Screening a hydroxystilbene library for selective inhibition of the B cell antigen receptor kinase cascade

Anthony C. Bishop, Dana Moore, Thomas S. Scanlan, Kevan M. Shokat

Research output: Contribution to journalArticle

8 Scopus citations


Protein tyrosine phosphorylation is a key post-translational modification used by eukaryotic cells in receptor mediated signal transduction. Selective inhibition of cellular phosphorylation would aid efforts to elucidate the individual events in a signaling pathway. A combinatorial library of putative kinase inhibitors has been screened using an antiphosphotyrosine blotting assay that can detect inhibition of individual phosphorylation events in whole cells. One member of the library, 3-hydroxy-4-methoxy-4'-nitro-trans-stilbene (2B), has been found to selectively disrupt the phosphorylation of several proteins in the B cell receptor mediated cascade while not affecting other cellular phosphorylation events. The kinase specificity of stilbene 2B is compared to known natural and synthetic kinase inhibitors.

Original languageEnglish (US)
Pages (from-to)11995-12004
Number of pages10
Issue number35
StatePublished - Sep 1 1997


ASJC Scopus subject areas

  • Biochemistry
  • Drug Discovery
  • Organic Chemistry

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