Synthesis of novel fluorescent probes for the molecular chaperone Hsp90 Journal Article

  


Authors: Llauger Bufi, L.; Felts, S. J.; Huezo, H.; Rosen, N.; Chiosis, G.
Article Title: Synthesis of novel fluorescent probes for the molecular chaperone Hsp90
Abstract: Heat shock protein 90 (Hsp90) is a molecular chaperone necessary for maintaining oncogenic transformation. There is substantial interest in developing novel agents that bind to the N-terminal of the chaperone. Here we report the synthesis and characterization of two fluorescent Hsp90 inhibitors and probe their use in an Hsp90 fluorescent polarization assay. © 2003 Elsevier Ltd. All rights reserved.
Keywords: protein protein interaction; fluorescent dyes; structure-activity relationship; kinetics; heat shock protein 90; hsp90 heat-shock proteins; molecular structure; ligand binding; synthesis; chemical modification; geldanamycin; chaperone; binding, competitive; michael addition; article; fluorescein derivative
Journal Title: Bioorganic & Medicinal Chemistry Letters
Volume: 13
Issue: 22
ISSN: 0960-894X
Publisher: Pergamon-Elsevier Science Ltd  
Date Published: 2003-11-17
Start Page: 3975
End Page: 3978
Language: English
DOI: 10.1016/j.bmcl.2003.08.065
PUBMED: 14592488
PROVIDER: scopus
DOI/URL:

http://www.scopus.com/inward/record.url?eid=2-s2.0-0242285605&partnerID=40&md5=28ed3b1ff67f24b10b546ab48528eb7f
Notes: Export Date: 12 September 2014 -- Source: Scopus
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MSK Authors
  1. Laura Llauger Bufi
    8 Llauger Bufi
  2. Neal Rosen
    425 Rosen
  3. Gabriela Chiosis
    279 Chiosis
  4. Henri Huezo
    11 Huezo
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