About: Selective Inhibition of USP7

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An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Selective Inhibition of USP7
Creator	Menard, Robert Sulea, Traian Li, Y Aharoni, A Bigley, A Cadieux, C Cerasoli, D Cheng, T.-C Gaidukov, L Ghanem, E Gä, A Harel, M Harvey, S Heidenreich, -H Kasten, S Kehe, M Kolakowski, J Koller, J Mccarthy, R Meged, O Melzer, M Raushel, J Ravelli, R Reeves, T Reiff, V Tsai, P.-C
Source	Elsevier; Medline; PMC
abstract	The deubiquitinating enzyme USP7 is an emerging oncology and antiviral target. Reverdy et al., in this issue of Chemistry & Biology, disclose the first small-molecule inhibitor selective for USP7, which recapitulates its knockdown in cancer cells and hence demonstrates the therapeutic feasibility of USP7 inhibitors.
has issue date	2012-04-20(xsd:dateTime)
bibo:doi	10.1016/j.chembiol.2012.04.001
bibo:pmid	22520747
has license	no-cc
sha1sum (hex)	2f3d0102dfa48e7e6a118a2464c77fb44ac159fa
schema:url	https://doi.org/10.1016/j.chembiol.2012.04.001
resource representing a document's title	Selective Inhibition of USP7
has PubMed Central identifier	PMC7111172
has PubMed identifier	22520747
schema:publication	Chem Biol
resource representing a document's body	covid:2f3d0102dfa48e7e6a118a2464c77fb44ac159fa#body_text
is schema:about of	named entity 'USP7' named entity 'INHIBITION' named entity 'SELECTIVE' named entity 'USP7' named entity 'off-target activity' named entity 'UV-induced' named entity 'cancer cells' named entity 'active site' named entity 'oncology' named entity 'USP7' named entity 'deubiquitinating' named entity 'substituent' named entity 'site-directed' named entity 'mass spectrometry' named entity 'PLpro' named entity 'USP7' named entity 'posttranslational' named entity 'USP7' named entity 'positively charged' named entity 'USPs' named entity 'small-molecule' named entity 'Molecular docking' named entity 'substrate' named entity 'phosphorylation' named entity 'USP' named entity 'potency' named entity 'Protein' named entity 'USPs' named entity 'HTS' named entity 'USP7' named entity 'endogenous' named entity 'covalent' named entity 'negatively charged' named entity 'cysteine protease' named entity 'USP7' named entity 'homologous' named entity 'USPs' named entity 'USPs' named entity 'cysteine proteases' named entity 'USP7' named entity 'Cys' named entity 'USPs' named entity 'substrates' named entity 'catalytic triad' named entity 'USP' named entity 'living cells' named entity 'Mdm2' named entity 'Claspin' named entity 'USP7' named entity 'Small-molecule' named entity 'Mdm2' named entity 'proteases' named entity 'thiolate' named entity 'potency' named entity 'USP' named entity 'solvent'

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