Biol. 26, 836–837.

     Not in our library10.1016/j.cub.2016.08.030 (opens in a new tab)

308. 308.
     Structural Organization of the 19S Proteasome Lid: Insights from MS of Intact Complexes · 2006

     No notice
309. 309.

     Shi Y. Chen X. Elsasser S. Stocks B. B. Tian G. Lee B. H.. (2016 ). Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasome. Science 351:9421.

     Not in our library10.1126/science.aad9421 (opens in a new tab)

310. 310.

     Shibahara T. Kawasaki H. Hirano H. (2002 ). Identification of the 19S regulatory particle subunits from the rice 26S proteasome. Eur. J. Biochem. 269, 1474–1483.

     Not in our library10.1046/j.1432-1033.2002.02792.x (opens in a new tab)

311. 311.

     Shirozu R. Yashiroda H. Murata S. (2015 ). Identification of minimum Rpn4-responsive elements in genes related to proteasome functions. FEBS Lett. 589, 933–940.

     Not in our library10.1016/j.febslet.2015.02.025 (opens in a new tab)

312. 312.

     Shpilka T. Welter E. Borovsky N. Amar N. Shimron F. Peleg Y.. (2015 ). Fatty acid synthase is preferentially degraded by autophagy upon nitrogen starvation. Proc. Natl. Acad. Sci. U.S.A. 112, 1434–1439.

     Not in our library10.1073/pnas.1409476112 (opens in a new tab)

313. 313.

     Silva G. M. Netto L. E. Simões V. Santos L. F. Gozzo F. C. Demasi M. A.. (2012 ). Redox control of 20S proteasome gating. Antioxid. Redox Signal. 16, 1183–1194.

     Not in our library10.1089/ars.2011.4210 (opens in a new tab)

314. 314.

     Smith D. M. Chang S. C. Park S. Finley D. Cheng Y. Goldberg A. L. (2007 ). Docking of the C-termini of the proteasomal ATPases into the 20 proteasome α-ring opens the gate for substrate entry. Mol. Cell 27, 731–744.

     Not in our library10.1016/j.molcel.2007.06.033 (opens in a new tab)

315. 315.

     Smith D. M. Fraga H. Reis C. Kafri G. Goldberg A. L. (2011 ). ATP binds to proteasomal ATPases in pairs with distinct functional effects, implying an ordered reaction cycle. Cell 144, 526–538.

     Not in our library10.1016/j.cell.2011.02.005 (opens in a new tab)

316. 316.

     Smith D. M. Kafri G. Cheng Y. Ng D. Walz T. Goldberg A. L. (2005 ). ATP binding to PAN or the regulatory particle ATPases causes association with the 20S proteasome, gate opening, and translocation of unfolded proteins. Mol. Cell 20, 687–698.

     Not in our library10.1016/j.molcel.2005.10.019 (opens in a new tab)

317. 317.

     Specht S. Miller S. B. Mogk A. Bukau B. (2011 ). Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae. J. Cell. Biol. 195, 617–629.

     Not in our library10.1083/jcb.201106037 (opens in a new tab)

318. 318.

     Stade K. Ford C. S. Guthrie C. Weis K. (1997 ). Exportin 1 (Crm1p) is an essential nuclear export factor. Cell 90, 1041–1050.

     Not in our library10.1016/s0092-8674(00)80370-0 (opens in a new tab)

319. 319.

     Stadtmueller B. M. Kish-Trier E. Ferrell K. Petersen C. N. Robinson H. Myszka D. G.. (2012 ). Structure of a proteasome Pba1-Pba2 complex: implications for proteasome assembly, activation, and biological function. J. Biol. Chem. 287, 37371–37382.

     Not in our library10.1074/jbc.m112.367003 (opens in a new tab)

320. 320.

     Steffen J. Seeger M. Koch A. Krüger E. (2010 ). Proteasomal degradation is transcriptionally controlled by TCF11 via an ERAD-dependent feedback loop. Mol. Cell 40, 147–158.

     Not in our library10.1016/j.molcel.2010.09.012 (opens in a new tab)

321. 321.
     Phosphatase UBLCP1 controls proteasome assembly · 2017

     Not checked
322. 322.

     Sun X. M. Butterworth M. MacFarlane M. Dubiel W. Ciechanover A. Cohen G. M. (2004 ). Caspase activation inhibits proteasome function during apoptosis. Mol. Cell 14, 81–93.

     Not in our library10.1016/s1097-2765(04)00156-x (opens in a new tab)

323. 323.

     Takagi K. Kim S. Yukii H. Ueno M. Morishita R. Endo Y. (2012 ). Structural basis for specific recognition of Rpt1p, an ATPase subunit of 26S proteasome, by the proteasome-dedicated chaperone Hsm3p. J. Biol. Chem. 287, 12172–12182.

     Not in our library10.1074/jbc.m112.345876 (opens in a new tab)

324. 324.

     Takagi K. Saeki Y. Yashiroda H. Yagi H. Kaiho A. Murata S.. (2014 ). Pba3-Pba4 heterodimer acts as a molecular matchmaker in proteasome α-ring formation. Biochem. Biophys. Res. Commun. 450, 1110–1114.

     Not in our library10.1016/j.bbrc.2014.06.119 (opens in a new tab)

325. 325.

     Takeda K. Yanagida M. (2005 ). Regulation of nuclear proteasomes by Rhp6/Ubc2 through ubiquitination and destruction of the sensor and anchor Cut8. Cell 122, 393–405.

     Not in our library10.1016/j.cell.2005.05.023 (opens in a new tab)

326. 326.

     Takeshige K. Baba M. Tsuboi S. Noda T. Ohsumi Y. (1992 ). Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction. J. Cell Biol. 119, 301–311.

     Not in our library10.1083/jcb.119.2.301 (opens in a new tab)

327. 327.

     Takeuchi J. Tamura T. (2004 ). Recombinant ATPases of the yeast 26S proteasome activate protein degradation by the 20S proteasome. FEBS Lett. 565, 39–42.

     Not in our library10.1016/j.febslet.2004.03.073 (opens in a new tab)

328. 328.

     Tanaka K. Ichihara A. (1989 ). Half-life of proteasomes (multi-protease complexes) in rat liver. Biochem. Biophys. Res. Commun. 159, 1309–1315.

     Not in our library10.1016/0006-291x(89)92253-5 (opens in a new tab)

329. 329.

     Tanaka K. Yoshimura T. Tamura T. Fujiwara T. Kumatori A. Ichihara A. (1990 ). Possible mechanism of nuclear transportation of proteasomes. FEBS Lett. 271, 41–46.

     Not in our library10.1016/0014-5793(90)80367-r (opens in a new tab)

330. 330.

     Thompson A. R. Doelling J. H. Suttangkakul A. Vierstra R. D. (2005 ). Autophagic nutrient recycling in Arabidopsis directed by the ATG8 and ATG12 conjugation pathways. Plant Physiol. 138, 2097–2110.

     Not in our library10.1104/pp.105.060673 (opens in a new tab)

331. 331.

     Tian G. Park S. Lee M. J. Huck B. McAllister F. Hill C. P.. (2011 ). An asymmetric interface between the regulatory and core particles of the proteasome. Nat. Struct. Mol. Biol. 18, 1259–1267.

     Not in our library10.1038/nsmb.2147 (opens in a new tab)

332. 332.

     Tomita T. Hirayama S. Sakurai Y. Ohte Y. Yoshihara H. Saeki Y.. (2019 ). Specific modification of aged proteasomes revealed by tag-exchangeable knock-in mice. Mol. Cell. Biol. 39:426.

     Not in our library10.1128/mcb.00426-18 (opens in a new tab)

333. 333.

     Tomko R. J. Funakoshi M. Schneider K. Wang J. Hochstrasser M. (2010 ). Hetero-hexameric ring arrangement of the eukaryotic proteasomal ATPases: implications for proteasome structure and assembly. Mol. Cell 38, 393–403.

     Not in our library10.1016/j.molcel.2010.02.035 (opens in a new tab)

334. 334.

     Tomko R. J. Hochstrasser M. (2011 ). Incorporation of the Rpn12 subunit couples completion of proteasome regulatory particle lid assembly to lid-base joining. Mol. Cell 44, 907–917.

     Not in our library10.1016/j.molcel.2011.11.020 (opens in a new tab)

335. 335.

     Tomko R. J. Hochstrasser M. (2014 ). The intrinsically disordered Sem1 protein functions as a molecular tether during proteasome lid biogenesis. Mol. Cell 53, 433–443.

     Not in our library10.1016/j.molcel.2013.12.009 (opens in a new tab)

336. 336.

     Tomko R. J. Taylor D. W. Chen Z. A. Wang H. W. Rappsilber J. Hochstrasser M. (2015 ). A single α-helix drives extensive re-modeling of the proteasome lid and completion of regulatory particle assembly. Cell 163, 432–444.

     Not in our library10.1016/j.cell.2015.09.022 (opens in a new tab)

337. 337.

     Tsuchiya H. Ohtake F. Arai N. Kaiho A. Yasuda S. Tanaka K.. (2017 ). In vivo ubiquitin linkage-type analysis reveals that the Cdc48-Rad23/Dsk2 axis contributes to K48-linked chain specificity of the proteasome. Mol. Cell 66, 488–502.

     Not in our library10.1016/j.molcel.2017.04.024 (opens in a new tab)

338. 338.

     Tsuchiya Y. Morita T. Kim M. Iemuram S. Natsume T. Yamamoto M. (2011 ). Dual regulation of the transcriptional activity of Nrf1 by SCF- and Hrd1-dependent degradation. Mol. Cell. Biol. 31, 4500–4512.

     Not in our library10.1128/mcb.05663-11 (opens in a new tab)

339. 339.

     Üstün S. Hafrén A. Liu Q. Marshall R. S. Minina E. A. Bozhkov P. V.. (2018 ). Bacteria exploit autophagy for proteasome degradation and enhanced virulence in plants. Plant Cell 30, 668–685.

     Not in our library10.1105/tpc.17.00815 (opens in a new tab)

340. 340.

     van Deventer S. Menendez-Benito V. van Leeuwen F. Neefjes J. (2015 ). N-terminal acetylation and replicative age affect proteasome localization and cell fitness during aging. J. Cell Sci. 128, 109–117.

     Not in our library10.1242/jcs.157354 (opens in a new tab)

341. 341.

     van Nocker S. Deveraux Q. Rechsteiner M. Vierstra R. D. (1996a ). The Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component of the 26S proteasome. Proc. Natl. Acad. Sci. U.S.A. 93, 856–860.

     Not in our library10.1073/pnas.93.2.856 (opens in a new tab)

342. 342.

     van Nocker S. Sadis S. Rubin D. M. Glickman M. H. Fu H. Coux O. (1996b ). The multi-ubiquitin chain binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a non-essential, substrate-specific role in protein turnover. Mol. Cell. Biol. 16, 6020–6028.

     Not in our library10.1128/mcb.16.11.6020 (opens in a new tab)

343. 343.

     Vangala J. R. Dudem S. Jain N. Kalivendi S. V. (2014 ). Regulation of PSMB5 protein and β-subunits of mammalian proteasomes by constitutively activated Signal Transducer and Activator of Transcription 3 (STAT3): a potential role in bortezomib-mediated anti-cancer therapy. J. Biol. Chem. 289, 12612–12622.

     Not in our library10.1074/jbc.m113.542829 (opens in a new tab)

344. 344.

     Vangala J. R. Sotzny F. Krüger E. Deshaies R. J. Radhakrishnan S. K. (2016 ). Nrf1 can be processed and activated in a proteasome-independent manner. Curr. Biol. 26, 834–835.

     Not in our library10.1016/j.cub.2016.08.008 (opens in a new tab)

345. 345.

     Velichutina I. Connerly P. L. Arendt C. S. Li X. Hochstrasser M. (2004 ). Plasticity in eukaryotic 20S proteasome ring assembly revealed by a subunit deletion in yeast. EMBO J. 23, 500–510.

     Not in our library10.1038/sj.emboj.7600059 (opens in a new tab)

346. 346.

     Verma R. Aravind L. Oania R. McDonald W. H. Yates J. R. Koonin E. V.. (2002 ). Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Science 298, 611–615.

     Not in our library10.1126/science.1075898 (opens in a new tab)

347. 347.

     Verma R. Oania R. Graumann J. Deshaies R. J. (2004 ). Multi-ubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system. Cell 118, 99–110.

     Not in our library10.1016/j.cell.2004.06.014 (opens in a new tab)

348. 348.

     Vierstra R. D. (2009 ). The ubiquitin-26S proteasome system at the nexus of plant biology. Nat. Rev. Mol. Cell Biol. 10, 385–397.

     Not in our library10.1038/nrm2688 (opens in a new tab)

349. 349.

     Vilchez D. Boyer L. Morantte I. Lutz M. Merkwirth C. Joyce D.. (2012 ). Increased proteasome activity in human embryonic stem cells is regulated by PSMD11. Nature 489, 304–308.

     Not in our library10.1038/nature11468 (opens in a new tab)

350. 350.

     Waite K. A. De La Mota-Peynado A. Vontz G. Roelofs J. (2016 ). Starvation induces proteasome autophagy with different pathways for core and regulatory particles. J. Biol. Chem. 291, 3239–3253.

     Not in our library10.1074/jbc.m115.699124 (opens in a new tab)

351. 351.

     Walters K. J. Kleijnen M. F. Goh A. M. Wagner G. Howley P. M. (2002 ). Structural studies of the interaction between ubiquitin family proteins and the proteasome subunit S5a. Biochemistry 41, 1767–1777.

     Not in our library10.1021/bi011892y (opens in a new tab)

352. 352.

     Wang L. Mao X. Ju D. Xie Y. (2004 ). Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase. J. Biol. Chem. 279, 55218–55223.

     Not in our library10.1074/jbc.m410085200 (opens in a new tab)

353. 353.

     Wang W. Chan J. Y. (2006 ). Nrf1 is targeted to the endoplasmic reticulum membrane by an N-terminal transmembrane domain: inhibition of nuclear translocation and trans-acting function. J. Biol. Chem. 281, 19676–19687.

     Not in our library10.1074/jbc.m602802200 (opens in a new tab)

354. 354.

     Wang X. Chemmama I. E. Yu C. Huszagh A. Xu Y. Viner R.. (2017 ). The proteasome-interacting Ecm29 protein disassembles the 26S proteasome in response to oxidative stress. J. Biol. Chem. 292, 16310–16320.

     Not in our library10.1074/jbc.m117.803619 (opens in a new tab)

355. 355.

     Wang X. Xu H. Ha S. W. Ju D. Xie Y. (2010a ). Proteasomal degradation of Rpn4 in Saccharomyces cerevisiae is critical for cell viability under stressed conditions. Genetics 184, 335–342.

     Not in our library10.1534/genetics.109.112227 (opens in a new tab)

356. 356.

     Wang X. Xu H. Ju D. Xie Y. (2008 ). Disruption of Rpn4-induced proteasome expression in Saccharomyces cerevisiae reduces cell viability under stressed conditions. Genetics 180, 1945–1953.

     Not in our library10.1534/genetics.108.094524 (opens in a new tab)

357. 357.

     Wang X. Yen J. Kaiser P. Huang L. (2010b ). Regulation of the 26S proteasome complex during oxidative stress. Sci. Signal. 3:88.

     Not in our library10.1126/scisignal.2001232 (opens in a new tab)

358. 358.

     Wang Z. Zhang H. (2019 ). Phase separation, transition, and autophagic degradation of proteins in development and pathogenesis. Trends Cell Biol. 29, 417–427.

     Not in our library10.1016/j.tcb.2019.01.008 (opens in a new tab)

359. 359.

     Wani P. S. Rowland M. A. Ondracek A. Deeds E. J. Roelofs J. (2015 ). Maturation of the proteasome core particle induces an affinity switch that controls regulatory particle association. Nat. Commun. 6:6384.

     Not in our library10.1038/ncomms7384 (opens in a new tab)

360. 360.

     Wani P. S. Suppahia A. Capalla X. Ondracek A. Roelofs J. (2016 ). Phosphorylation of the C-terminal tail of proteasome subunit α7 is required for binding of the proteasome quality control factor Ecm29. Sci. Rep. 6:27873.

     Not in our library10.1038/srep27873 (opens in a new tab)

361. 361.

     Weberruss M. H. Savulescu A. F. Jando J. Bissinger T. Harel A. Glickman M. H.. (2013 ). Blm10 facilitates nuclear import of proteasome core particles. EMBO J. 32, 2697–2707.

     Not in our library10.1038/emboj.2013.192 (opens in a new tab)

362. 362.

     Wehmer M. Rudack T. Beck F. Aufderheide A. Pfeifer G. Plitzko J. M.. (2017 ). Structural insights into the functional cycle of the ATPase module of the 26S proteasome. Proc. Natl. Acad. Sci. U.S.A. 114, 1305–1310.

     Not in our library10.1073/pnas.1621129114 (opens in a new tab)

363. 363.

     Wei S. J. Williams J. G. Dang H. Darden T. A. Betz B. L. Humble M. M.. (2008 ). Identification of a specific motif of the DSS1 protein required for proteasome interaction and p53 protein degradation. J. Mol. Biol. 383, 693–712.

     Not in our library10.1016/j.jmb.2008.08.044 (opens in a new tab)

364. 364.

     Welk V. Coux O. Kleene V. Abeza C. Trümbach D. Eickelberg O.. (2016 ). Inhibition of proteasome activity induces formation of alternative proteasome complexes. J. Biol. Chem. 291, 13147–13159.

     Not in our library10.1074/jbc.m116.717652 (opens in a new tab)

365. 365.

     Wendler P. Lehmann A. Janek K. Baumgart S. Enenkel C. (2004 ). The bipartite nuclear localization sequence of Rpn2 is required for nuclear import of proteasomal base complexes via karyopherin αβ. J. Biol. Chem. 279, 37751–37762.

     Not in our library10.1074/jbc.m403551200 (opens in a new tab)

366. 366.

     Wilkinson C. R. Seeger M. Hartmann-Petersen R. Stone M. Wallace M. Semple C.. (2001 ). Proteins containing the UBA domain are able to bind to multi-ubiquitin chains. Nat. Cell Biol. 3, 939–943.

     Not in our library10.1038/ncb1001-939 (opens in a new tab)

367. 367.

     Wilkinson K. D. Urban M. K. Haas A. L. (1980 ). Ubiquitin is the ATP-dependent proteolysis factor I of rabbit reticulocytes. J. Biol. Chem. 255, 7529–7532.

     Not in our library

368. 368.

     Worden E. J. Dong K. C. Martin A. (2017 ). An AAA motor-driven switch in Rpn11 controls deubiquitination at the 26S proteasome. Mol. Cell 67, 799–811.

     Not in our library10.1016/j.molcel.2017.07.023 (opens in a new tab)

369. 369.

     Worden E. J. Padovani C. Martin A. (2014 ). Structure of the Rpn11-Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degradation. Nat. Struct. Mol. Biol. 21, 220–227.

     Not in our library10.1038/nsmb.2771 (opens in a new tab)

370. 370.

     Wyant G. A. Abu-Remaileh M. Frenkel E. M. Laqtom N. N. Dharamdasani V. Lewis C. A.. (2018 ). NUFIP1 is a ribosome receptor for starvation-induced ribophagy. Science 360, 751–758.

     Not in our library10.1126/science.aar2663 (opens in a new tab)

371. 371.
     Physical association of ubiquitin ligases and the 26S proteasome · 2000

     Not checked
372. 372.

     Xie Y. Varshavsky A. (2001 ). Rpn4 is a ligand, substrate and transcriptional regulator of the 26S proteasome: a negative feedback circuit. Proc. Natl. Acad. Sci. U.S.A. 98, 3056–3061.

     Not in our library10.1073/pnas.071022298 (opens in a new tab)

373. 373.

     Xiong Q. Fischer S. Karow M. Müller R. Meßling S. Eichinger L. (2018 ). ATG16 mediates the autophagic degradation of the 19S proteasomal subunits PSMD1 and PSMD2. Eur. J. Cell Biol. 97, 523–532.

     Not in our library10.1016/j.ejcb.2018.09.002 (opens in a new tab)

374. 374.

     Xu H. Fu J. Ha S. W. Ju D. Zheng J. Li L.. (2012 ). The CCAAT box-binding transcription factor NF-Y regulates basal expression of human proteasome genes. Biochim. Biophys. Acta 1823, 818–825.

     Not in our library10.1016/j.bbamcr.2012.01.002 (opens in a new tab)

375. 375.

     Xu P. Duong D. M. Seyfried N. T. Cheng D. Xie Y. Robert J.. (2009 ). Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation. Cell 137, 133–145.

     Not in our library10.1016/j.cell.2009.01.041 (opens in a new tab)

376. 376.

     Yabuta Y. Osada R. Morishita T. Nishizawa-Yokoi A. Tamoi M. Maruta T.. (2011 ). Involvement of an Arabidopsis NAC transcription factor in the regulation of 20S and 26S proteasomes. Plant Sci. 181, 421–427.

     Not in our library10.1016/j.plantsci.2011.07.001 (opens in a new tab)

377. 377.

     Yamano K. Matsuda N. Tanaka K. (2016 ). The ubiquitin signal and autophagy: an orchestrated dance leading to mitochondrial degradation. EMBO Rep. 17, 300–316.

     Not in our library10.15252/embr.201541486 (opens in a new tab)

378. 378.

     Yamano T. Mikukami S. Murata S. Chiba T. Tanaka K. Udono H. (2008 ). Hsp90-mediated assembly of the 26S proteasome is involved in major histocompatibility complex class I antigen processing. J. Biol. Chem. 283, 28060–28065.

     Not in our library10.1074/jbc.m803077200 (opens in a new tab)

379. 379.
     Arabidopsis PROTEASOME REGULATOR1 is required for auxin-mediated suppression of proteasome activity and regulates auxin signalling · 2016

     No notice
380. 380.

     Yang P. Fu H. Walker J. M. Papa C. M. Smalle J. Ju Y. M. (2004 ). Purification of the Arabidopsis 26S proteasome: biochemical and molecular analyses reveal the presence of multiple isoforms. J. Biol. Chem. 279, 6401–6413.

     Not in our library10.1074/jbc.m311977200 (opens in a new tab)

381. 381.

     Yang Y. Früh K. Ahn K. Peterson P. A. (1995 ). In vivo assembly of the proteasomal complexes, and implications for antigen processing. J. Biol. Chem. 270, 27687–27694.

     Not in our library10.1074/jbc.270.46.27687 (opens in a new tab)

382. 382.

     Yao T. Cohen R. E. (2002 ). A cryptic protease couples deubiquitylation and degradation by the proteasome. Nature 419, 403–407.

     Not in our library10.1038/nature01071 (opens in a new tab)

383. 383.

     Yao T. Song L. Xu W. DeMartino G. N. Florens L. Swanson S. K.. (2006 ). Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1. Nat. Cell Biol. 8, 994–1002.

     Not in our library10.1038/ncb1460 (opens in a new tab)

384. 384.

     Yao Y. Toth C. R. Huang L. Wong M. L. Dias P. Burlingame A. L. (1999 ). The α5 subunit of the Trypanosoma brucei proteasome can self-assemble to form a cylinder of four stacked heptameric rings. Biochem. J. 344, 349–358.

     Not in our library10.1042/bj3440349 (opens in a new tab)

385. 385.

     Yashiroda H. Mizushima T. Okamoto K. Kameyama T. Hayashi H. Kishimoto T.. (2008 ). Crystal structure of a chaperone complex that contributes to the assembly of yeast 20S proteasomes. Nat. Struct. Mol. Biol. 15, 228–236.

     Not in our library10.1038/nsmb.1386 (opens in a new tab)

386. 386.

     Yashiroda H. Toda Y. Otsu S. Takagi K. Mizushima T. Murata S. (2015 ). N-terminal α7 deletion of the proteasome 20S core particle substitutes for yeast PI31 function. Mol. Cell. Biol. 35, 141–152.

     Not in our library10.1128/mcb.00582-14 (opens in a new tab)

387. 387.

     Yau R. G. Doerner K. Castellanos E. R. Haakonsen D. L. Werner A. Wang N.. (2017 ). Assembly and function of heterotypic ubiquitin chains in the cell cycle and protein quality control. Cell 171, 918–933.

     Not in our library10.1016/j.cell.2017.09.040 (opens in a new tab)

388. 388.

     Yedidi R. S. Fatehi A. K. Enenkel C. (2016 ). Proteasome dynamics between proliferation and quiescence stages of Saccharomyces cerevisiae. Crit. Rev. Biochem. Mol. Biol. 51, 497–512.

     Not in our library10.1080/10409238.2016.1230087 (opens in a new tab)

389. 389.

     Yu H. Kago G. Yellman C. M. Matouschek A. (2016 ). Ubiquitin-like domains can target to the proteasome, but proteolysis requires a disordered region. EMBO J. 35, 1522–1536.

     Not in our library10.15252/embj.201593147 (opens in a new tab)

390. 390.

     Zaiss D. M. Standera S. Holzhütter H. Kloetzel P. M. Sijts A. J. (1999 ). The proteasome inhibitor PI31 competes with PA28 for binding to 20S proteasomes. FEBS Lett. 457, 333–338.

     Not in our library10.1016/s0014-5793(99)01072-8 (opens in a new tab)

391. 391.

     Zhang F. Hu M. Tian G. Zhang P. Finley D. Jeffrey P. D.. (2009 ). Structural insights into the regulatory particle of the proteasome from Methanocaldococcus jannaschii. Mol. Cell 34, 473–484.

     Not in our library10.1016/j.molcel.2009.04.021 (opens in a new tab)

392. 392.

     Zhang F. Su K. Yang X. Bowe D. B. Paterson A. J. Kudlow J. E. (2003 ). O-GlcNAc modification is an endogenous inhibitor of the proteasome. Cell 115, 715–725.

     Not in our library10.1016/s0092-8674(03)00974-7 (opens in a new tab)

393. 393.

     Zhang T. Shen S. Qu J. Ghaemmaghami S. (2016 ). Global analysis of cellular protein flux quantifies the selectivity of basal autophagy. Cell Rep. 14, 2426–2439.

     Not in our library10.1016/j.celrep.2016.02.040 (opens in a new tab)

394. 394.

     Zhang Y. Lucocq J. M. Yamamoto M. Hayes J. D. (2007 ). The NHB1 (N-terminal homology box 1) sequence in transcription factor Nrf1 is required to anchor it to the endoplasmic reticulum and enable its asparagine-linked glycosylation. Biochem J. 408, 161–172.

     Not in our library10.1042/bj20070761 (opens in a new tab)

395. 395.

     Zheng N. Shabek N. (2017 ). Ubiquitin ligases: structure, function and regulation. Annu. Rev. Biochem. 86, 129–157.

     Not in our library10.1146/annurev-biochem-060815-014922 (opens in a new tab)

396. 396.

     Zong N. Ping P. Lau E. Choi H. J. Ng D. C. Meyer D.. (2014 ). Lysine ubiquitination and acetylation of human cardiac 20S proteasomes. Proteomics Clin. Appl. 8, 590–594.

     Not in our library10.1002/prca.201400029 (opens in a new tab)

397. 397.

     Zuin A. Bichmann A. Isasa M. Puig-Sàrries P. Diaz L. M. Crosas B. (2015 ). RPN10 mono-ubiquitination orchestrates the association of the ubiquilin-type DSK2 receptor with the proteasome. Biochem. J. 472, 353–365.

     Not in our library10.1042/bj20150609 (opens in a new tab)

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