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http://www.w3.org/1999/02/22-rdf-syntax-ns#type
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http://www.tkuhn.ch/bel2nanopub/RAeEunMiQJA3o1cOYOgm5fwDnD37uTrhRaUgA67kTXXvc#_1
http://semanticscience.org/resource/SIO_000139
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http://www.tkuhn.ch/bel2nanopub/RAeEunMiQJA3o1cOYOgm5fwDnD37uTrhRaUgA67kTXXvc#_1
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://amigo.geneontology.org/amigo/term/GO:0016791
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http://purl.obolibrary.org/obo/RO_0002204
http://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=13417
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http://purl.obolibrary.org/obo/BFO_0000066
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http://www.selventa.com/vocabulary/decreases
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http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
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http://www.w3.org/2000/01/rdf-schema#label
a(CHEBI:"okadaic acid") -| phos(p(HGNC:PPP2R3B))
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Approximately 61,000 statements.
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Copyright (c) 2011-2012, Selventa. All rights reserved.
http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel
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BEL Framework Large Corpus Document
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1.4
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http://www.w3.org/ns/prov#value
To determine whether PP2A can directly dephosphorylate the autophosphorylation sites on the Pim kinases, Pim-3 immunoprecipitates were subjected to in vitro kinase assays followed by in vitro phosphatase assays. When wild-type Pim-3 immunoprecipitates were subjected to in vitro kinase-in vitro phosphatase reactions, recombinant PP2A was able to dephosphorylate the autophosphorylation sites on Pim-3 (Fig. 2, lanes 4 and 5). This effect of PP2A was blocked by addition of okadaic acid, an inhibitor of PP2A catalytic activity, to the phosphatase reactions (Fig. 2, lanes 7 and 8).
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http://www.w3.org/ns/prov#wasQuotedFrom
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http://www.w3.org/2000/01/rdf-schema#label
Selventa
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http://www.w3.org/ns/prov#hadPrimarySource
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2014-07-03T14:30:07.830+02:00
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http://orcid.org/0000-0001-6818-334X
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