Results 211 to 220 of about 28,234 (247)
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Deubiquitinating enzyme YOD1 deubiquitinates and destabilizes α-synuclein
Biochemical and Biophysical Research Communications, 2023α-synuclein is one of the proteins involved in degenerative neuronal diseases such as Parkinson's disease (PD) or Lewy body dementia (LBD). The pathogenesis is imparted by the abnormal accumulation of α-synuclein resulting in the formation of a Lewy body (LB) and exerting neurotoxicity via an unknown mechanism.
Sang-Soo Park +4 more
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Acta Pharmaceutica Sinica B, 2023 Deubiquitinating enzymes (DUBs) or deubiquitinases facilitate the escape of multiple proteins from ubiquitin‒proteasome degradation and are critical for regulating protein expression levels in vivo. Therefore, dissecting the underlying mechanism of DUB recognition is needed to advance the development of drugs related to DUB signaling pathways. To data,
Qiaojun He, Ji Cao, Yi-Zheng Fang
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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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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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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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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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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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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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