Year |
Citation |
Score |
2023 |
Davis C, Spaller BL, Choi E, Kurrasch J, Chong H, Elsasser S, Finley D, Matouschek A. A strict requirement in proteasome substrates for spacing between ubiquitin tag and degradation initiation elements. Biorxiv : the Preprint Server For Biology. PMID 37609285 DOI: 10.1101/2023.08.08.552540 |
0.349 |
|
2023 |
Elsasser S, Elia LP, Morimoto RI, Powers ET, Elsasser S, Finley D, Costa B, Budron M, Tokuno Z, Wang S, Iyer RG, Barth B, Mockler E, Elia LP, Finkbeiner S, et al. A Comprehensive Enumeration of the Human Proteostasis Network. 2. Components of the Autophagy-Lysosome Pathway. Biorxiv : the Preprint Server For Biology. PMID 36993380 DOI: 10.1101/2023.03.22.533675 |
0.347 |
|
2022 |
Zhang S, Zou S, Yin D, Zhao L, Finley D, Wu Z, Mao Y. USP14-regulated allostery of the human proteasome by time-resolved cryo-EM. Nature. PMID 35477760 DOI: 10.1038/s41586-022-04671-8 |
0.329 |
|
2022 |
Cable J, Weber-Ban E, Clausen T, Walters KJ, Sharon M, Finley DJ, Gu Y, Hanna J, Feng Y, Martens S, Simonsen A, Hansen M, Zhang H, Goodwin JM, Reggio A, et al. Targeted protein degradation: from small molecules to complex organelles-a Keystone Symposia report. Annals of the New York Academy of Sciences. PMID 35000205 DOI: 10.1111/nyas.14745 |
0.444 |
|
2020 |
Whiteley AM, Prado MA, de Poot SAH, Paulo JA, Ashton M, Dominguez S, Weber M, Ngu H, Szpyt J, Jedrychowski MP, Easton A, Gygi SP, Kurz T, Monteiro MJ, Brown EJ, ... Finley D, et al. Global proteomics of Ubqln2-based murine models of ALS. The Journal of Biological Chemistry. PMID 33277362 DOI: 10.1074/jbc.RA120.015960 |
0.685 |
|
2020 |
Wu JJ, Cai A, Greenslade JE, Higgins NR, Fan C, Le NTT, Tatman M, Whiteley AM, Prado MA, Dieriks BV, Curtis MA, Shaw CE, Siddique T, Faull RLM, Scotter EL, ... Finley D, et al. ALS/FTD mutations in UBQLN2 impede autophagy by reducing autophagosome acidification through loss of function. Proceedings of the National Academy of Sciences of the United States of America. PMID 32513711 DOI: 10.1073/pnas.1917371117 |
0.604 |
|
2019 |
Ye Y, Klenerman D, Finley D. N-Terminal Ubiquitination of Amyloidogenic Proteins Triggers Removal of their Oligomers by the Proteasome Holoenzyme. Journal of Molecular Biology. PMID 31518613 DOI: 10.1016/J.Jmb.2019.08.021 |
0.318 |
|
2019 |
Finley D, Prado MA. The Proteasome and Its Network: Engineering for Adaptability. Cold Spring Harbor Perspectives in Biology. PMID 30833452 DOI: 10.1101/cshperspect.a033985 |
0.365 |
|
2018 |
Bretones G, Álvarez MG, Arango JR, Rodríguez D, Nadeu F, Prado MA, Valdés-Mas R, Puente DA, Paulo JA, Delgado J, Villamor N, López-Guillermo A, Finley DJ, Gygi SP, Campo E, et al. Altered patterns of global protein synthesis and translational fidelity in RPS15-mutated chronic lymphocytic leukemia. Blood. PMID 30181176 DOI: 10.1182/Blood-2017-09-804401 |
0.316 |
|
2017 |
de Poot SAH, Tian G, Finley D. Meddling with fate: The proteasomal deubiquitinating enzymes. Journal of Molecular Biology. PMID 28988953 DOI: 10.1016/j.jmb.2017.09.015 |
0.307 |
|
2017 |
Boselli M, Lee BH, Robert J, Prado MA, Min SW, Cheng C, Silva MC, Seong C, Elsasser S, Hatle KM, Gahman TC, Gygi SP, Haggarty SJ, Gan L, King RW, ... Finley D, et al. An inhibitor of the proteasomal deubiquitinating enzyme USP14 induces tau elimination in cultured neurons. The Journal of Biological Chemistry. PMID 28972160 DOI: 10.1074/Jbc.M117.815126 |
0.336 |
|
2017 |
Whiteley AM, Prado MA, Peng I, Abbas AR, Haley B, Paulo JA, Reichelt M, Katakam A, Sagolla M, Modrusan Z, Lee DY, Roose-Girma M, Kirkpatrick DS, McKenzie BS, Gygi SP, ... Finley D, et al. Ubiquilin1 promotes antigen-receptor mediated proliferation by eliminating mislocalized mitochondrial proteins. Elife. 6. PMID 28933694 DOI: 10.7554/Elife.26435 |
0.659 |
|
2017 |
Nguyen AT, Prado MA, Schmidt PJ, Sendamarai AK, Wilson-Grady JT, Min M, Campagna DR, Tian G, Shi Y, Dederer V, Kawan M, Kuehnle N, Paulo JA, Yao Y, Weiss MJ, ... ... Finley D, et al. UBE2O remodels the proteome during terminal erythroid differentiation. Science (New York, N.Y.). 357. PMID 28774900 DOI: 10.1126/Science.Aan0218 |
0.401 |
|
2016 |
Choi WH, de Poot SA, Lee JH, Kim JH, Han DH, Kim YK, Finley D, Lee MJ. Open-gate mutants of the mammalian proteasome show enhanced ubiquitin-conjugate degradation. Nature Communications. 7: 10963. PMID 26957043 DOI: 10.1038/ncomms10963 |
0.408 |
|
2015 |
Xu D, Shan B, Lee BH, Zhu K, Zhang T, Sun H, Liu M, Shi L, Liang W, Qian L, Xiao J, Wang L, Pan L, Finley D, Yuan J. Phosphorylation and activation of ubiquitin-specific protease-14 by Akt regulates the ubiquitin-proteasome system. Elife. 4. PMID 26523394 DOI: 10.7554/Elife.10510 |
0.302 |
|
2015 |
Isasa M, Rose CM, Elsasser S, Navarrete-Perea J, Paulo JA, Finley DJ, Gygi SP. Multiplexed, Proteome-Wide Protein Expression Profiling: Yeast Deubiquitylating Enzyme Knockout Strains. Journal of Proteome Research. PMID 26503604 DOI: 10.1021/Acs.Jproteome.5B00802 |
0.355 |
|
2015 |
Silva GM, Finley D, Vogel C. K63 polyubiquitination is a new modulator of the oxidative stress response. Nature Structural & Molecular Biology. 22: 116-23. PMID 25622294 DOI: 10.1038/nsmb.2955 |
0.344 |
|
2014 |
Liu YP, Tsai IC, Morleo M, Oh EC, Leitch CC, Massa F, Lee BH, Parker DS, Finley D, Zaghloul NA, Franco B, Katsanis N. Ciliopathy proteins regulate paracrine signaling by modulating proteasomal degradation of mediators. The Journal of Clinical Investigation. 124: 2059-70. PMID 24691443 DOI: 10.1172/Jci71898 |
0.371 |
|
2014 |
Hanna J, Waterman D, Isasa M, Elsasser S, Shi Y, Gygi S, Finley D. Cuz1/Ynl155w, a zinc-dependent ubiquitin-binding protein, protects cells from metalloid-induced proteotoxicity. The Journal of Biological Chemistry. 289: 1876-85. PMID 24297164 DOI: 10.1074/Jbc.M113.534032 |
0.762 |
|
2014 |
Schmidt M, Finley D. Regulation of proteasome activity in health and disease. Biochimica Et Biophysica Acta. 1843: 13-25. PMID 23994620 DOI: 10.1016/j.bbamcr.2013.08.012 |
0.438 |
|
2013 |
Ehlinger A, Park S, Fahmy A, Lary JW, Cole JL, Finley D, Walters KJ. Conformational dynamics of the Rpt6 ATPase in proteasome assembly and Rpn14 binding. Structure (London, England : 1993). 21: 753-65. PMID 23562395 DOI: 10.1016/J.Str.2013.02.021 |
0.351 |
|
2012 |
Finley D, Ulrich HD, Sommer T, Kaiser P. The ubiquitin-proteasome system of Saccharomyces cerevisiae. Genetics. 192: 319-60. PMID 23028185 DOI: 10.1534/Genetics.112.140467 |
0.453 |
|
2012 |
Hanna J, Waterman D, Boselli M, Finley D. Spg5 protein regulates the proteasome in quiescence. The Journal of Biological Chemistry. 287: 34400-9. PMID 22904326 DOI: 10.1074/Jbc.M112.390294 |
0.755 |
|
2012 |
Matouschek A, Finley D. Cell biology. An ancient portal to proteolysis. Science (New York, N.Y.). 337: 813-4. PMID 22904006 DOI: 10.1126/Science.1227301 |
0.463 |
|
2012 |
Elsasser S, Shi Y, Finley D. Binding of ubiquitin conjugates to proteasomes as visualized with native gels. Methods in Molecular Biology (Clifton, N.J.). 832: 403-22. PMID 22350901 DOI: 10.1007/978-1-61779-474-2_28 |
0.395 |
|
2011 |
Dange T, Smith D, Noy T, Rommel PC, Jurzitza L, Cordero RJ, Legendre A, Finley D, Goldberg AL, Schmidt M. Blm10 protein promotes proteasomal substrate turnover by an active gating mechanism. The Journal of Biological Chemistry. 286: 42830-9. PMID 22025621 DOI: 10.1074/jbc.M111.300178 |
0.361 |
|
2011 |
Finley D. Misfolded proteins driven to destruction by Hul5. Nature Cell Biology. 13: 1290-2. PMID 21983564 DOI: 10.1038/ncb2371 |
0.371 |
|
2011 |
Park S, Kim W, Tian G, Gygi SP, Finley D. Structural defects in the regulatory particle-core particle interface of the proteasome induce a novel proteasome stress response. The Journal of Biological Chemistry. 286: 36652-66. PMID 21878652 DOI: 10.1074/Jbc.M111.285924 |
0.304 |
|
2010 |
Lee BH, Lee MJ, Park S, Oh DC, Elsasser S, Chen PC, Gartner C, Dimova N, Hanna J, Gygi SP, Wilson SM, King RW, Finley D. Enhancement of proteasome activity by a small-molecule inhibitor of USP14. Nature. 467: 179-84. PMID 20829789 DOI: 10.1038/Nature09299 |
0.355 |
|
2010 |
Isasa M, Katz EJ, Kim W, Yugo V, González S, Kirkpatrick DS, Thomson TM, Finley D, Gygi SP, Crosas B. Monoubiquitination of RPN10 regulates substrate recruitment to the proteasome. Molecular Cell. 38: 733-45. PMID 20542005 DOI: 10.1016/J.Molcel.2010.05.001 |
0.359 |
|
2010 |
Park S, Tian G, Roelofs J, Finley D. Assembly manual for the proteasome regulatory particle: the first draft. Biochemical Society Transactions. 38: 6-13. PMID 20074027 DOI: 10.1042/Bst0380006 |
0.333 |
|
2009 |
Finley D. Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annual Review of Biochemistry. 78: 477-513. PMID 19489727 DOI: 10.1146/annurev.biochem.78.081507.101607 |
0.321 |
|
2009 |
Zhang F, Wu Z, Zhang P, Tian G, Finley D, Shi Y. Mechanism of substrate unfolding and translocation by the regulatory particle of the proteasome from Methanocaldococcus jannaschii. Molecular Cell. 34: 485-96. PMID 19481528 DOI: 10.1016/J.Molcel.2009.04.022 |
0.346 |
|
2009 |
Zhang F, Hu M, Tian G, Zhang P, Finley D, Jeffrey PD, Shi Y. Structural insights into the regulatory particle of the proteasome from Methanocaldococcus jannaschii. Molecular Cell. 34: 473-84. PMID 19481527 DOI: 10.1016/J.Molcel.2009.04.021 |
0.315 |
|
2009 |
Roelofs J, Park S, Haas W, Tian G, McAllister FE, Huo Y, Lee BH, Zhang F, Shi Y, Gygi SP, Finley D. Chaperone-mediated pathway of proteasome regulatory particle assembly. Nature. 459: 861-5. PMID 19412159 DOI: 10.1038/Nature08063 |
0.417 |
|
2009 |
Xu P, Duong DM, Seyfried NT, Cheng D, Xie Y, Robert J, Rush J, Hochstrasser M, Finley D, Peng J. Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation. Cell. 137: 133-45. PMID 19345192 DOI: 10.1016/J.Cell.2009.01.041 |
0.535 |
|
2008 |
Schreiner P, Chen X, Husnjak K, Randles L, Zhang N, Elsasser S, Finley D, Dikic I, Walters KJ, Groll M. Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction. Nature. 453: 548-52. PMID 18497827 DOI: 10.1038/Nature06924 |
0.377 |
|
2008 |
Goh AM, Walters KJ, Elsasser S, Verma R, Deshaies RJ, Finley D, Howley PM. Components of the ubiquitin-proteasome pathway compete for surfaces on Rad23 family proteins. Bmc Biochemistry. 9: 4. PMID 18234089 DOI: 10.1186/1471-2091-9-4 |
0.403 |
|
2007 |
Kleijnen MF, Roelofs J, Park S, Hathaway NA, Glickman M, King RW, Finley D. Stability of the proteasome can be regulated allosterically through engagement of its proteolytic active sites. Nature Structural & Molecular Biology. 14: 1180-8. PMID 18026118 DOI: 10.1038/Nsmb1335 |
0.314 |
|
2007 |
Hanna J, Meides A, Zhang DP, Finley D. A ubiquitin stress response induces altered proteasome composition. Cell. 129: 747-59. PMID 17512408 DOI: 10.1016/j.cell.2007.03.042 |
0.322 |
|
2007 |
Hanna J, Finley D. A proteasome for all occasions. Febs Letters. 581: 2854-61. PMID 17418826 DOI: 10.1016/j.febslet.2007.03.053 |
0.384 |
|
2006 |
Crosas B, Hanna J, Kirkpatrick DS, Zhang DP, Tone Y, Hathaway NA, Buecker C, Leggett DS, Schmidt M, King RW, Gygi SP, Finley D. Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities. Cell. 127: 1401-13. PMID 17190603 DOI: 10.1016/J.Cell.2006.09.051 |
0.305 |
|
2006 |
Hanna J, Hathaway NA, Tone Y, Crosas B, Elsasser S, Kirkpatrick DS, Leggett DS, Gygi SP, King RW, Finley D. Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degradation. Cell. 127: 99-111. PMID 17018280 DOI: 10.1016/J.Cell.2006.07.038 |
0.312 |
|
2006 |
Kirkpatrick DS, Hathaway NA, Hanna J, Elsasser S, Rush J, Finley D, King RW, Gygi SP. Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology. Nature Cell Biology. 8: 700-10. PMID 16799550 DOI: 10.1038/Ncb1436 |
0.337 |
|
2006 |
Wilkinson CRM, Dittmar GAG, Ohi MD, Uetz P, Jones N, Finley D. Ubiquitin-like Protein Hub1 Is Required for pre-mRNA Splicing and Localization of an Essential Splicing Factor in Fission Yeast (DOI:10.1016/j.cub.2004.11.058) Current Biology. 16: 2488. DOI: 10.1016/J.Cub.2006.12.004 |
0.313 |
|
2006 |
Finley D, Wilkinson KD. Cecile Pickart 1954–2006 Cell. 125: 635-637. DOI: 10.1016/J.Cell.2006.05.001 |
0.304 |
|
2005 |
Schmidt M, Hanna J, Elsasser S, Finley D. Proteasome-associated proteins: regulation of a proteolytic machine. Biological Chemistry. 386: 725-37. PMID 16201867 DOI: 10.1515/BC.2005.085 |
0.463 |
|
2005 |
Elsasser S, Finley D. Delivery of ubiquitinated substrates to protein-unfolding machines. Nature Cell Biology. 7: 742-9. PMID 16056265 DOI: 10.1038/ncb0805-742 |
0.435 |
|
2005 |
Leggett DS, Glickman MH, Finley D. Purification of proteasomes, proteasome subcomplexes, and proteasome-associated proteins from budding yeast. Methods in Molecular Biology (Clifton, N.J.). 301: 57-70. PMID 15917626 DOI: 10.1385/1-59259-895-1:057 |
0.396 |
|
2005 |
Shang F, Deng G, Liu Q, Guo W, Haas AL, Crosas B, Finley D, Taylor A. Lys6-modified ubiquitin inhibits ubiquitin-dependent protein degradation. The Journal of Biological Chemistry. 280: 20365-74. PMID 15790562 DOI: 10.1074/Jbc.M414356200 |
0.412 |
|
2005 |
Schmidt M, Haas W, Crosas B, Santamaria PG, Gygi SP, Walz T, Finley D. The HEAT repeat protein Blm10 regulates the yeast proteasome by capping the core particle. Nature Structural & Molecular Biology. 12: 294-303. PMID 15778719 DOI: 10.1038/Nsmb914 |
0.35 |
|
2004 |
Wilkinson CR, Dittmar GA, Ohi MD, Uetz P, Jones N, Finley D. Ubiquitin-like protein Hub1 is required for pre-mRNA splicing and localization of an essential splicing factor in fission yeast. Current Biology : Cb. 14: 2283-8. PMID 15620657 DOI: 10.1016/J.Cub.2004.11.058 |
0.407 |
|
2004 |
Baumeister W, Bachmair A, Chau V, Cohen R, Coffino P, Demartino G, Deshaies R, Dohmen J, Emr S, Finley D, Hampton R, Hill C, Hochstrasser M, Huber R, Jackson P, et al. Varshavsky's contributions. Science (New York, N.Y.). 306: 1290-2. PMID 15550643 DOI: 10.1126/Science.306.5700.1290 |
0.68 |
|
2004 |
Elsasser S, Chandler-Militello D, Müller B, Hanna J, Finley D. Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome. The Journal of Biological Chemistry. 279: 26817-22. PMID 15117949 DOI: 10.1074/jbc.M404020200 |
0.37 |
|
2004 |
Finley D, Ciechanover A, Varshavsky A. Ubiquitin as a central cellular regulator. Cell. 116: S29-32, 2 p followin. PMID 15055578 DOI: 10.1016/S0092-8674(03)00971-1 |
0.523 |
|
2004 |
Janse DM, Crosas B, Finley D, Church GM. Localization to the proteasome is sufficient for degradation. The Journal of Biological Chemistry. 279: 21415-20. PMID 15039430 DOI: 10.1074/Jbc.M402954200 |
0.408 |
|
2003 |
Hanna J, Leggett DS, Finley D. Ubiquitin depletion as a key mediator of toxicity by translational inhibitors. Molecular and Cellular Biology. 23: 9251-61. PMID 14645527 DOI: 10.1128/MCB.23.24.9251-9261.2003 |
0.353 |
|
2003 |
Peng J, Schwartz D, Elias JE, Thoreen CC, Cheng D, Marsischky G, Roelofs J, Finley D, Gygi SP. A proteomics approach to understanding protein ubiquitination. Nature Biotechnology. 21: 921-6. PMID 12872131 DOI: 10.1038/Nbt849 |
0.359 |
|
2003 |
Bajorek M, Finley D, Glickman MH. Proteasome disassembly and downregulation is correlated with viability during stationary phase. Current Biology : Cb. 13: 1140-4. PMID 12842014 DOI: 10.1016/S0960-9822(03)00417-2 |
0.304 |
|
2003 |
Santamaria PG, Finley D, Ballesta JP, Remacha M. Rpn6p, a proteasome subunit from Saccharomyces cerevisiae, is essential for the assembly and activity of the 26 S proteasome. The Journal of Biological Chemistry. 278: 6687-95. PMID 12486135 DOI: 10.1074/jbc.M209420200 |
0.342 |
|
2002 |
Leggett DS, Hanna J, Borodovsky A, Crosas B, Schmidt M, Baker RT, Walz T, Ploegh H, Finley D. Multiple associated proteins regulate proteasome structure and function. Molecular Cell. 10: 495-507. PMID 12408819 DOI: 10.1016/S1097-2765(02)00638-X |
0.426 |
|
2002 |
Elsasser S, Gali RR, Schwickart M, Larsen CN, Leggett DS, Müller B, Feng MT, Tübing F, Dittmar GA, Finley D. Proteasome subunit Rpn1 binds ubiquitin-like protein domains. Nature Cell Biology. 4: 725-30. PMID 12198498 DOI: 10.1038/ncb845 |
0.378 |
|
2002 |
Dittmar GA, Wilkinson CR, Jedrzejewski PT, Finley D. Role of a ubiquitin-like modification in polarized morphogenesis. Science (New York, N.Y.). 295: 2442-6. PMID 11923536 DOI: 10.1126/science.1069989 |
0.35 |
|
2002 |
Jarosch E, Taxis C, Volkwein C, Bordallo J, Finley D, Wolf DH, Sommer T. Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. Nature Cell Biology. 4: 134-9. PMID 11813000 DOI: 10.1038/Ncb746 |
0.413 |
|
2000 |
Spence J, Gali RR, Dittmar G, Sherman F, Karin M, Finley D. Cell cycle-regulated modification of the ribosome by a variant multiubiquitin chain Cell. 102: 67-76. PMID 10929714 DOI: 10.1016/S0092-8674(00)00011-8 |
0.33 |
|
1999 |
Braun BC, Glickman M, Kraft R, Dahlmann B, Kloetzel PM, Finley D, Schmidt M. The base of the proteasome regulatory particle exhibits chaperone-like activity Nature Cell Biology. 1: 221-226. PMID 10559920 |
0.389 |
|
1999 |
Horwich AL, Weber-Ban EU, Finley D. Chaperone rings in protein folding and degradation. Proceedings of the National Academy of Sciences of the United States of America. 96: 11033-40. PMID 10500119 DOI: 10.1073/Pnas.96.20.11033 |
0.32 |
|
1999 |
Fu H, Girod PA, Doelling JH, Van Nocker S, Hochstrasser M, Finley D, Vierstra RD. Structure and functional analyses of the 26S proteasome subunits from plants Plant 26S proteasome Molecular Biology Reports. 26: 137-146. PMID 10363660 DOI: 10.1023/A:1006926322501 |
0.596 |
|
1998 |
Glickman MH, Rubin DM, Coux O, Wefes I, Pfeifer G, Cjeka Z, Baumeister W, Fried VA, Finley D. A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and elF3 Cell. 94: 615-623. PMID 9741626 DOI: 10.1016/S0092-8674(00)81603-7 |
0.318 |
|
1998 |
Rubin DM, Glickman MH, Larsen CN, Dhruvakumar S, Finley D. Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome Embo Journal. 17: 4909-4919. PMID 9724628 DOI: 10.1093/emboj/17.17.4909 |
0.362 |
|
1998 |
Finley D, Tanaka K, Mann C, Feldmann H, Hochstrasser M, Vierstra R, Johnston S, Hampton R, Haber J, Mccusker J, Silver P, Frontali L, Thorsness P, Varshavsky A, Byers B, et al. Unified nomenclature for subunits of the Saccharomyces cerevisiae proteasome regulatory particle. Trends in Biochemical Sciences. 23: 244-5. PMID 9697412 DOI: 10.1016/S0968-0004(98)01222-5 |
0.676 |
|
1998 |
Fu H, Sadis S, Rubin DM, Glickman M, Van Nocker S, Finley D, Vierstra RD. Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 S proteasome subunit Mcb1 Journal of Biological Chemistry. 273: 1970-1981. PMID 9442033 DOI: 10.1074/Jbc.273.4.1970 |
0.309 |
|
1997 |
Rubin DM, Van Nocker S, Glickman M, Coux O, Wefes I, Sadis S, Fu H, Goldberg A, Vierstra R, Finley D. ATPase and ubiquitin-binding proteins of the yeast proteasome Molecular Biology Reports. 24: 17-26. PMID 9228276 DOI: 10.1023/A:1006844305067 |
0.443 |
|
1996 |
Van Nocker S, Sadis S, Rubin DM, Glickman M, Fu H, Coux O, Wefes I, Finley D, Vierstra RD. The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate- specific role in protein turnover Molecular and Cellular Biology. 16: 6020-6028. PMID 8887631 DOI: 10.1128/Mcb.16.11.6020 |
0.458 |
|
1995 |
Yaglom J, Linskens MHK, Sadis S, Rubin DM, Futcher B, Finley D. p34(Cdc28)-mediated control of Cln3 cyclin degradation Molecular and Cellular Biology. 15: 731-741. PMID 7823941 |
0.365 |
|
1995 |
Rubin DM, Finley D. Proteolysis: The proteasome: a protein-degrading organelle? Current Biology. 5: 854-858. PMID 7583140 DOI: 10.1016/S0960-9822(95)00172-2 |
0.416 |
|
1994 |
Finley D, Sadis S, Monia BP, Boucher P, Ecker DJ, Crooke ST, Chau V. Inhibition of proteolysis and cell cycle progression in a multiubiquitination-deficient yeast mutant. Molecular and Cellular Biology. 14: 5501-9. PMID 8035826 |
0.444 |
|
1993 |
Driscoll J, Brown MG, Finley D, Monaco JJ. MHC-linked LMP gene products specifically alter peptidase activities of the proteasome Nature. 365: 262-264. PMID 8371781 DOI: 10.1038/365262A0 |
0.315 |
|
1992 |
Park EC, Finley D, Szostak JW. A strategy for the generation of conditional mutations by protein destabilization. Proceedings of the National Academy of Sciences of the United States of America. 89: 1249-52. PMID 1311090 DOI: 10.1073/Pnas.89.4.1249 |
0.348 |
|
1991 |
Finley D, Chau V. Ubiquitination. Annual Review of Cell Biology. 7: 25-69. PMID 1667082 DOI: 10.1146/annurev.cb.07.110191.000325 |
0.321 |
|
1989 |
Varshavsky A, Bachmair A, Finley D, Gonda DK, Wünning I. Targeting of proteins for degradation. Biotechnology (Reading, Mass.). 13: 109-43. PMID 2553172 |
0.576 |
|
1989 |
Finley D, Bartel B, Varshavsky A. The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis. Nature. 338: 394-401. PMID 2538753 DOI: 10.1038/338394A0 |
0.746 |
|
1987 |
Varshavsky A, Bachmair A, Finley D. The N-end rule of selective protein turnover: mechanistic aspects and functional implications. Biochemical Society Transactions. 15: 815-6. PMID 3691950 DOI: 10.1042/Bst0150815 |
0.584 |
|
1987 |
Ozkaynak E, Finley D, Solomon MJ, Varshavsky A. The yeast ubiquitin genes: a family of natural gene fusions. The Embo Journal. 6: 1429-39. PMID 3038523 DOI: 10.1002/J.1460-2075.1987.Tb02384.X |
0.708 |
|
1987 |
Finley D, Ozkaynak E, Varshavsky A. The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses. Cell. 48: 1035-46. PMID 3030556 DOI: 10.1016/0092-8674(87)90711-2 |
0.636 |
|
1987 |
Varshavsky A, Bachmair A, Finley D. The N-End Rule of Selective Protein Turnover and Its Implications [Abstract Only] Philosophical Transactions of the Royal Society B. 317: 471-471. DOI: 10.1098/Rstb.1987.0073 |
0.622 |
|
1986 |
Bachmair A, Finley D, Varshavsky A. In vivo half-life of a protein is a function of its amino-terminal residue. Science (New York, N.Y.). 234: 179-86. PMID 3018930 DOI: 10.1126/Science.3018930 |
0.588 |
|
1986 |
Swerdlow PS, Finley D, Varshavsky A. Enhancement of immunoblot sensitivity by heating of hydrated filters. Analytical Biochemistry. 156: 147-53. PMID 3017146 DOI: 10.1016/0003-2697(86)90166-1 |
0.481 |
|
1985 |
Ciechanover A, Finley D, Varshavsky A. Mammalian cell cycle mutant defective in intracellular protein degradation and ubiquitin-protein conjugation. Progress in Clinical and Biological Research. 180: 17-31. PMID 2994083 |
0.664 |
|
1985 |
Finley D, Varshavsky A. The ubiquitin system: functions and mechanisms Trends in Biochemical Sciences. 10: 343-347. DOI: 10.1016/0968-0004(85)90108-2 |
0.683 |
|
1984 |
Ciechanover A, Finley D, Varshavsky A. The ubiquitin-mediated proteolytic pathway and mechanisms of energy-dependent intracellular protein degradation. Journal of Cellular Biochemistry. 24: 27-53. PMID 6327743 DOI: 10.1002/Jcb.240240104 |
0.62 |
|
1984 |
Ciechanover A, Finley D, Varshavsky A. Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85. Cell. 37: 57-66. PMID 6327060 DOI: 10.1016/0092-8674(84)90300-3 |
0.654 |
|
1984 |
Finley D, Ciechanover A, Varshavsky A. Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85. Cell. 37: 43-55. PMID 6327059 DOI: 10.1016/0092-8674(84)90299-X |
0.654 |
|
1984 |
Ozkaynak E, Finley D, Varshavsky A. The yeast ubiquitin gene: head-to-tail repeats encoding a polyubiquitin precursor protein. Nature. 312: 663-6. PMID 6095120 DOI: 10.1038/312663A0 |
0.661 |
|
1983 |
Varshavsky A, Levinger L, Sundin O, Barsoum J, Ozkaynak E, Swerdlow P, Finley D. Cellular and SV40 chromatin: replication, segregation, ubiquitination, nuclease-hypersensitive sites, HMG-containing nucleosomes, and heterochromatin-specific protein. Cold Spring Harbor Symposia On Quantitative Biology. 47: 511-28. PMID 6305564 DOI: 10.1101/Sqb.1983.047.01.061 |
0.57 |
|
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