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http://purl.uniprot.org/citations/25313996http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25313996http://www.w3.org/2000/01/rdf-schema#comment"An affinity-based mass spectrometry screening technology was used to identify novel binders to both nonphosphorylated and phosphorylated ERK2. Screening of inactive ERK2 identified a pyrrolidine analogue 1 that bound to both nonphosphorylated and phosphorylated ERK2 and inhibited ERK2 kinase activity. Chemical optimization identified compound 4 as a novel, potent, and highly selective ERK1,2 inhibitor which not only demonstrated inhibition of phosphorylation of ERK substrate p90RSK but also demonstrated inhibition of ERK1,2 phosphorylation on the activation loop. X-ray cocrystallography revealed that upon binding of compound 4 to ERK2, Tyr34 undergoes a rotation (flip) along with a shift in the poly-Gly rich loop to create a new binding pocket into which 4 can bind. This new binding mode represents a novel mechanism by which high affinity ATP-competitive compounds may achieve excellent kinase selectivity."xsd:string
http://purl.uniprot.org/citations/25313996http://purl.org/dc/terms/identifier"doi:10.1021/jm500847m"xsd:string
http://purl.uniprot.org/citations/25313996http://purl.uniprot.org/core/author"Deng Y."xsd:string
http://purl.uniprot.org/citations/25313996http://purl.uniprot.org/core/author"Jin W."xsd:string
http://purl.uniprot.org/citations/25313996http://purl.uniprot.org/core/author"Nan Y."xsd:string
http://purl.uniprot.org/citations/25313996http://purl.uniprot.org/core/author"Xiao L."xsd:string
http://purl.uniprot.org/citations/25313996http://purl.uniprot.org/core/author"Wang T."xsd:string
http://purl.uniprot.org/citations/25313996http://purl.uniprot.org/core/author"Zhu H.Y."xsd:string
http://purl.uniprot.org/citations/25313996http://purl.uniprot.org/core/author"Carr D."xsd:string
http://purl.uniprot.org/citations/25313996http://purl.uniprot.org/core/author"Cooper A."xsd:string
http://purl.uniprot.org/citations/25313996http://purl.uniprot.org/core/author"Dayananth P."xsd:string
http://purl.uniprot.org/citations/25313996http://purl.uniprot.org/core/author"Windsor W.T."xsd:string
http://purl.uniprot.org/citations/25313996http://purl.uniprot.org/core/author"Kirschmeier P."xsd:string
http://purl.uniprot.org/citations/25313996http://purl.uniprot.org/core/author"Chuang C.C."xsd:string
http://purl.uniprot.org/citations/25313996http://purl.uniprot.org/core/author"English J.M."xsd:string
http://purl.uniprot.org/citations/25313996http://purl.uniprot.org/core/author"Samatar A.A."xsd:string
http://purl.uniprot.org/citations/25313996http://purl.uniprot.org/core/author"Annis D.A."xsd:string
http://purl.uniprot.org/citations/25313996http://purl.uniprot.org/core/author"Shipps G.W. Jr."xsd:string
http://purl.uniprot.org/citations/25313996http://purl.uniprot.org/core/author"Hruza A.W."xsd:string
http://purl.uniprot.org/citations/25313996http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/25313996http://purl.uniprot.org/core/name"J Med Chem"xsd:string
http://purl.uniprot.org/citations/25313996http://purl.uniprot.org/core/pages"8817-8826"xsd:string
http://purl.uniprot.org/citations/25313996http://purl.uniprot.org/core/title"Discovery of novel, dual mechanism ERK inhibitors by affinity selection screening of an inactive kinase."xsd:string
http://purl.uniprot.org/citations/25313996http://purl.uniprot.org/core/volume"57"xsd:string