Matches in Nanopublications for { <http://www.tkuhn.ch/bel2nanopub/RAO-I_9HYtFa99rW9FtCdIZr6P9C7FkDKOfppqHRi28ZY#_4> ?p ?o ?g. }
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- _4 value "Tyrosine phosphorylation of Tyr(688) or mutation of tyrosine 688 to aspartic acid is sufficient to allow binding to the NH(2)-terminal SH2 domain of p85. Thus an intramolecular interaction between phosphorylated Tyr(688) and the NH(2)-terminal SH2 domain of p85 can relieve the inhibitory activity of p85 on p110." provenance.
- _4 wasQuotedFrom 11337495 provenance.