Results 21 to 30 of about 10,823 (192)
A Novel Type of Deubiquitinating Enzyme [PDF]
Journal of Biological Chemistry, 2003 A previous report from this laboratory described two novel proteins that have sequence similarity to A20, a negative regulator of NF-kappaB (Evans, P. C., Taylor, E. R., Coadwell, J., Heyninck, K., Beyaert, R., and Kilshaw, P. J. (2001) Biochem. J. 357, 617-623).
Paul C, Evans +9 more
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Deubiquitinating enzymes regulate PARK2-mediated mitophagy [PDF]
Autophagy, 2015 The selective degradation of mitochondria by the process of autophagy, termed mitophagy, is one of the major mechanisms of mitochondrial quality control. The best-studied mitophagy pathway is the one mediated by PINK1 and PARK2/Parkin. From recent studies it has become clear that ubiquitin-ligation plays a pivotal role and most of the focus has been on
Wang Yuqing +7 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.
Benjamin, Nicholson +3 more
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VHL protein‐interacting deubiquitinating enzyme 2 deubiquitinates and stabilizes HIF‐1α [PDF]
EMBO reports, 2005 Hypoxia‐inducible factor (HIF)‐1α is a short‐lived protein and is ubiquitinated and degraded through the von Hippel–Lindau protein (pVHL)–E3 ubiquitin ligase pathway at normoxia. Deubiquitination, by reversing ubiquitination, has been recognized as an important regulatory step in ubiquitination‐related processes.
Zaibo, Li +3 more
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Systematic analysis of the physiological importance of deubiquitinating enzymes. [PDF]
PLoS ONE, 2012 Deubiquitinating enzymes (DUBs) are proteases that control the post-translational modification of proteins by ubiquitin and in turn regulate diverse cellular pathways.
Wei-Ling Tsou +6 more
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Mechanisms for regulating deubiquitinating enzymes [PDF]
Protein Science, 2014 AbstractUbiquitination is a reversible post‐translational modification that plays a dynamic role in regulating most eukaryotic processes. Deubiquitinating enzymes (DUBs), which hydrolyze the isopeptide or peptide linkages joining ubiquitin to substrate lysines or N‐termini, therefore play a key role in ubiquitin signaling.
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Deubiquitinating enzymes (DUBs): DoUBle-edged swords in CNS autoimmunity
Journal of Neuroinflammation, 2020 Multiple sclerosis (MS) is the most common autoimmune disease of the CNS. The etiology of MS is still unclear but it is widely recognized that both genetic and environmental factors contribute to its pathogenesis.
Jing Ruan, Dirk Schlüter, Xu Wang
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Writing and erasing MYC ubiquitination and SUMOylation
Genes and Diseases, 2019 The transcription factor c-MYC (MYC thereafter) controls diverse transcription programs and plays a key role in the development of many human cancers. Cells develop multiple mechanisms to ensure that MYC levels and activity are precisely controlled in ...
Yingxiao Chen +3 more
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Protease addiction and synthetic lethality in cancer
Frontiers in Oncology, 2011 The oncogene addiction concept refers to the dependence of cancer cells on the function of the oncogenes responsible for their transformed phenotype, while the term non-oncogene addiction has been introduced to define the exacerbated necessity of the ...
Jose M.P. Freije +2 more
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Nature Communications, 2021 Ubiquitination has an important function in the regulation of antiviral immunity involving the signalling molecule MAVS. Here the authors investigate deubiquitinating enzymes and show USP18 regulates MAVS mediated antiviral signalling through modulating ...
Jinxiu Hou +9 more
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