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Science's STKE, 2003
Ubiquitination is associated with targeting of proteins for degradation (polyubiquitination) or regulation (monoubiquitination). Chen et al. stimulated synaptosomes (pinched off nerve terminals enriched in presynaptic components from brain) with high K + to depolarize the membranes, which in ...
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Ubiquitination is associated with targeting of proteins for degradation (polyubiquitination) or regulation (monoubiquitination). Chen et al. stimulated synaptosomes (pinched off nerve terminals enriched in presynaptic components from brain) with high K + to depolarize the membranes, which in ...
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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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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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USP7 Deubiquitinates and Stabilizes SIRT1
The Anatomical Record, 2019ABSTRACTThe NAD+‐dependent protein deacetylase silent information regulator 1 (SIRT1) targets multiple proteins for deacetylation, and it has been implicated in a variety of cellular pathways and human diseases. However, it remains unclear how the abundance of SIRT1 is regulated. Here, by mass spectrometry analysis of SIRT1‐containing protein complexes,
Nan Song +4 more
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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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Dysregulation of deubiquitination in breast cancer
GeneBreast cancer (BC) is a highly frequent malignant tumor that poses a serious threat to women's health and has different molecular subtypes, histological subtypes, and biological features, which act by activating oncogenic factors and suppressing cancer inhibitors.
Lili Kong, Xiaofeng Jin
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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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Dual roles of the Arabidopsis PEAT complex in histone H2A deubiquitination and H4K5 acetylation
Molecular Plant, 2023Danyang Yuan
exaly

