K. Wilkinson

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The discovery of ubiquitin-dependent proteolysis

Keith D Wilkinson, K. Wilkinson, 2005, Proceedings of the National Academy of Sciences of the United States of America.

Regulation of ubiquitin‐dependent processes by deubiquitinating enzymes

K. Wilkinson, 1997, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Molecular discrimination of structurally equivalent Lys 63‐linked and linear polyubiquitin chains

David Komander, D. Barford, K. Wilkinson, 2009, EMBO reports.

Comparison of the three-dimensional structures of human, yeast, and oat ubiquitin.

C. Bugg, R. Vierstra, K. Wilkinson, 1987, The Journal of biological chemistry.

Crystal structure of a deubiquitinating enzyme (human UCH‐L3) at 1.8 å resolution

K D Wilkinson, C. Hill, C. Larsen, 1997, The EMBO journal.

BAP1: a novel ubiquitin hydrolase which binds to the BRCA1 RING finger and enhances BRCA1-mediated cell growth suppression

Keith D Wilkinson, Niels Tommerup, H. Gardner, 1998, Oncogene.

Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes.

Keith D Wilkinson, K. Wilkinson, Francisca E. Reyes-Turcu, 2009, Annual review of biochemistry.

Structural Basis for Ubiquitin Recognition by the Otu1 Ovarian Tumor Domain Protein*

R. Shiekhattar, K. Wilkinson, R. Marmorstein, 2008, Journal of Biological Chemistry.

Polyubiquitin binding and disassembly by deubiquitinating enzymes.

Keith D Wilkinson, K. Wilkinson, Francisca E. Reyes-Turcu, 2009, Chemical reviews.

Aggregation and Prion-Inducing Properties of the G-Protein Gamma Subunit Ste18 are Regulated by Membrane Association

T. Karpova, K. Wilkinson, Y. Chernoff, 2020, International journal of molecular sciences.

The ubiquitin pathway in Parkinson's disease

Georg Auburger, Peter J. Steinbach, Eva Mezey, 1998, Nature.

Quantitation of Binding 15 15 From : Methods in Molecular Biology

K. Wilkinson, 2017 .

Quantitative analysis of protein-protein interactions.

K. Wilkinson, 2004, Methods in molecular biology.

Deubiquitinating enzyme purification, assay inhibitors, and characterization.

K. Wilkinson, N. Russell, 2005, Methods in molecular biology.

Specific and Covalent Targeting of Conjugating and Deconjugating Enzymes of Ubiquitin-Like Proteins

H. Ploegh, H. Ovaa, J. Hemelaar, 2004, Molecular and Cellular Biology.

Methodology employed for anaerobic spectrophotometric titrations and for computer-assisted data analysis.

R. Matthews, K. Wilkinson, C. Thorpe, 1979, Methods in enzymology.

Nucleolar protein B23/nucleophosmin regulates the vertebrate SUMO pathway through SENP3 and SENP5 proteases

A. Yergey, P. Backlund, K. Wilkinson, 2008, The Journal of cell biology.

Nucleolar protein B 23 / nucleophosmin regulates the vertebrate SUMO pathway through SENP 3 and SENP 5 proteases

A. Yergey, P. Backlund, K. Wilkinson, 2008 .

SUSP1 antagonizes formation of highly SUMO2/3-conjugated species

K. Wilkinson, T. Anan, M. Dasso, 2006, The Journal of cell biology.

Specific and Covalent Targeting of Conjugating and Deconjugating Enzymes of Ubiquitin-Like Proteins

H. Ploegh, H. Ovaa, J. Hemelaar, 2004, Molecular and Cellular Biology.

Two ZnF-UBP domains in isopeptidase T (USP5).

Yun-Xing Wang, K. Wilkinson, X. Zuo, 2012, Biochemistry.

Identification and Developmental Expression of Xenopus laevis SUMO Proteases

K. Wilkinson, M. Dasso, Yunbo Shi, 2009, PloS one.

Derivitization of the C-terminus of ubiquitin and ubiquitin-like proteins using intein chemistry: methods and uses.

K. Wilkinson, T. Gan-Erdene, Nagamalleswari Kolli, 2005, Methods in enzymology.

Substrate binding and catalysis by ubiquitin C-terminal hydrolases: identification of two active site residues.

C. Larsen, K. Wilkinson, J. S. Price, 1996, Biochemistry.

DUBs at a glance

K. Wilkinson, 2009, Journal of Cell Science.

Signal transduction: Aspirin, ubiquitin and cancer

K. Wilkinson, 2003, Nature.

Identification of a novel 29-linked polyubiquitin binding protein, Ufd3, using polyubiquitin chain analogues.

K. Wilkinson, N. Russell, 2004, Biochemistry.

Specificity of Ubiquitin-Binding Proteins: Recognition of Different Faces of Ubiquitin

Luming Yin, K. Wilkinson, Dongmei Cheng, 2006 .

Cell biology: Unchaining the condemned

K. Wilkinson, 2002, Nature.

Ubiquitination and deubiquitination: targeting of proteins for degradation by the proteasome.

K. Wilkinson, 2000, Seminars in cell & developmental biology.

Affinity chromatography using protein immobilized via arginine residues: purification of ubiquitin carboxyl-terminal hydrolases.

K. Wilkinson, P. Duerksen-Hughes, M. M. Williamson, 1989, Biochemistry.

Synthesis and characterization of ubiquitin ethyl ester, a new substrate for ubiquitin carboxyl-terminal hydrolase.

K. Wilkinson, T. Frey, M. J. Cox, 1986, Biochemistry.

β-Arrestin-dependent signaling and trafficking of 7-transmembrane receptors is reciprocally regulated by the deubiquitinase USP33 and the E3 ligase Mdm2

R. Lefkowitz, K. Wilkinson, W. Miller, 2009, Proceedings of the National Academy of Sciences.

Ubiquitin carboxyl‐terminal hydrolase (PGP 9.5) is selectively present in ubiquitinated inclusion bodies characteristic of human neurodegenerative diseases

J. Lowe, K. Wilkinson, R. Mayer, 1990, The Journal of pathology.

OTU takes the chains OUT.

M. Balakirev, K. Wilkinson, 2008, Nature chemical biology.

Role of ubiquitin conformations in the specificity of protein degradation: iodinated derivatives with altered conformations and activities.

A. Haas, K. Wilkinson, M. J. Cox, 1986, Archives of biochemistry and biophysics.

Tryptic peptide mapping of ubiquitin and derivatives using reverse-phase high performance liquid chromatography.

K. Wilkinson, R. Shapira, M. J. Cox, 1986, Analytical biochemistry.

Prion induction by the short-lived, stress-induced protein Lsb2 is regulated by ubiquitination and association with the actin cytoskeleton.

J. McNally, T. Karpova, K. Wilkinson, 2011, Molecular cell.

The ubiquitin signal: assembly, recognition and termination

K. Wilkinson, J. Mullally, K. Friedrich, 2005 .

The ubiquitin signal: assembly, recognition and termination. Symposium on ubiquitin and signaling.

K. Wilkinson, J. Mullally, K. Friedrich, 2005, EMBO reports.

Comparisons of neuronal (PGP 9.5) and non-neuronal ubiquitin C-terminal hydrolases.

C. Larsen, K. Wilkinson, Seema S. Deshpande, 1992, Biochemical Society transactions.

Ubiquitin–proteasome degradation of KLF5 transcription factor in cancer and untransformed epithelial cells

J. Simons, K. Wilkinson, T. Murphy, 2005, Oncogene.

Characterization of ubiquitin and ubiquitin-like-protein isopeptidase activities

D. Sterner, T. Butt, K. Wilkinson, 2008, Protein science : a publication of the Protein Society.

An -N-acetyl-D-glycosamine binding lectin from Bandeiraea simplicifolia seeds.

I. Goldstein, K. Wilkinson, L. Goldstein, 1976, Archives of biochemistry and biophysics.

The neuron-specific protein PGP 9.5 is a ubiquitin carboxyl-terminal hydrolase.

K D Wilkinson, K. Wilkinson, P. Duerksen-Hughes, 1989, Science.

Detection, resolution, and nomenclature of multiple ubiquitin carboxyl-terminal esterases from bovine calf thymus.

K. Wilkinson, Alan N. Mayer, A. Mayer, 1989, Biochemistry.

Stimulation of ATP-dependent proteolysis requires ubiquitin with the COOH-terminal sequence Arg-Gly-Gly.

K. Wilkinson, T. Audhya, 1981, The Journal of biological chemistry.

The fragile X mental retardation protein inhibits translation via interacting with mRNA.

S. Warren, K. Wilkinson, Yue Feng, 2001, Nucleic acids research.

Immobilization of proteins via arginine residues.

K. Wilkinson, P. Duerksen, 1987, Analytical biochemistry.

Nonhydrolyzable diubiquitin analogues are inhibitors of ubiquitin conjugation and deconjugation.

K. Wilkinson, B. Krantz, N. Russell, 2000, Biochemistry.

Racemization of Individual Aspartate Residues in Human Myelin Basic Protein

K. Wilkinson, R. Shapira, G. Shapira, 1988, Journal of neurochemistry.

FMR1 protein: conserved RNP family domains and selective RNA binding.

S. Warren, C. T. Ashley, K. Wilkinson, 1993, Science.

Burkholderia mallei tssM Encodes a Putative Deubiquitinase That Is Secreted and Expressed inside Infected RAW 264.7 Murine Macrophages

M. Schell, D. DeShazer, K. Wilkinson, 2009, Infection and Immunity.

A specific inhibitor of the ubiquitin activating enzyme: synthesis and characterization of adenosyl-phospho-ubiquitinol, a nonhydrolyzable ubiquitin adenylate analogue.

K. Wilkinson, E. Sternberg, S. Smith, 1990, Biochemistry.

Purification and Structural Properties of Ubiquitin

K. Wilkinson, 1988 .

Regulation of proteolysis by human deubiquitinating enzymes.

Ziad M. Eletr, K. Wilkinson, 2014, Biochimica et biophysica acta.

Evidence for bidentate substrate binding as the basis for the K48 linkage specificity of otubain 1.

Tao Wang, Cynthia Wolberger, Keith D Wilkinson, 2009, Journal of molecular biology.

Human genes containing polymorphic trinucleotide repeats

G. Riggins, S. Warren, J. L. Chastain, 1992, Nature Genetics.

Recognition of Polyubiquitin Isoforms by the Multiple Ubiquitin Binding Modules of Isopeptidase T*

K. Wilkinson, D. Komander, Francisca E. Reyes-Turcu, 2008, Journal of Biological Chemistry.

Microarray Identification of FMRP-Associated Brain mRNAs and Altered mRNA Translational Profiles in Fragile X Syndrome

J. Darnell, R. Darnell, P. Jin, 2001, Cell.

BRCA1-associated protein-1 is a tumor suppressor that requires deubiquitinating activity and nuclear localization.

Erwin G. Van Meir, K. Wilkinson, T. Chernova, 2008, Cancer research.

BAP1 is a tumor suppressor that requires deubiquitinating activity and nuclear localization

Erwin G. Van Meir, K. Wilkinson, T. Chernova, 2022 .

Divergent N-terminal Sequences of a Deubiquitinating Enzyme Modulate Substrate Specificity*

Luming Yin, K. Wilkinson, S. Wing, 2001, The Journal of Biological Chemistry.

Dynamic Compartmentalization of Base Excision Repair Proteins in Response to Nuclear and Mitochondrial Oxidative Stress

K. Wilkinson, A. Corbett, P. Doetsch, 2008, Molecular and Cellular Biology.

Physiological and environmental control of yeast prions.

K. Wilkinson, Y. Chernoff, T. Chernova, 2014, FEMS microbiology reviews.

Wss1 metalloprotease partners with Cdc48/Doa1 in processing genotoxic SUMO conjugates

X. Gidrol, M. Balakirev, K. Wilkinson, 2015, eLife.

Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family.

H. Ploegh, H. Ovaa, K. Wilkinson, 2002, Chemistry & biology.

Prions, Chaperones, and Proteostasis in Yeast.

K. Wilkinson, Y. Chernoff, T. Chernova, 2017, Cold Spring Harbor perspectives in biology.

Protein partners of deubiquitinating enzymes.

K. Wilkinson, Karen H. Ventii, 2008, The Biochemical journal.

In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome

A. Amerik, M. Hochstrasser, K. Wilkinson, 1997, The EMBO journal.

Metabolism of the polyubiquitin degradation signal: structure, mechanism, and role of isopeptidase T.

C. Larsen, C. Pickart, K. Wilkinson, 1995, Biochemistry.

Functional Consequence of Substitutions at Residue 171 in Human Galactose-1-phosphate Uridylyltransferase*

J. Fridovich-Keil, K. Wilkinson, L. Wells, 2000, The Journal of Biological Chemistry.

Functional Requirements of the Active Site Position 185 in the Human Enzyme Galactose-1-phosphate Uridylyltransferase*

B. Quimby, J. Fridovich-Keil, K. Wilkinson, 1996, The Journal of Biological Chemistry.

Three-dimensional structure of ubiquitin at 2.8 A resolution.

K D Wilkinson, C. Bugg, K. Wilkinson, 1985, Proceedings of the National Academy of Sciences of the United States of America.

Purified Recombinant Fmrp Exhibits Selective RNA Binding as an Intrinsic Property of the Fragile X Mental Retardation Protein*

C. Gunter, S. Warren, V. Brown, 1998, The Journal of Biological Chemistry.

Author response: Wss1 metalloprotease partners with Cdc48/Doa1 in processing genotoxic SUMO conjugates

X. Gidrol, M. Balakirev, K. Wilkinson, 2015 .

Prion-based memory of heat stress in yeast

K. Wilkinson, Y. Chernoff, T. Chernova, 2017, Prion.

Hsp70 Chaperones as Modulators of Prion Life Cycle

S. Müller, K. Wilkinson, Y. Chernoff, 2005, Genetics.

A novel active site‐directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14

H. Ploegh, K. Wilkinson, B. Kessler, 2001, The EMBO journal.

The Ubiquitin Binding Domain ZnF UBP Recognizes the C-Terminal Diglycine Motif of Unanchored Ubiquitin

Xiaodong Cheng, K. Wilkinson, J. Horton, 2006, Cell.

Ubiquitin is the ATP-dependent proteolysis factor I of rabbit reticulocytes.

A. Haas, K. Wilkinson, M. Urban, 1980, The Journal of biological chemistry.

Doa1 Is a Cdc48 Adapter That Possesses a Novel Ubiquitin Binding Domain

K. Wilkinson, T. Chernova, J. Mullally, 2006, Molecular and Cellular Biology.

NADH inhibition and NAD activation of Escherichia coli lipoamide dehydrogenase catalyzing the NADH-lipoamide reaction.

K. Wilkinson, C. Williams, 1981, The Journal of biological chemistry.

Evidence for multiple electronic forms of two-electron-reduced lipoamide dehydrogenase from Escherichia coli.

K. Wilkinson, C. Williams, 1979, The Journal of biological chemistry.

Inhibition of the 26 S Proteasome by Polyubiquitin Chains Synthesized to Have Defined Lengths*

C. Pickart, K. Wilkinson, L. Hoffman, 1997, The Journal of Biological Chemistry.

BAP1 is phosphorylated at serine 592 in S‐phase following DNA damage

Luming Yin, Ziad M. Eletr, K. Wilkinson, 2013, FEBS letters.

Interactions of guanidinium chloride and pyridine nucleotides with oxidized and two-electron-reduced lipoamide dehydrogenase from Escherichia coli.

K. Wilkinson, C. Williams, 1979, The Journal of biological chemistry.

Structure and mechanisms of the proteasome‐associated deubiquitinating enzyme USP14

Yigong Shi, Yigong Shi, P. Jeffrey, 2005, The EMBO journal.

Proteolytic Processing and Deubiquitinating Activity of Papain-Like Proteases of Human Coronavirus NL63

A. Mesecar, K. Wilkinson, K. Ratia, 2007, Journal of Virology.

An Emerging Model for BAP1’s Role in Regulating Cell Cycle Progression

Ziad M. Eletr, K. Wilkinson, 2011, Cell Biochemistry and Biophysics.

Pleiotropic Effects of Ubp6 Loss on Drug Sensitivities and Yeast Prion Are Due to Depletion of the Free Ubiquitin Pool*

K. Wilkinson, Y. Chernoff, T. Chernova, 2003, Journal of Biological Chemistry.

Stress-dependent Proteolytic Processing of the Actin Assembly Protein Lsb1 Modulates a Yeast Prion*

N. Seyfried, J. McNally, Luming Yin, 2014, The Journal of Biological Chemistry.

Yeast Prion the Actin Assembly Protein Lsb 1 Stress-dependent Proteolytic Processing of Molecular Bases of Disease :

N. Seyfried, J. McNally, Luming Yin, 2014 .

Structure of a complex between Nedd8 and the Ulp/Senp protease family member Den1.

Keith D Wilkinson, David Reverter, Kenneth Wu, 2005, Journal of molecular biology.

Identification and Characterization of DEN1, a Deneddylase of the ULP Family*

Luming Yin, K. Wilkinson, Z. Pan, 2003, Journal of Biological Chemistry.

Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery

K. Wilkinson, Y. Chernoff, T. Chernova, 2019, Molecules.

Recent Advances in Nutritional Sciences Ubiquitin-Dependent Signaling : The Role of Ubiquitination in the Response of Cells to Their Environment . 1

K. Wilkinson, 1999 .

DEN1 Is a Dual Function Protease Capable of Processing the C Terminus of Nedd8 and Deconjugating Hyper-neddylated CUL1*

N. Wei, K. Wilkinson, Angus Chen, 2003, Journal of Biological Chemistry.

Distribution and paralogue specificity of mammalian deSUMOylating enzymes.

Keith D Wilkinson, J. Mikolajczyk, G. Salvesen, 2010, The Biochemical journal.

Modulating huntingtin half‐life alters polyglutamine‐dependent aggregate formation and cell toxicity

K. Wilkinson, M. D. Kaytor, S. T. Warren, 2004, Journal of neurochemistry.

The Deubiquitinating Enzymes

K. Wilkinson, N. Russell, 2008 .

The binding site for UCH-L3 on ubiquitin: mutagenesis and NMR studies on the complex between ubiquitin and UCH-L3.

A. Wand, A. Haas, S. Walsh, 1999, Journal of molecular biology.

Cellular Regulation by Ubiquitin-Dependent Processes

K. Wilkinson, 1998 .

Roles of ubiquitinylation in proteolysis and cellular regulation.

K. Wilkinson, 1995, Annual review of nutrition.

Effects of Ubiquitin System Alterations on the Formation and Loss of a Yeast Prion*♦

K. Wilkinson, Y. Chernoff, T. Chernova, 2007, Journal of Biological Chemistry.

Polyubiquitin binding and cross‐reactivity in the USP domain deubiquitinase USP21

Keith D Wilkinson, Masato Akutsu, David Komander, 2011, EMBO reports.

Structure and recognition of polyubiquitin chains of different lengths and linkage

D. Fushman, K. Wilkinson, David Fushman, 2011, F1000 biology reports.

Yeast Short-Lived Actin-Associated Protein Forms a Metastable Prion in Response to Thermal Stress.

K. Wilkinson, Y. Chernoff, T. Chernova, 2017, Cell reports.

A suggestion for naming faces of ring compounds.

K D Wilkinson, I. A. Rose, K. Wilkinson, 1980, Proceedings of the National Academy of Sciences of the United States of America.

Detection and inhibition of ubiquitin-dependent proteolysis.

K. Wilkinson, 1990, Methods in enzymology.

Molecular discrimination of structurally equivalent Lys 63‐linked and linear polyubiquitin chains

D. Barford, K. Wilkinson, D. Komander, 2009 .

Familial Parkinson's Disease-associated L166P Mutation Disrupts DJ-1 Protein Folding and Function*

Keith D Wilkinson, A. Levey, H. Ke, 2004, Journal of Biological Chemistry.

Ubiquitin-dependent signaling: the role of ubiquitination in the response of cells to their environment.

K. Wilkinson, 1999, The Journal of nutrition.

Positional-scanning fluorigenic substrate libraries reveal unexpected specificity determinants of DUBs (deubiquitinating enzymes).

J. Mikolajczyk, G. Salvesen, K. Wilkinson, 2008, The Biochemical journal.

Substrate specificity of deubiquitinating enzymes: ubiquitin C-terminal hydrolases.

K D Wilkinson, C. Larsen, K. Wilkinson, 1998, Biochemistry.

Protein ubiquitination: a regulatory post-translational modification.

K D Wilkinson, K. Wilkinson, 1987, Anti-cancer drug design.

Structure and function of ubiquitin: evidence for differential interactions of arginine-74 with the activating enzyme and the proteases of ATP-dependent proteolysis.

K. Wilkinson, P. Duerksen-Hughes, X. X. Xu, 1987, Biochemistry.

Alcohol-induced conformational changes of ubiquitin.

K. Wilkinson, Alan N. Mayer, A. Mayer, 1986, Archives of Biochemistry and Biophysics.

The large scale purification of ubiquitin from human erythrocytes.

A. Haas, K. Wilkinson, 1985, Preparative biochemistry.

Quantitative analysis of protein-protein interactions.

Ziad M Eletr, Keith D Wilkinson, Ziad M. Eletr, 2015, Methods in molecular biology.

Glucose exchange and catalysis by two crystalline hexokinase x glucose complexes. Evidence for an obligatory ATP-dependent conformational change in catalysis.

I. A. Rose, K. Wilkinson, 1980, The Journal of biological chemistry.

Isotope trapping studies of yeast hexokinase during steady state catalysis. A combined rapid quench and isotope trapping technique.

I. A. Rose, K. Wilkinson, 1979, The Journal of biological chemistry.

Ubiquitin-dependent proteolysis of native and alkylated bovine serum albumin: effects of protein structure and ATP concentration on selectivity.

K. Wilkinson, A. Evans, 1985, Biochemistry.

Identification and developmental expression of Xenopus laevis SUMO proteases.

K. Wilkinson, M. Dasso, Yunbo Shi, 2009 .

Structure and activities of a variant ubiquitin sequence from bakers' yeast.

K. Wilkinson, R. Shapira, L. O'Connor, 1986, Biochemistry.

Polyubiquitin binding and disassembly by deubiquitinating enzymes.

K. Wilkinson, Francisca E. Reyes-Turcu, 2009, Chemical reviews.

Prions, Chaperones, and Proteostasis in Yeast.

K. Wilkinson, Y. Chernoff, T. Chernova, 2017, Cold Spring Harbor perspectives in biology.

125I-ubiquitin is kinetically invalid as a tracer radiolabel for studies of ATP-dependent proteolysis.

K. Wilkinson, M. J. Cox, 1985, Progress in clinical and biological research.