Year |
Citation |
Score |
2020 |
Chernova TA, Yang Z, Karpova TS, Shanks JR, Shcherbik N, Wilkinson KD, Chernoff YO. Aggregation and Prion-Inducing Properties of the G-Protein Gamma Subunit Ste18 are Regulated by Membrane Association. International Journal of Molecular Sciences. 21. PMID 32708832 DOI: 10.3390/Ijms21145038 |
0.399 |
|
2019 |
Chernova TA, Chernoff YO, Wilkinson KD. Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery. Molecules (Basel, Switzerland). 24. PMID 31540362 DOI: 10.3390/Molecules24183388 |
0.387 |
|
2017 |
Chernova TA, Chernoff YO, Wilkinson KD. Prion-based memory of heat stress in yeast. Prion. 1-11. PMID 28521568 DOI: 10.1080/19336896.2017.1328342 |
0.343 |
|
2017 |
Chernova TA, Kiktev DA, Romanyuk AV, Shanks JR, Laur O, Ali M, Ghosh A, Kim D, Yang Z, Mang M, Chernoff YO, Wilkinson KD. Yeast Short-Lived Actin-Associated Protein Forms a Metastable Prion in Response to Thermal Stress. Cell Reports. 18: 751-761. PMID 28099852 DOI: 10.1016/J.Celrep.2016.12.082 |
0.416 |
|
2016 |
Chernova TA, Wilkinson KD, Chernoff YO. Prions, Chaperones, and Proteostasis in Yeast. Cold Spring Harbor Perspectives in Biology. PMID 27815300 DOI: 10.1101/Cshperspect.A023663 |
0.44 |
|
2015 |
Balakirev MY, Mullally JE, Favier A, Assard N, Sulpice E, Lindsey DF, Rulina AV, Gidrol X, Wilkinson KD. Wss1 metalloprotease partners with Cdc48/Doa1 in processing genotoxic SUMO conjugates. Elife. 4. PMID 26349035 DOI: 10.7554/Elife.06763 |
0.412 |
|
2015 |
Eletr ZM, Wilkinson KD. Quantitative analysis of protein-protein interactions. Methods in Molecular Biology (Clifton, N.J.). 1278: 23-37. PMID 25859941 DOI: 10.1007/978-1-4939-2425-7_2 |
0.405 |
|
2014 |
Ali M, Chernova TA, Newnam GP, Yin L, Shanks J, Karpova TS, Lee A, Laur O, Subramanian S, Kim D, McNally JG, Seyfried NT, Chernoff YO, Wilkinson KD. Stress-dependent proteolytic processing of the actin assembly protein Lsb1 modulates a yeast prion. The Journal of Biological Chemistry. 289: 27625-39. PMID 25143386 DOI: 10.1074/Jbc.M114.582429 |
0.468 |
|
2014 |
Chernova TA, Wilkinson KD, Chernoff YO. Physiological and environmental control of yeast prions. Fems Microbiology Reviews. 38: 326-44. PMID 24236638 DOI: 10.1111/1574-6976.12053 |
0.438 |
|
2014 |
Eletr ZM, Wilkinson KD. Regulation of proteolysis by human deubiquitinating enzymes. Biochimica Et Biophysica Acta. 1843: 114-28. PMID 23845989 DOI: 10.1016/J.Bbamcr.2013.06.027 |
0.604 |
|
2013 |
Eletr ZM, Yin L, Wilkinson KD. BAP1 is phosphorylated at serine 592 in S-phase following DNA damage. Febs Letters. 587: 3906-11. PMID 24211834 DOI: 10.1016/J.Febslet.2013.10.035 |
0.317 |
|
2012 |
Avvakumov GV, Walker JR, Xue S, Allali-Hassani A, Asinas A, Nair UB, Fang X, Zuo X, Wang YX, Wilkinson KD, Dhe-Paganon S. Two ZnF-UBP domains in isopeptidase T (USP5). Biochemistry. 51: 1188-98. PMID 22283393 DOI: 10.1021/Bi200854Q |
0.463 |
|
2011 |
Fushman D, Wilkinson KD. Structure and recognition of polyubiquitin chains of different lengths and linkage. F1000 Biology Reports. 3: 26. PMID 22162729 DOI: 10.3410/B3-26 |
0.442 |
|
2011 |
Chernova TA, Romanyuk AV, Karpova TS, Shanks JR, Ali M, Moffatt N, Howie RL, O'Dell A, McNally JG, Liebman SW, Chernoff YO, Wilkinson KD. Prion induction by the short-lived, stress-induced protein Lsb2 is regulated by ubiquitination and association with the actin cytoskeleton. Molecular Cell. 43: 242-52. PMID 21777813 DOI: 10.1016/J.Molcel.2011.07.001 |
0.452 |
|
2011 |
Eletr ZM, Wilkinson KD. An emerging model for BAP1's role in regulating cell cycle progression. Cell Biochemistry and Biophysics. 60: 3-11. PMID 21484256 DOI: 10.1007/S12013-011-9184-6 |
0.423 |
|
2011 |
Ye Y, Akutsu M, Reyes-Turcu F, Enchev RI, Wilkinson KD, Komander D. Polyubiquitin binding and cross-reactivity in the USP domain deubiquitinase USP21. Embo Reports. 12: 350-7. PMID 21399617 DOI: 10.1038/Embor.2011.17 |
0.474 |
|
2010 |
Kolli N, Mikolajczyk J, Drag M, Mukhopadhyay D, Moffatt N, Dasso M, Salvesen G, Wilkinson KD. Distribution and paralogue specificity of mammalian deSUMOylating enzymes. The Biochemical Journal. 430: 335-44. PMID 20590526 DOI: 10.1042/Bj20100504 |
0.517 |
|
2009 |
Wang Y, Mukhopadhyay D, Mathew S, Hasebe T, Heimeier RA, Azuma Y, Kolli N, Shi YB, Wilkinson KD, Dasso M. Identification and developmental expression of Xenopus laevis SUMO proteases. Plos One. 4: e8462. PMID 20041154 DOI: 10.1371/Journal.Pone.0008462 |
0.457 |
|
2009 |
Wilkinson KD. DUBs at a glance. Journal of Cell Science. 122: 2325-9. PMID 19571111 DOI: 10.1242/Jcs.041046 |
0.447 |
|
2009 |
Reyes-Turcu FE, Ventii KH, Wilkinson KD. Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes. Annual Review of Biochemistry. 78: 363-97. PMID 19489724 DOI: 10.1146/Annurev.Biochem.78.082307.091526 |
0.792 |
|
2009 |
Komander D, Reyes-Turcu F, Licchesi JD, Odenwaelder P, Wilkinson KD, Barford D. Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains. Embo Reports. 10: 466-73. PMID 19373254 DOI: 10.1038/Embor.2009.55 |
0.416 |
|
2009 |
Reyes-Turcu FE, Wilkinson KD. Polyubiquitin binding and disassembly by deubiquitinating enzymes. Chemical Reviews. 109: 1495-508. PMID 19243136 DOI: 10.1021/Cr800470J |
0.593 |
|
2009 |
Wang T, Yin L, Cooper EM, Lai MY, Dickey S, Pickart CM, Fushman D, Wilkinson KD, Cohen RE, Wolberger C. Evidence for bidentate substrate binding as the basis for the K48 linkage specificity of otubain 1. Journal of Molecular Biology. 386: 1011-23. PMID 19211026 DOI: 10.1016/J.Jmb.2008.12.085 |
0.368 |
|
2009 |
Shanks J, Burtnick MN, Brett PJ, Waag DM, Spurgers KB, Ribot WJ, Schell MA, Panchal RG, Gherardini FC, Wilkinson KD, Deshazer D. Burkholderia mallei tssM encodes a putative deubiquitinase that is secreted and expressed inside infected RAW 264.7 murine macrophages. Infection and Immunity. 77: 1636-48. PMID 19168747 DOI: 10.1128/Iai.01339-08 |
0.333 |
|
2009 |
Griffiths LM, Swartzlander D, Meadows KL, Wilkinson KD, Corbett AH, Doetsch PW. Dynamic compartmentalization of base excision repair proteins in response to nuclear and mitochondrial oxidative stress. Molecular and Cellular Biology. 29: 794-807. PMID 19029246 DOI: 10.1128/Mcb.01357-08 |
0.304 |
|
2008 |
Yun C, Wang Y, Mukhopadhyay D, Backlund P, Kolli N, Yergey A, Wilkinson KD, Dasso M. Nucleolar protein B23/nucleophosmin regulates the vertebrate SUMO pathway through SENP3 and SENP5 proteases. The Journal of Cell Biology. 183: 589-95. PMID 19015314 DOI: 10.1083/Jcb.200807185 |
0.418 |
|
2008 |
Ventii KH, Devi NS, Friedrich KL, Chernova TA, Tighiouart M, Van Meir EG, Wilkinson KD. BRCA1-associated protein-1 is a tumor suppressor that requires deubiquitinating activity and nuclear localization. Cancer Research. 68: 6953-62. PMID 18757409 DOI: 10.1158/0008-5472.Can-08-0365 |
0.731 |
|
2008 |
Ventii KH, Wilkinson KD. Protein partners of deubiquitinating enzymes. The Biochemical Journal. 414: 161-75. PMID 18687060 DOI: 10.1042/Bj20080798 |
0.791 |
|
2008 |
Drag M, Mikolajczyk J, Bekes M, Reyes-Turcu FE, Ellman JA, Wilkinson KD, Salvesen GS. Positional-scanning fluorigenic substrate libraries reveal unexpected specificity determinants of DUBs (deubiquitinating enzymes). The Biochemical Journal. 415: 367-75. PMID 18601651 DOI: 10.1042/Bj20080779 |
0.451 |
|
2008 |
Haas AL, Wilkinson KD. DeTEKting ubiquitination of APC/C substrates. Cell. 133: 570-2. PMID 18485863 DOI: 10.1016/J.Cell.2008.04.034 |
0.498 |
|
2008 |
Reyes-Turcu FE, Shanks JR, Komander D, Wilkinson KD. Recognition of polyubiquitin isoforms by the multiple ubiquitin binding modules of isopeptidase T. The Journal of Biological Chemistry. 283: 19581-92. PMID 18482987 DOI: 10.1074/Jbc.M800947200 |
0.458 |
|
2008 |
Nicholson B, Leach CA, Goldenberg SJ, Francis DM, Kodrasov MP, Tian X, Shanks J, Sterner DE, Bernal A, Mattern MR, Wilkinson KD, Butt TR. Characterization of ubiquitin and ubiquitin-like-protein isopeptidase activities. Protein Science : a Publication of the Protein Society. 17: 1035-43. PMID 18424514 DOI: 10.1110/Ps.083450408 |
0.526 |
|
2008 |
Balakirev MY, Wilkinson KD. OTU takes the chains OUT. Nature Chemical Biology. 4: 227-8. PMID 18347589 DOI: 10.1038/Nchembio0408-227 |
0.418 |
|
2008 |
Messick TE, Russell NS, Iwata AJ, Sarachan KL, Shiekhattar R, Shanks JR, Reyes-Turcu FE, Wilkinson KD, Marmorstein R. Structural basis for ubiquitin recognition by the Otu1 ovarian tumor domain protein. The Journal of Biological Chemistry. 283: 11038-49. PMID 18270205 DOI: 10.1074/Jbc.M704398200 |
0.746 |
|
2007 |
Chen Z, Wang Y, Ratia K, Mesecar AD, Wilkinson KD, Baker SC. Proteolytic processing and deubiquitinating activity of papain-like proteases of human coronavirus NL63. Journal of Virology. 81: 6007-18. PMID 17392370 DOI: 10.1128/Jvi.02747-06 |
0.451 |
|
2007 |
Allen KD, Chernova TA, Tennant EP, Wilkinson KD, Chernoff YO. Effects of ubiquitin system alterations on the formation and loss of a yeast prion. The Journal of Biological Chemistry. 282: 3004-13. PMID 17142456 DOI: 10.1074/Jbc.M609597200 |
0.388 |
|
2006 |
Mukhopadhyay D, Ayaydin F, Kolli N, Tan SH, Anan T, Kametaka A, Azuma Y, Wilkinson KD, Dasso M. SUSP1 antagonizes formation of highly SUMO2/3-conjugated species. The Journal of Cell Biology. 174: 939-49. PMID 17000875 DOI: 10.1083/Jcb.200510103 |
0.436 |
|
2006 |
Reyes-Turcu FE, Horton JR, Mullally JE, Heroux A, Cheng X, Wilkinson KD. The ubiquitin binding domain ZnF UBP recognizes the C-terminal diglycine motif of unanchored ubiquitin. Cell. 124: 1197-208. PMID 16564012 DOI: 10.1016/J.Cell.2006.02.038 |
0.48 |
|
2006 |
Mullally JE, Chernova T, Wilkinson KD. Doa1 is a Cdc48 adapter that possesses a novel ubiquitin binding domain. Molecular and Cellular Biology. 26: 822-30. PMID 16428438 DOI: 10.1128/Mcb.26.3.822-830.2006 |
0.465 |
|
2006 |
Yin L, Russell NS, Cheng D, Peng J, Wilkinson KD. Specificity of Ubiquitin-Binding Proteins: Recognition of Different Faces of Ubiquitin Israel Journal of Chemistry. 46: 159-169. DOI: 10.1560/46F8-Edwb-6Qxp-Cb14 |
0.716 |
|
2006 |
Finley D, Wilkinson KD. Cecile Pickart 1954–2006 Cell. 125: 635-637. DOI: 10.1016/J.Cell.2006.05.001 |
0.433 |
|
2005 |
Wilkinson KD, Gan-Erdene T, Kolli N. Derivitization of the C-terminus of ubiquitin and ubiquitin-like proteins using intein chemistry: methods and uses. Methods in Enzymology. 399: 37-51. PMID 16338347 DOI: 10.1016/S0076-6879(05)99003-4 |
0.492 |
|
2005 |
Wilkinson KD. The discovery of ubiquitin-dependent proteolysis. Proceedings of the National Academy of Sciences of the United States of America. 102: 15280-2. PMID 16230621 DOI: 10.1073/Pnas.0504842102 |
0.508 |
|
2005 |
Hu M, Li P, Song L, Jeffrey PD, Chenova TA, Wilkinson KD, Cohen RE, Shi Y. Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14. The Embo Journal. 24: 3747-56. PMID 16211010 DOI: 10.1038/Sj.Emboj.7600832 |
0.489 |
|
2005 |
Wilkinson KD, Ventii KH, Friedrich KL, Mullally JE. The ubiquitin signal: assembly, recognition and termination. Symposium on ubiquitin and signaling. Embo Reports. 6: 815-20. PMID 16113643 DOI: 10.1038/Sj.Embor.7400506 |
0.781 |
|
2005 |
Russell NS, Wilkinson KD. Deubiquitinating enzyme purification, assay inhibitors, and characterization. Methods in Molecular Biology (Clifton, N.J.). 301: 207-19. PMID 15917634 DOI: 10.1385/1-59259-895-1:207 |
0.683 |
|
2005 |
Chen C, Sun X, Ran Q, Wilkinson KD, Murphy TJ, Simons JW, Dong JT. Ubiquitin-proteasome degradation of KLF5 transcription factor in cancer and untransformed epithelial cells. Oncogene. 24: 3319-27. PMID 15735697 DOI: 10.1038/Sj.Onc.1208497 |
0.467 |
|
2005 |
Reverter D, Wu K, Erdene TG, Pan ZQ, Wilkinson KD, Lima CD. Structure of a complex between Nedd8 and the Ulp/Senp protease family member Den1. Journal of Molecular Biology. 345: 141-51. PMID 15567417 DOI: 10.1016/J.Jmb.2004.10.022 |
0.417 |
|
2005 |
Allen KD, Wegrzyn RD, Chernova TA, Müller S, Newnam GP, Winslett PA, Wittich KB, Wilkinson KD, Chernoff YO. Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]. Genetics. 169: 1227-42. PMID 15545639 DOI: 10.1534/Genetics.104.037168 |
0.439 |
|
2004 |
Wilkinson KD. Ubiquitin: a Nobel protein. Cell. 119: 741-5. PMID 15607971 DOI: 10.1016/J.Cell.2004.12.001 |
0.515 |
|
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, ... ... Wilkinson KD, et al. Varshavsky's contributions. Science (New York, N.Y.). 306: 1290-2. PMID 15550643 DOI: 10.1126/Science.306.5700.1290 |
0.409 |
|
2004 |
Kaytor MD, Wilkinson KD, Warren ST. Modulating huntingtin half-life alters polyglutamine-dependent aggregate formation and cell toxicity. Journal of Neurochemistry. 89: 962-73. PMID 15140195 DOI: 10.1111/J.1471-4159.2004.02376.X |
0.398 |
|
2004 |
Russell NS, Wilkinson KD. Identification of a novel 29-linked polyubiquitin binding protein, Ufd3, using polyubiquitin chain analogues. Biochemistry. 43: 4844-54. PMID 15096053 DOI: 10.1021/Bi035626R |
0.713 |
|
2004 |
Wilkinson KD. Quantitative analysis of protein-protein interactions. Methods in Molecular Biology (Clifton, N.J.). 261: 15-32. PMID 15064447 DOI: 10.1385/1-59259-762-9:015 |
0.342 |
|
2004 |
Hemelaar J, Borodovsky A, Kessler BM, Reverter D, Cook J, Kolli N, Gan-Erdene T, Wilkinson KD, Gill G, Lima CD, Ploegh HL, Ovaa H. Specific and covalent targeting of conjugating and deconjugating enzymes of ubiquitin-like proteins. Molecular and Cellular Biology. 24: 84-95. PMID 14673145 DOI: 10.1128/Mcb.24.1.84-95.2004 |
0.539 |
|
2004 |
Olzmann JA, Brown K, Wilkinson KD, Rees HD, Huai Q, Ke H, Levey AI, Li L, Chin LS. Familial Parkinson's disease-associated L166P mutation disrupts DJ-1 protein folding and function. The Journal of Biological Chemistry. 279: 8506-15. PMID 14665635 DOI: 10.1074/Jbc.M311017200 |
0.383 |
|
2003 |
Chernova TA, Allen KD, Wesoloski LM, Shanks JR, Chernoff YO, Wilkinson KD. Pleiotropic effects of Ubp6 loss on drug sensitivities and yeast prion are due to depletion of the free ubiquitin pool. The Journal of Biological Chemistry. 278: 52102-15. PMID 14559899 DOI: 10.1074/Jbc.M310283200 |
0.47 |
|
2003 |
Wilkinson KD. Signal transduction: aspirin, ubiquitin and cancer. Nature. 424: 738-9. PMID 12917671 DOI: 10.1038/424738A |
0.364 |
|
2003 |
Wu K, Yamoah K, Dolios G, Gan-Erdene T, Tan P, Chen A, Lee CG, Wei N, Wilkinson KD, Wang R, Pan ZQ. DEN1 is a dual function protease capable of processing the C terminus of Nedd8 and deconjugating hyper-neddylated CUL1. The Journal of Biological Chemistry. 278: 28882-91. PMID 12759363 DOI: 10.1074/Jbc.M302888200 |
0.464 |
|
2003 |
Gan-Erdene T, Nagamalleswari K, Yin L, Wu K, Pan ZQ, Wilkinson KD. Identification and characterization of DEN1, a deneddylase of the ULP family. The Journal of Biological Chemistry. 278: 28892-900. PMID 12759362 DOI: 10.1074/Jbc.M302890200 |
0.47 |
|
2002 |
Borodovsky A, Ovaa H, Kolli N, Gan-Erdene T, Wilkinson KD, Ploegh HL, Kessler BM. Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family. Chemistry & Biology. 9: 1149-59. PMID 12401499 DOI: 10.1016/S1074-5521(02)00248-X |
0.495 |
|
2002 |
Wilkinson KD. Cell biology: unchaining the condemned. Nature. 419: 351-3. PMID 12353019 DOI: 10.1038/419351A |
0.473 |
|
2001 |
Borodovsky A, Kessler BM, Casagrande R, Overkleeft HS, Wilkinson KD, Ploegh HL. A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14. The Embo Journal. 20: 5187-96. PMID 11566882 DOI: 10.1093/Emboj/20.18.5187 |
0.471 |
|
2001 |
Li Z, Zhang Y, Ku L, Wilkinson KD, Warren ST, Feng Y. The fragile X mental retardation protein inhibits translation via interacting with mRNA Nucleic Acids Research. 29: 2276-2283. PMID 11376146 DOI: 10.1093/Nar/29.11.2276 |
0.367 |
|
2000 |
Yin L, Krantz B, Russell NS, Deshpande S, Wilkinson KD. Nonhydrolyzable diubiquitin analogues are inhibitors of ubiquitin conjugation and deconjugation Biochemistry. 39: 10001-10010. PMID 10933821 DOI: 10.1021/Bi0007019 |
0.684 |
|
2000 |
Wilkinson KD. Ubiquitination and deubiquitination: targeting of proteins for degradation by the proteasome. Seminars in Cell & Developmental Biology. 11: 141-8. PMID 10906270 DOI: 10.1006/Scdb.2000.0164 |
0.567 |
|
2000 |
Crews C, Wilkinson KD, Wells L, Perkins C, Fridovich-Keil JL. Functional consequence of substitutions at residue 171 in human galactose-1-phosphate uridylyltransferase. The Journal of Biological Chemistry. 275: 22847-53. PMID 10811638 DOI: 10.1074/Jbc.M001053200 |
0.466 |
|
1999 |
Wilkinson KD. Ubiquitin-dependent signaling: the role of ubiquitination in the response of cells to their environment. The Journal of Nutrition. 129: 1933-6. PMID 10539765 DOI: 10.1093/Jn/129.11.1933 |
0.512 |
|
1999 |
Wilkinson KD, Laleli-Sahin E, Urbauer J, Larsen CN, Shih GH, Haas AL, Walsh ST, Wand AJ. The binding site for UCH-L3 on ubiquitin: mutagenesis and NMR studies on the complex between ubiquitin and UCH-L3. Journal of Molecular Biology. 291: 1067-77. PMID 10518943 DOI: 10.1006/Jmbi.1999.3038 |
0.469 |
|
1998 |
Leroy E, Boyer R, Auburger G, Leube B, Ulm G, Mezey E, Harta G, Brownstein MJ, Jonnalagada S, Chernova T, Dehejia A, Lavedan C, Gasser T, Steinbach PJ, Wilkinson KD, et al. The ubiquitin pathway in Parkinson's disease. Nature. 395: 451-2. PMID 9774100 DOI: 10.1038/26652 |
0.352 |
|
1998 |
Brown V, Small K, Lakkis L, Feng Y, Gunter C, Wilkinson KD, Warren ST. Purified recombinant Fmrp exhibits selective RNA binding as an intrinsic property of the fragile X mental retardation protein Journal of Biological Chemistry. 273: 15521-15527. PMID 9624140 DOI: 10.1074/Jbc.273.25.15521 |
0.364 |
|
1998 |
Jensen DE, Proctor M, Marquis ST, Gardner HP, Ha SI, Chodosh LA, Ishov AM, Tommerup N, Vissing H, Sekido Y, Minna J, Borodovsky A, Schultz DC, Wilkinson KD, Maul GG, et al. BAP1: a novel ubiquitin hydrolase which binds to the BRCA1 RING finger and enhances BRCA1-mediated cell growth suppression. Oncogene. 16: 1097-112. PMID 9528852 DOI: 10.1038/Sj.Onc.1201861 |
0.385 |
|
1998 |
Larsen CN, Krantz BA, Wilkinson KD. Substrate specificity of deubiquitinating enzymes: Ubiquitin C-terminal hydrolases Biochemistry. 37: 3358-3368. PMID 9521656 DOI: 10.1021/Bi972274D |
0.478 |
|
1998 |
Wilkinson KD. Regulation of ubiquitin-dependent processes by deubiquitinating enzymes. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 11: 1245-56. PMID 9409543 DOI: 10.1096/Fasebj.11.14.9409543 |
0.555 |
|
1998 |
Wilkinson KD. Cellular Regulation by Ubiquitin-Dependent Processes Advances in Molecular and Cell Biology. 27: 71-104. DOI: 10.1016/S1569-2558(08)60458-0 |
0.557 |
|
1997 |
Amerik AY, Swaminathan S, Krantz BA, Wilkinson KD, Hochstrasser M. In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome Embo Journal. 16: 4826-4838. PMID 9305625 DOI: 10.1093/Emboj/16.16.4826 |
0.533 |
|
1997 |
Johnston SC, Larsen CN, Cook WJ, Wilkinson KD, Hill CP. Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 A resolution. The Embo Journal. 16: 3787-96. PMID 9233788 DOI: 10.1093/Emboj/16.13.3787 |
0.386 |
|
1996 |
Larsen CN, Price JS, Wilkinson KD. Substrate binding and catalysis by ubiquitin C-terminal hydrolases: identification of two active site residues. Biochemistry. 35: 6735-44. PMID 8639624 DOI: 10.1021/Bi960099F |
0.468 |
|
1996 |
Wilkinson KD. Roles of ubiquitinylation in proteolysis and cellular regulation. Annual Review of Nutrition. 15: 161-89. PMID 8527216 DOI: 10.1146/Annurev.Nu.15.070195.001113 |
0.427 |
|
1995 |
Wilkinson KD, Tashayev VL, O'Connor LB, Larsen CN, Kasperek E, Pickart CM. Metabolism of the polyubiquitin degradation signal: structure, mechanism, and role of isopeptidase T. Biochemistry. 34: 14535-46. PMID 7578059 DOI: 10.1021/Bi00044A032 |
0.514 |
|
1993 |
Ashley CT, Wilkinson KD, Reines D, Warren ST. FMR1 protein: Conserved RNP family domains and selective RNA binding Science. 262: 563-566. PMID 7692601 DOI: 10.1126/Science.7692601 |
0.364 |
|
1990 |
Wilkinson KD, Smith SE, O'Connor L, Sternberg E, Taggart JJ, Berges DA, Butt T. A specific inhibitor of the ubiquitin activating enzyme: synthesis and characterization of adenosyl-phospho-ubiquitinol, a nonhydrolyzable ubiquitin adenylate analogue. Biochemistry. 29: 7373-80. PMID 2171643 DOI: 10.1021/Bi00484A004 |
0.475 |
|
1990 |
Wilkinson KD. Detection and inhibition of ubiquitin-dependent proteolysis. Methods in Enzymology. 185: 387-97. PMID 2166221 DOI: 10.1016/0076-6879(90)85034-L |
0.314 |
|
1990 |
Lowe J, McDermott H, Landon M, Mayer RJ, Wilkinson KD. Ubiquitin carboxyl-terminal hydrolase (PGP 9.5) is selectively present in ubiquitinated inclusion bodies characteristic of human neurodegenerative diseases. The Journal of Pathology. 161: 153-60. PMID 2166150 DOI: 10.1002/Path.1711610210 |
0.327 |
|
1989 |
Mayer AN, Wilkinson KD. Detection, resolution, and nomenclature of multiple ubiquitin carboxyl-terminal esterases from bovine calf thymus. Biochemistry. 28: 166-72. PMID 2539853 DOI: 10.1021/Bi00427A024 |
0.528 |
|
1989 |
Duerksen-Hughes PJ, Williamson MM, Wilkinson KD. Affinity chromatography using protein immobilized via arginine residues: purification of ubiquitin carboxyl-terminal hydrolases. Biochemistry. 28: 8530-6. PMID 2532544 DOI: 10.1021/Bi00447A039 |
0.461 |
|
1989 |
Wilkinson KD, Lee K, Deshpande S, Duerksen-Hughes P, Boss JM, Pohl J. The neuron-specific protein PGP 9.5 is a ubiquitin carboxyl-terminal hydrolase Science. 246: 670-673. PMID 2530630 DOI: 10.1126/Science.2530630 |
0.441 |
|
1989 |
Duerksen-Hughes PJ, Williamson MM, Wilkinson KD. Affinity chromatography using protein immobilized via arginine residues: Purification of ubiquitin carboxyl-terminal hydrolases Biochemistry. 28: 8530-8536. |
0.353 |
|
1988 |
Shapira R, Wilkinson KD, Shapira G. Racemization of individual aspartate residues in human myelin basic protein Journal of Neurochemistry. 50: 649-654. PMID 2447246 DOI: 10.1111/J.1471-4159.1988.Tb02960.X |
0.358 |
|
1987 |
Duerksen PJ, Wilkinson KD. Immobilization of proteins via arginine residues. Analytical Biochemistry. 160: 444-54. PMID 3034093 DOI: 10.1016/0003-2697(87)90074-1 |
0.482 |
|
1987 |
Wilkinson KD, Cox MJ, Mayer AN, Frey T. Synthesis and characterization of ubiquitin ethyl ester, a new substrate for ubiquitin carboxyl-terminal hydrolase. Biochemistry. 25: 6644-9. PMID 3024715 DOI: 10.1021/bi00369a047 |
0.319 |
|
1987 |
Duerksen-Hughes PJ, Xu X, Wilkinson KD. Structure and function of ubiquitin: Evidence for differential interactions of arginine-74 with the activating enzyme and the proteases of ATP-dependent proteolysis Biochemistry. 26: 6980-6987. PMID 2827740 DOI: 10.1021/Bi00396A019 |
0.449 |
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1986 |
Cox MJ, Haas AL, Wilkinson KD. Role of ubiquitin conformations in the specificity of protein degradation: Iodinated derivatives with altered conformations and activities Archives of Biochemistry and Biophysics. 250: 400-409. PMID 3022650 DOI: 10.1016/0003-9861(86)90742-3 |
0.513 |
|
1986 |
Wilkinson KD, Cox MJ, O'Connor LB, Shapira R. Structure and activities of a variant ubiquitin sequence from bakers' yeast. Biochemistry. 25: 4999-5004. PMID 3021209 DOI: 10.1021/bi00366a005 |
0.384 |
|
1985 |
Evans AC, Wilkinson KD. Ubiquitin-dependent proteolysis of native and alkylated bovine serum albumin: effects of protein structure and ATP concentration on selectivity. Biochemistry. 24: 2915-23. PMID 2990536 DOI: 10.1021/Bi00333A015 |
0.49 |
|
1985 |
Vijay-Kumar S, Bugg CE, Wilkinson KD, Cook WJ. Three-dimensional structure of ubiquitin at 2.8 A resolution. Proceedings of the National Academy of Sciences of the United States of America. 82: 3582-5. PMID 2987935 DOI: 10.1073/Pnas.82.11.3582 |
0.318 |
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1979 |
Williams CH, Arscott LD, Matthews RG, Thorpe C, Wilkinson KD. Methodology employed for anaerobic spectrophotometric titrations and for computer-assisted data analysis. Methods in Enzymology. 62: 185-98. PMID 374972 DOI: 10.1016/0076-6879(79)62217-6 |
0.306 |
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