Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde.

By Min Hu, Pingwei Li, Muyang Li, Wenyu Li, T. Yao, Jia-Wei Wu, W. Gu, R. Cohen, Yigong Shi. Cell, 2002

636 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/fc289b40918a7e00742170e36cc1686b68073249

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Citations in the corpus

• Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGA-associated Ubp8. (2003, background): “A putative catalytic substitution was generated within Ubp8 (C146S), based on its conserved sequence with previously characterized ubiquitin proteases (Hu et al. 2002).”
• CYLD is a deubiquitinating enzyme that negatively regulates NF-κB activation by TNFR family members (2003, background): “CYLD might be activated by binding to the ubiquitin moiety of target proteins, as this has been reported for another deubiquitinas”
• Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein (2017, background): “His–Asp is pre-formed, different from USP7, where the catalytic residues are only well aligned upon Ub binding to the enzyme (Hu et al., 2002).”
• In silico pharmacology for drug discovery: applications to targets and beyond (2007, background): “fically de-ubiquitinates the ubiquitinated p53 protein, may also assist in drug development despite the peptidic nature of its substrate (Hu et al., 2002).”
• p53 ubiquitination: Mdm2 and beyond. (2006, background): “The finding that the herpesvirus-associated ubiquitin-specific protease (HAUSP) could bind to and stabilize p53 added yet another layer of regulation to the p53 ubiquitination pathway and was one of the first indications that DUBs exhibited substrate specificity (Hu et al., 2002; Li et al., 2002a).”
• Ubiquitin-binding domains (2005, background): “In another example, although ubiquitin-binding regions in the catalytic domains of ubiquitin-pathway enzymes are not generally counted as UBDs, a DUB has been shown to bind simultaneously to conjugated ubiquitin and to a region of the ubiquitylated protein through interactions that are individually ”
• The SARS-Coronavirus papain-like protease: Structure, function and inhibition by designed antiviral compounds (2014, positive): “In order for the catalytic triad of USP7 to adopt the proper orientation for catalysis, a substrate-induced alignment must occur upon association with ubiquitin or other regulatory domains (Hu et al., 2002; Molland et al., 2014; Ratia et al., 2006).”
• Ubiquitin: structures, functions, mechanisms. (2004, background): “Ubiquitin binding to Hausp, for example, alters the positions of a histidine (general base) and an asparagine (oxyanion hole) so that these side chains become catalytically competent [62].”
• Regulation and Cellular Roles of Ubiquitin-specific Deubiquitinating Enzymes (2009, background): “Structures of USP domains bound to ubiquitin or a ubiquitin-based inhibitor show that the C terminus of ubiquitin sits in a cleft located between the thumb and the palm subdomains, and the globular portion of ubiquitin interacts with the finger (62, 63, 65).”
• Molecular Basis of NF-κB Signaling (2013, background): “The putative binding site is located at a position similar to ubiquitin-binding sites of two other DUBs, Yuh1 and HAUSP (36, 47).”