A genomic and functional inventory of deubiquitinating enzymes.

By Sebastian M. B. Nijman, M. Luna-Vargas, A. Velds, T. Brummelkamp, A. Dirac, T. Sixma, René Bernards. Cell, 2005

1,876 citations recorded by the source corpus.

Subfields: Epidemiology, Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/08a434bc179a780e5e4ed19d84c48f0c009cb148

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In Epidemiology

1. Stephen P. Jackson
2. Ivan Dikic
3. D. Komander

In Molecular Biology

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2. W. Gu
3. C. Brooks
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In Oncology

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7. K. Wilkinson
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Citations in the corpus

• Histone ubiquitination: triggering gene activity. (2008, background): “Consistent with a role in signaling, monoubiquitination is reversible; ubiquitin can be removed from target substrates by a class of thiol proteases known as ubiquitin-specific proteases (UBPs in yeast; USPs in mammals) (reviewed in Nijman et al., 2005).”
• The role of ubiquitination in tumorigenesis and targeted drug discovery (2020, background): “Targeting DUB activity As mentioned, ubiquitination is a dynamic and reversible process, and DUBs mediate the removal and processing of Ub or polyubiquitin chains from ubiquitinated proteins.(427) Many DUBs have been found to participate in various events during the cell cycle progression, genomic i”
• Regulation and Cellular Roles of Ubiquitin-specific Deubiquitinating Enzymes (2009, background): “Thus, a more transient and acute knockdown is needed, and the technique of RNAi has proven productive in revealing the role of DUBs in these processes (12, 59, 177, 178).”
• Targeting the ubiquitin system in cancer therapy (2009, background): “Most human DUBs are cysteine proteases and can be divided into five subfamilies: ubiquitin-specific proteases (Usp), ubiquitin carboxy-terminal hydrolases (UCH), ovarian tumour-like proteases (OTU), JAMM/MPN metalloproteases, and Machado–Jakob-disease proteases (MJD”
• Breaking the chains: structure and function of the deubiquitinases (2009, background): “The human genome encodes approximately 79 deubiquitinases (DUBs; also known as deubiquitylating or deubiquitinating enzymes) that are predicted to be active and which oppose the function of E3 ligase”
• Riding the DUBway: regulation of protein trafficking by deubiquitylating enzymes (2006, neutral): “"”
• p53 ubiquitination: Mdm2 and beyond. (2006, background): “How is HAUSP regulated? Are there unidentified deubiquitinases involved in this pathway? A growing number of substrate-specific mammalian DUBs involved in tumorigenesis are continually being revealed such as USP1 and USP9X, which deubiquitinate FANCD2 and b-catenin, respectively (Nijman et al., 2005”
• Deubiquitylating enzymes and drug discovery: emerging opportunities (2017, background): “Also, DUBs need to accommodate substantial globular post-translational modifications (ubiquitin, UBL, or ubiquitin-UBL chains) into their catalytic site 215 .”