Targeting cancer with small molecule kinase inhibitors View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2009-01

AUTHORS

Jianming Zhang, Priscilla L. Yang, Nathanael S. Gray

ABSTRACT

Key PointsSmall-molecule kinase inhibitors are being intensively pursued as new anticancer therapeutics. To date, approximately 80 inhibitors have been advanced to some stage of clinical evaluation.Understanding the structural basis of kinase inhibitor selectivity is crucial to the ultimate goal of developing selective inhibitors to target every member of the kinome. Most currently known kinase inhibitors target the ATP binding site with the kinase activation loop in the active (type 1) or inactive (type 2) conformation.New kinase inhibitors are primarily developed with a combination of methods, including high-throughput screening using biochemical or cellular assays, analogue synthesis, structure-guided design and fragment-based assembly strategies.The repertoire of kinases targeted by a given inhibitor can be determined by profiling its activity in binding and enzymatic assays against extensive panels of recombinant kinases, by profiling activity in cellular assays and by affinity approaches integrated with detection by mass spectrometry.Kinase inhibitor resistance resulting from selection for mutant alleles or upregulation of alternative signalling pathways is a recurrent theme in the clinic. Strategies for developing multiple inhibitors targeting different kinase sites and for discovering synergistic inhibitor combinations are urgently needed. More... »

PAGES

28-39

References to SciGraph publications

  • 2008-06-25. Essential roles of PI(3)K–p110β in cell growth, metabolism and tumorigenesis in NATURE
  • 2002-04. Protein kinases — the major drug targets of the twenty-first century? in NATURE REVIEWS DRUG DISCOVERY
  • 2006-01-15. Allosteric inhibitors of Bcr-abl–dependent cell proliferation in NATURE CHEMICAL BIOLOGY
  • 2006-08. Mechanisms of Disease: oncogene addiction—a rationale for molecular targeting in cancer therapy in NATURE REVIEWS CLINICAL ONCOLOGY
  • 2008-01-08. A quantitative analysis of kinase inhibitor selectivity in NATURE BIOTECHNOLOGY
  • 2006-01-17. COSMIC 2005 in BRITISH JOURNAL OF CANCER
  • 2008-08-24. Identification of ALK as a major familial neuroblastoma predisposition gene in NATURE
  • 2004-11-14. Structures of human MAP kinase kinase 1 (MEK1) and MEK2 describe novel noncompetitive kinase inhibition in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 2007-01-28. A clickable inhibitor reveals context-dependent autoactivation of p90 RSK in NATURE CHEMICAL BIOLOGY
  • 2005-08-19. The Concept of Synthetic Lethality in the Context of Anticancer Therapy in NATURE REVIEWS CANCER
  • 2004-02-22. VX-680, a potent and selective small-molecule inhibitor of the Aurora kinases, suppresses tumor growth in vivo in NATURE MEDICINE
  • 2004-03. A census of human cancer genes in NATURE REVIEWS CANCER
  • 2008-03. The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth in NATURE
  • 2007-03. Patterns of somatic mutation in human cancer genomes in NATURE
  • 2007-08-26. Quantitative chemical proteomics reveals mechanisms of action of clinical ABL kinase inhibitors in NATURE BIOTECHNOLOGY
  • 2002-06-09. Mutations of the BRAF gene in human cancer in NATURE
  • 2006-06-16. Rational design of inhibitors that bind to inactive kinase conformations in NATURE CHEMICAL BIOLOGY
  • 2005-02-13. A small molecule–kinase interaction map for clinical kinase inhibitors in NATURE BIOTECHNOLOGY
  • 2006-08-01. Current development of mTOR inhibitors as anticancer agents in NATURE REVIEWS DRUG DISCOVERY
  • Journal

    TITLE

    Nature Reviews Cancer

    ISSUE

    1

    VOLUME

    9

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nrc2559

    DOI

    http://dx.doi.org/10.1038/nrc2559

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1001079875

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/19104514


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