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All Rights Reserved. http://resource.belframework.org/belframework/20131211/knowledge/small_corpus.bel http://purl.org/dc/elements/1.1/title BEL Framework Small Corpus Document http://resource.belframework.org/belframework/20131211/knowledge/small_corpus.bel http://purl.org/dc/terms/license Creative Commons Attribution-Non-Commercial-ShareAlike 3.0 Unported License http://resource.belframework.org/belframework/20131211/knowledge/small_corpus.bel http://purl.org/pav/authoredBy http://www.tkuhn.ch/bel2nanopub/RANa5hTz-iPSqzFqnYm-PSPDVZijTw21FusITtZxO6TkY#_6 http://resource.belframework.org/belframework/20131211/knowledge/small_corpus.bel http://purl.org/pav/version 20131211 http://www.tkuhn.ch/bel2nanopub/RANa5hTz-iPSqzFqnYm-PSPDVZijTw21FusITtZxO6TkY#_5 http://www.w3.org/ns/prov#value VEGF induced tyrosine phosphorylation of the regulatory p85 subunit of PI 3-kinase, evidenced by immunoblotting of anti-p85 immunoprecipitates with an anti-pY mAb (Fig. 5b). Moreover, immunoblotting of anti-pY immunoprecipitates with specific p85 mAb showed an increased association of p85 with tyrosine-phosphorylated proteins, which was maximal after 5 min of VEGF treatment (Fig. 5c). To determine whether VEGF-induced p85 phosphorylation regulates p110, the catalytic counterpart of PI 3-kinase, we performed in vitrokinase assays using PI 4,5-bisphosphate as a substrate. 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