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Ron Kopito - Publications

Affiliations: 
Stanford University, Palo Alto, CA 
Area:
Biology
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72 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2024 Hickey KL, Panov A, Whelan EM, Schäfer T, Mizrak A, Kopito RR, Baumeister W, Fernández-Busnadiego R, Harper JW. Temporal control of acute protein aggregate turnover by UBE3C and NRF1-dependent proteasomal pathways. Proceedings of the National Academy of Sciences of the United States of America. 121: e2417390121. PMID 39636856 DOI: 10.1073/pnas.2417390121  0.418
2024 Hickey KL, Panov A, Whelan EM, Schäfer T, Mizrak A, Kopito RR, Baumeister W, Fernández-Busnadiego R, Harper JW. Temporal control of acute protein aggregate turnover by UBE3C and NRF1-dependent proteasomal pathways. Biorxiv : the Preprint Server For Biology. PMID 39282280 DOI: 10.1101/2024.08.30.610524  0.418
2024 DaRosa PA, Penchev I, Gumbin SC, Scavone F, Wąchalska M, Paulo JA, Ordureau A, Peter JJ, Kulathu Y, Harper JW, Becker T, Beckmann R, Kopito RR. UFM1 E3 ligase promotes recycling of 60S ribosomal subunits from the ER. Nature. PMID 38383785 DOI: 10.1038/s41586-024-07073-0  0.316
2023 Riepe C, Wąchalska M, Deol KK, Amaya AK, Porteus MH, Olzmann JA, Kopito RR. Small molecule correctors divert CFTR-F508del from ERAD by stabilizing sequential folding states. Molecular Biology of the Cell. mbcE23080336. PMID 38019608 DOI: 10.1091/mbc.E23-08-0336  0.629
2023 Riepe C, Wąchalska M, Deol KK, Amaya AK, Porteus MH, Olzmann JA, Kopito RR. Small molecule correctors divert CFTR-F508del from ERAD by stabilizing sequential folding states. Biorxiv : the Preprint Server For Biology. PMID 37745470 DOI: 10.1101/2023.09.15.556420  0.63
2023 Roberts MA, Deol KK, Mathiowetz AJ, Lange M, Leto DE, Stevenson J, Hashemi SH, Morgens DW, Easter E, Heydari K, Nalls MA, Bassik MC, Kampmann M, Kopito RR, Faghri F, et al. Parallel CRISPR-Cas9 screens identify mechanisms of PLIN2 and lipid droplet regulation. Developmental Cell. PMID 37494933 DOI: 10.1016/j.devcel.2023.07.001  0.602
2023 Scavone F, Gumbin SC, Da Rosa PA, Kopito RR. RPL26/uL24 UFMylation is essential for ribosome-associated quality control at the endoplasmic reticulum. Proceedings of the National Academy of Sciences of the United States of America. 120: e2220340120. PMID 37036982 DOI: 10.1073/pnas.2220340120  0.336
2023 Scavone F, Gumbin SC, DaRosa PA, Kopito RR. RPL26/uL24 UFMylation is essential for ribosome-associated quality control at the endoplasmic reticulum. Biorxiv : the Preprint Server For Biology. PMID 36945571 DOI: 10.1101/2023.03.08.531792  0.336
2022 Peter JJ, Magnussen HM, DaRosa PA, Millrine D, Matthews SP, Lamoliatte F, Sundaramoorthy R, Kopito RR, Kulathu Y. A non-canonical scaffold-type E3 ligase complex mediates protein UFMylation. The Embo Journal. e111015. PMID 36121123 DOI: 10.15252/embj.2022111015  0.316
2019 Gottlieb CD, Thompson ACS, Ordureau A, Harper JW, Kopito RR. Acute unfolding of a single protein immediately stimulates recruitment of ubiquitin protein ligase E3C (UBE3C) to 26S proteasomes. The Journal of Biological Chemistry. PMID 31375563 DOI: 10.1074/jbc.RA119.009654  0.426
2019 Leto DE, Kopito RR. Methods for genetic analysis of mammalian ER-associated degradation. Methods in Enzymology. 619: 97-120. PMID 30910031 DOI: 10.1016/Bs.Mie.2019.01.006  0.325
2019 Walczak CP, Leto DE, Zhang L, Riepe C, Muller RY, DaRosa PA, Ingolia NT, Elias JE, Kopito RR. Ribosomal protein RPL26 is the principal target of UFMylation. Proceedings of the National Academy of Sciences of the United States of America. PMID 30626644 DOI: 10.1073/Pnas.1816202116  0.411
2019 Leto DE, Morgens DW, Zhang L, Walczak CP, Elias JE, Bassik MC, Kopito RR. Genome-wide CRISPR Analysis Identifies Substrate-Specific Conjugation Modules in ER-Associated Degradation. Molecular Cell. 73: 377-389.e11. PMID 30581143 DOI: 10.1016/J.Molcel.2018.11.015  0.412
2018 van der Goot AT, Pearce MMP, Leto DE, Shaler TA, Kopito RR. Redundant and Antagonistic Roles of XTP3B and OS9 in Decoding Glycan and Non-glycan Degrons in ER-Associated Degradation. Molecular Cell. PMID 29706535 DOI: 10.1016/J.Molcel.2018.03.026  0.378
2017 Hwang J, Walczak CP, Shaler TA, Olzmann JA, Zhang L, Elias JE, Kopito RR. Characterization of protein complexes of the endoplasmic reticulum associated degradation E3 ubiquitin ligase Hrd1. The Journal of Biological Chemistry. PMID 28411238 DOI: 10.1074/Jbc.M117.785055  0.695
2017 Sweeney P, Park H, Baumann M, Dunlop J, Frydman J, Kopito R, McCampbell A, Leblanc G, Venkateswaran A, Nurmi A, Hodgson R. Protein misfolding in neurodegenerative diseases: implications and strategies. Translational Neurodegeneration. 6: 6. PMID 28293421 DOI: 10.1186/S40035-017-0077-5  0.403
2017 Pearce MM, Kopito RR. Prion-Like Characteristics of Polyglutamine-Containing Proteins. Cold Spring Harbor Perspectives in Medicine. PMID 28096245 DOI: 10.1101/cshperspect.a024257  0.404
2016 Schrul B, Kopito RR. Peroxin-dependent targeting of a lipid-droplet-destined membrane protein to ER subdomains. Nature Cell Biology. PMID 27295553 DOI: 10.1038/ncb3373  0.357
2016 Bersuker K, Brandeis M, Kopito RR. Protein misfolding specifies recruitment to cytoplasmic inclusion bodies. The Journal of Cell Biology. 213: 229-41. PMID 27114501 DOI: 10.1083/jcb.201511024  0.37
2015 Pearce MM, Spartz EJ, Hong W, Luo L, Kopito RR. Prion-like transmission of neuronal huntingtin aggregates to phagocytic glia in the Drosophila brain. Nature Communications. 6: 6768. PMID 25866135 DOI: 10.1038/ncomms7768  0.314
2013 Bersuker K, Hipp MS, Calamini B, Morimoto RI, Kopito RR. Heat shock response activation exacerbates inclusion body formation in a cellular model of Huntington disease. The Journal of Biological Chemistry. 288: 23633-8. PMID 23839939 DOI: 10.1074/Jbc.C113.481945  0.352
2013 Olzmann JA, Richter CM, Kopito RR. Spatial regulation of UBXD8 and p97/VCP controls ATGL-mediated lipid droplet turnover. Proceedings of the National Academy of Sciences of the United States of America. 110: 1345-50. PMID 23297223 DOI: 10.1073/Pnas.1213738110  0.66
2013 Olzmann JA, Kopito RR, Christianson JC. The mammalian endoplasmic reticulum-associated degradation system. Cold Spring Harbor Perspectives in Biology. 5. PMID 23232094 DOI: 10.1101/Cshperspect.A013185  0.808
2012 Tyler RE, Pearce MM, Shaler TA, Olzmann JA, Greenblatt EJ, Kopito RR. Unassembled CD147 is an endogenous endoplasmic reticulum-associated degradation substrate. Molecular Biology of the Cell. 23: 4668-78. PMID 23097496 DOI: 10.1091/Mbc.E12-06-0428  0.759
2012 Greenblatt EJ, Olzmann JA, Kopito RR. Making the cut: intramembrane cleavage by a rhomboid protease promotes ERAD. Nature Structural & Molecular Biology. 19: 979-81. PMID 23037595 DOI: 10.1038/Nsmb.2398  0.785
2012 Trevino RS, Lauckner JE, Sourigues Y, Pearce MM, Bousset L, Melki R, Kopito RR. Fibrillar structure and charge determine the interaction of polyglutamine protein aggregates with the cell surface. The Journal of Biological Chemistry. 287: 29722-8. PMID 22753412 DOI: 10.1074/jbc.M112.372474  0.332
2012 Hipp MS, Bersuker K, Kopito RR. Live-cell imaging of ubiquitin-proteasome system function. Methods in Molecular Biology (Clifton, N.J.). 832: 463-72. PMID 22350906 DOI: 10.1007/978-1-61779-474-2_33  0.33
2012 Christianson JC, Olzmann JA, Shaler TA, Sowa ME, Bennett EJ, Richter CM, Tyler RE, Greenblatt EJ, Harper JW, Kopito RR. Defining human ERAD networks through an integrative mapping strategy. Nature Cell Biology. 14: 93-105. PMID 22119785 DOI: 10.1038/Ncb2383  0.764
2011 Greenblatt EJ, Olzmann JA, Kopito RR. Derlin-1 is a rhomboid pseudoprotease required for the dislocation of mutant α-1 antitrypsin from the endoplasmic reticulum. Nature Structural & Molecular Biology. 18: 1147-52. PMID 21909096 DOI: 10.1038/Nsmb.2111  0.786
2011 Olzmann JA, Kopito RR. Lipid droplet formation is dispensable for endoplasmic reticulum-associated degradation. The Journal of Biological Chemistry. 286: 27872-4. PMID 21693705 DOI: 10.1074/Jbc.C111.266452  0.679
2011 Riley BE, Kaiser SE, Kopito RR. Autophagy inhibition engages Nrf2-p62 Ub-associated signaling. Autophagy. 7: 338-40. PMID 21252622 DOI: 10.4161/Auto.7.3.14780  0.374
2010 Riley BE, Kaiser SE, Shaler TA, Ng AC, Hara T, Hipp MS, Lage K, Xavier RJ, Ryu KY, Taguchi K, Yamamoto M, Tanaka K, Mizushima N, Komatsu M, Kopito RR. Ubiquitin accumulation in autophagy-deficient mice is dependent on the Nrf2-mediated stress response pathway: a potential role for protein aggregation in autophagic substrate selection. The Journal of Cell Biology. 191: 537-52. PMID 21041446 DOI: 10.1083/Jcb.201005012  0.303
2010 Brundin P, Melki R, Kopito R. Prion-like transmission of protein aggregates in neurodegenerative diseases. Nature Reviews. Molecular Cell Biology. 11: 301-7. PMID 20308987 DOI: 10.1038/Nrm2873  0.433
2009 Wang Y, Pearce MM, Sliter DA, Olzmann JA, Christianson JC, Kopito RR, Boeckmann S, Gagen C, Leichner GS, Roitelman J, Wojcikiewicz RJ. SPFH1 and SPFH2 mediate the ubiquitination and degradation of inositol 1,4,5-trisphosphate receptors in muscarinic receptor-expressing HeLa cells. Biochimica Et Biophysica Acta. 1793: 1710-8. PMID 19751772 DOI: 10.1016/J.Bbamcr.2009.09.004  0.743
2009 Ren PH, Lauckner JE, Kachirskaia I, Heuser JE, Melki R, Kopito RR. Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates. Nature Cell Biology. 11: 219-25. PMID 19151706 DOI: 10.1038/Ncb1830  0.759
2008 Kaganovich D, Kopito R, Frydman J. Misfolded proteins partition between two distinct quality control compartments. Nature. 454: 1088-95. PMID 18756251 DOI: 10.1038/Nature07195  0.514
2008 Christianson JC, Shaler TA, Tyler RE, Kopito RR. OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nature Cell Biology. 10: 272-82. PMID 18264092 DOI: 10.1038/Ncb1689  0.746
2007 Bruns CK, Kopito RR. Impaired post-translational folding of familial ALS-linked Cu, Zn superoxide dismutase mutants. The Embo Journal. 26: 855-66. PMID 17255946 DOI: 10.1038/Sj.Emboj.7601528  0.782
2006 DeLaBarre B, Christianson JC, Kopito RR, Brunger AT. Central pore residues mediate the p97/VCP activity required for ERAD. Molecular Cell. 22: 451-62. PMID 16713576 DOI: 10.1016/J.Molcel.2006.03.036  0.679
2006 Betarbet R, Canet-Aviles RM, Sherer TB, Mastroberardino PG, McLendon C, Kim JH, Lund S, Na HM, Taylor G, Bence NF, Kopito R, Seo BB, Yagi T, Yagi A, Klinefelter G, et al. Intersecting pathways to neurodegeneration in Parkinson's disease: effects of the pesticide rotenone on DJ-1, alpha-synuclein, and the ubiquitin-proteasome system. Neurobiology of Disease. 22: 404-20. PMID 16439141 DOI: 10.1016/J.Nbd.2005.12.003  0.723
2005 Bence NF, Bennett EJ, Kopito RR. Application and analysis of the GFPu family of ubiquitin-proteasome system reporters. Methods in Enzymology. 399: 481-90. PMID 16338377 DOI: 10.1016/S0076-6879(05)99033-2  0.721
2005 Iwata A, Riley BE, Johnston JA, Kopito RR. HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin. The Journal of Biological Chemistry. 280: 40282-92. PMID 16192271 DOI: 10.1074/Jbc.M508786200  0.411
2005 Iwata A, Christianson JC, Bucci M, Ellerby LM, Nukina N, Forno LS, Kopito RR. Increased susceptibility of cytoplasmic over nuclear polyglutamine aggregates to autophagic degradation. Proceedings of the National Academy of Sciences of the United States of America. 102: 13135-40. PMID 16141322 DOI: 10.1073/Pnas.0505801102  0.739
2005 Mukai H, Isagawa T, Goyama E, Tanaka S, Bence NF, Tamura A, Ono Y, Kopito RR. Formation of morphologically similar globular aggregates from diverse aggregation-prone proteins in mammalian cells. Proceedings of the National Academy of Sciences of the United States of America. 102: 10887-92. PMID 16040812 DOI: 10.1073/Pnas.0409283102  0.763
2005 Bennett EJ, Bence NF, Jayakumar R, Kopito RR. Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation. Molecular Cell. 17: 351-65. PMID 15694337 DOI: 10.1016/J.Molcel.2004.12.021  0.79
2005 Rajan RS, Kopito RR. Suppression of wild-type rhodopsin maturation by mutants linked to autosomal dominant retinitis pigmentosa. The Journal of Biological Chemistry. 280: 1284-91. PMID 15509574 DOI: 10.1074/Jbc.M406448200  0.79
2003 Gelman MS, Kopito RR. Cystic fibrosis: premature degradation of mutant proteins as a molecular disease mechanism. Methods in Molecular Biology (Clifton, N.J.). 232: 27-37. PMID 12840537 DOI: 10.1385/1-59259-394-1:27  0.316
2003 Kopito RR, Green WN, Andersen O. The 56th Annual Meeting and Symposium of the Society of General Physiologists: trafficking of transporters. The Journal of General Physiology. 121: 73-9. PMID 12566536 DOI: 10.1085/Jgp.20038806  0.327
2002 Johnston JA, Illing ME, Kopito RR. Cytoplasmic dynein/dynactin mediates the assembly of aggresomes. Cell Motility and the Cytoskeleton. 53: 26-38. PMID 12211113 DOI: 10.1002/cm.10057  0.344
2002 Illing ME, Rajan RS, Bence NF, Kopito RR. A rhodopsin mutant linked to autosomal dominant retinitis pigmentosa is prone to aggregate and interacts with the ubiquitin proteasome system. The Journal of Biological Chemistry. 277: 34150-60. PMID 12091393 DOI: 10.1074/Jbc.M204955200  0.757
2002 Lenk U, Yu H, Walter J, Gelman MS, Hartmann E, Kopito RR, Sommer T. A role for mammalian Ubc6 homologues in ER-associated protein degradation. Journal of Cell Science. 115: 3007-14. PMID 12082160  0.432
2001 Rajan RS, Illing ME, Bence NF, Kopito RR. Specificity in intracellular protein aggregation and inclusion body formation. Proceedings of the National Academy of Sciences of the United States of America. 98: 13060-5. PMID 11687604 DOI: 10.1073/Pnas.181479798  0.792
2001 Bence NF, Sampat RM, Kopito RR. Impairment of the ubiquitin-proteasome system by protein aggregation. Science (New York, N.Y.). 292: 1552-5. PMID 11375494 DOI: 10.1126/science.292.5521.1552  0.794
2000 Kopito RR, Sitia R. Aggresomes and Russell bodies - Symptoms of cellular indigestion? Embo Reports. 1: 225-231. PMID 11256604  0.403
2000 Kopito RR. Aggresomes, inclusion bodies and protein aggregation Trends in Cell Biology. 10: 524-530. PMID 11121744 DOI: 10.1016/S0962-8924(00)01852-3  0.387
2000 Johnston JA, Dalton MJ, Gurney ME, Kopito RR. Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis. Proceedings of the National Academy of Sciences of the United States of America. 97: 12571-6. PMID 11050163 DOI: 10.1073/pnas.220417997  0.339
1999 Yu H, Kopito RR. The role of multiubiquitination in dislocation and degradation of the α subunit of the T cell antigen receptor Journal of Biological Chemistry. 274: 36852-36858. PMID 10601236 DOI: 10.1074/jbc.274.52.36852  0.313
1998 Johnston JA, Ward CL, Kopito RR. Aggresomes: A cellular response to misfolded proteins Journal of Cell Biology. 143: 1883-1898. PMID 9864362 DOI: 10.1083/jcb.143.7.1883  0.466
1998 Tang XB, Fujinaga J, Kopito R, Casey JR. Topology of the region surrounding Glu681 of human AE1 protein, the erythrocyte anion exchanger Journal of Biological Chemistry. 273: 22545-22553. PMID 9712881 DOI: 10.1074/Jbc.273.35.22545  0.362
1998 Sato S, Ward CL, Kopito RR. Cotranslational ubiquitination of cystic fibrosis transmembrane conductance regulator in vitro Journal of Biological Chemistry. 273: 7189-7192. PMID 9516408 DOI: 10.1074/jbc.273.13.7189  0.365
1997 Zeng W, Lee MG, Yan M, Diaz J, Benjamin I, Marino CR, Kopito R, Freedman S, Cotton C, Muallem S, Thomas P. Immuno and functional characterization of CFTR in submandibular and pancreatic acinar and duct cells. The American Journal of Physiology. 273: C442-55. PMID 9277342 DOI: 10.1152/Ajpcell.1997.273.2.C442  0.313
1997 Yu H, Kaung G, Kobayashi S, Kopito RR. Cytosolic degradation of T-cell receptor α chains by the proteasome Journal of Biological Chemistry. 272: 20800-20804. PMID 9252404 DOI: 10.1074/jbc.272.33.20800  0.31
1995 Sekler I, Kopito R, Casey JR. High level expression, partial purification, and functional reconstitution of the human AE1 anion exchanger in Saccharomyces cerevisiae Journal of Biological Chemistry. 270: 21028-21034. PMID 7673129 DOI: 10.1074/Jbc.270.36.21028  0.407
1995 Ward CL, Omura S, Kopito RR. Degradation of CFTR by the ubiquitin-proteasome pathway Cell. 83: 121-127. PMID 7553863 DOI: 10.1016/0092-8674(95)90240-6  0.332
1993 Ruetz S, Lindsey AE, Ward CL, Kopito RR. Functional activation of plasma membrane anion exchangers occurs in a pre- Golgi compartment Journal of Cell Biology. 121: 37-48. PMID 8458871  0.302
1993 Raley-Susman KM, Sapolsky RM, Kopito RR. Cl-/HCO3- exchange function differs in adult and fetal rat hippocampal neurons. Brain Research. 614: 308-14. PMID 8348323 DOI: 10.1016/0006-8993(93)91049-X  0.367
1991 Raley-Susman KM, Cragoe EJ, Sapolsky RM, Kopito RR. Regulation of intracellular pH in cultured hippocampal neurons by an amiloride-insensitive Na+/H+ exchanger. The Journal of Biological Chemistry. 266: 2739-45. PMID 1847131  0.397
1990 Lux SE, John KM, Kopito RR, Lodish HF. Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1). Proceedings of the National Academy of Sciences of the United States of America. 86: 9089-93. PMID 2594752 DOI: 10.1073/Pnas.86.23.9089  0.516
1989 Kellokumpu S, Neff L, Jämsä-Kellokumpu S, Kopito R, Baron R. A 115-kD polypeptide immunologically related to erythrocyte band 3 is present in Golgi membranes. Science (New York, N.Y.). 242: 1308-11. PMID 2461589 DOI: 10.1126/Science.2461589  0.348
1987 Kopito RR, Andersson MA, Lodish HF. Multiple tissue-specific sites of transcriptional initiation of the mouse anion antiport gene in erythroid and renal cells Proceedings of the National Academy of Sciences of the United States of America. 84: 7149-7153. PMID 3478687 DOI: 10.1073/Pnas.84.20.7149  0.38
1985 Kopito RR, Lodish HF. Structure of the murine anion exchange protein. Journal of Cellular Biochemistry. 29: 1-17. PMID 3840489 DOI: 10.1002/Jcb.240290102  0.465
1985 Kopito RR, Lodish HF. Primary structure and transmembrane orientation of the murine anion exchange protein. Nature. 316: 234-8. PMID 2410791 DOI: 10.1038/316234A0  0.43
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