Design of a fluorescence polarization assay platform for the study of human Hsp70 Journal Article


Authors: Kang, Y.; Taldone, T.; Clement, C. C.; Fewell, S. W.; Aguirre, J.; Brodsky, J. L.; Chiosis, G.
Article Title: Design of a fluorescence polarization assay platform for the study of human Hsp70
Abstract: The 70 kDa heat shock proteins (Hsp70) are molecular chaperones that assist in folding of newly synthesized polypeptides, refolding or denaturation of misfolded proteins, and translocation of proteins across biological membranes. In addition, Hsp70 play regulatory roles in signal transduction, cell cycle, and apoptosis. Here, we present a novel assay platform based on fluorescence polarization that is suitable for investigating the yet elusive molecular mechanics of human Hsp70 allosteric regulation. © 2008 Elsevier Ltd. All rights reserved.
Keywords: signal transduction; cell cycle; apoptosis; fluorescent dyes; spectrometry, fluorescence; protein binding; dose-response relationship, drug; fluorescence polarization; kinetics; cell membrane; peptides; computer simulation; heat shock protein 70; high performance liquid chromatography; protein folding; molecular conformation; fluorescein isothiocyanate; hsp70; hsp70 heat-shock proteins; molecular chaperones; protein denaturation; allosteric site
Journal Title: Bioorganic & Medicinal Chemistry Letters
Volume: 18
Issue: 13
ISSN: 0960-894X
Publisher: Pergamon-Elsevier Science Ltd  
Date Published: 2008-07-01
Start Page: 3749
End Page: 3751
Language: English
DOI: 10.1016/j.bmcl.2008.05.046
PUBMED: 18515098
PROVIDER: scopus
PMCID: PMC2538440
DOI/URL:
Notes: --- - "Cited By (since 1996): 7" - "Export Date: 17 November 2011" - "CODEN: BMCLE" - "Source: Scopus"
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  1. Cristina C Clement
    12 Clement
  2. Gabriela Chiosis
    279 Chiosis
  3. Yanlong Kang
    22 Kang
  4. Julia Aguirre
    15 Aguirre