A new screening assay for allosteric inhibitors of cSrc View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2009-04-26

AUTHORS

Jeffrey R Simard, Sabine Klüter, Christian Grütter, Matthäus Getlik, Matthias Rabiller, Haridas B Rode, Daniel Rauh

ABSTRACT

Targeting kinases outside the highly conserved ATP pocket is thought to be a promising strategy for overcoming bottlenecks in kinase inhibitor research, such as limited selectivity and drug resistance. Here we report the development and application of a direct binding assay to detect small molecules that stabilize the inactive conformation of the tyrosine kinase cSrc. Protein X-ray crystallography validated the assay results and confirmed an exclusively allosteric binding mode. More... »

PAGES

394-396

References to SciGraph publications

  • 2006-01-15. Allosteric inhibitors of Bcr-abl–dependent cell proliferation in NATURE CHEMICAL BIOLOGY
  • 2002-03-18. Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 2004-12. Strategies to overcome resistance to targeted protein kinase inhibitors in NATURE REVIEWS DRUG DISCOVERY
  • 2006-08-04. Drug–target residence time and its implications for lead optimization in NATURE REVIEWS DRUG DISCOVERY
  • 2009-01. Targeting cancer with small molecule kinase inhibitors in NATURE REVIEWS CANCER
  • 2004-05-01. The discovery of receptor tyrosine kinases: targets for cancer therapy in NATURE REVIEWS CANCER
  • 2004-06-01. A renaissance for SRC in NATURE REVIEWS CANCER
  • 2006-06-16. Rational design of inhibitors that bind to inactive kinase conformations in NATURE CHEMICAL BIOLOGY
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nchembio.162

    DOI

    http://dx.doi.org/10.1038/nchembio.162

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1027085190

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/19396179


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