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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