Results 181 to 190 of about 538,441 (213)
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The role of deubiquitinating enzymes in apoptosis
Cellular and Molecular Life Sciences, 2010It has become apparent that ubiquitination plays a critical role in cell survival and cell death. In addition, deubiquitinating enzymes (DUBs) have been determined to be highly important regulators of these processes. Cells can be subjected to various stresses and respond in a variety of different ways ranging from activation of survival pathways to ...
Suresh, Ramakrishna +2 more
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1998
As detailed elsewhere in this volume, modification of proteins by the 76-residue ubiquitin polypeptide is involved in many aspects of protein metabolism. Among the cellular processes affected by ubiquitin-dependent reactions are chromosome structure and segregation, cell-cycle progression, receptor-mediated signal transduction, gene expression, protein
Keith D. Wilkinson, Mark Hochstrasser
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As detailed elsewhere in this volume, modification of proteins by the 76-residue ubiquitin polypeptide is involved in many aspects of protein metabolism. Among the cellular processes affected by ubiquitin-dependent reactions are chromosome structure and segregation, cell-cycle progression, receptor-mediated signal transduction, gene expression, protein
Keith D. Wilkinson, Mark Hochstrasser
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Deubiquitinating Enzymes as Cellular Regulators
Journal of Biochemistry, 2003Modification of proteins by the covalent attachment of ubiquitin is a key regulatory mechanism of many cellular processes including protein degradation by the 26S proteasome. Deubiquitination, reversal of this modification, must also regulate the fate and function of ubiquitin-conjugated proteins.
Jung Hwa, Kim +4 more
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Strategies for Assaying Deubiquitinating Enzymes
2005A general method for assaying deubiquitinating enzymes (DUBs) has been developed. This new method employs an indirect enzyme assay for determining the activity of DUBs using a linear fusion of polyHis-glutathione-S-transferase-ubiquitin-ecotin (His-GST-Ub-ecotin) as a substrate. Because ecotin, a trypsin inhibitor protein from Escherichia coli, is heat
Sung Hwan, Kang +4 more
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Deubiquitinating enzymes as novel anticancer targets [PDF]
Future Oncology, 2007 Tagging proteins with mono- or poly-ubiquitin is now recognized as a multifaceted and universal means of regulating cell growth and physiology. It does so by controlling the cellular lifetime of nearly all eukaryotic proteins and the cellular localization of many critical proteins.
Michael Mattern +2 more
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Polyubiquitin Binding and Disassembly By Deubiquitinating Enzymes [PDF]
Chemical Reviews, 2009 Ubiquitin (Ub) is a highly conserved protein of 76 amino acids that is covalently linked to target proteins altering their localization, function, or stability 1-3. Proteins can be modified with a large number of different isoforms of ubiquitin and these different ubiquitins are thought to signal different outcomes.
Keith D Wilkinson
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Mechanisms, biology and inhibitors of deubiquitinating enzymes
Nature Chemical Biology, 2007The addition of ubiquitin (Ub) and ubiquitin-like (Ubl) modifiers to proteins serves to modulate function and is a key step in protein degradation, epigenetic modification and intracellular localization. Deubiquitinating enzymes and Ubl-specific proteases, the proteins responsible for the removal of Ub and Ubls, act as an additional level of control ...
Kerry Routenberg, Love +3 more
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Targeting Deubiquitinating Enzymes
2009Deubiquitinating enzymes (DUBs) or isopeptidases belong to the enzyme class of hydrolases which include more than 100 members identified thus far. These proteins, which are grouped into four cysteine protease families and one metallo-protease family, catalyze the removal of ubiquitin from specific protein targets by cleavage of the linking isopeptide ...
Carmen Priolo +3 more
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Identification of a Deubiquitinating Enzyme
Science, 2007Modification of proteins by the covalent attachment of ubiquitin chains has emerged as a major regulatory mechanism in cells. The enzymes that oppose this reaction, the deubiquitinating enzymes, are relatively poorly understood. Kayagaki et al.
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Deubiquitinating Enzymes are IN(Trinsic to Proteasome Function)
Current Protein and Peptide Science, 2004Covalent conjugation of the ubiquitin tag to cellular proteins plays a central role in a number of processes, the most notable among them being degradation by the 26S proteasome. A fundamental property of this process is that ubiquitination, in contrast to subsequent degradation, is reversible due to a number of deubiquitinating enzymes that mediate ...
Adi, Guterman, Michael H, Glickman
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