Client Proteins and Small Molecule Inhibitors Display Distinct Binding Preferences for Constitutive...
Client Proteins and Small Molecule Inhibitors Display Distinct Binding Preferences for Constitutive and Stress-Induced HSP90 Isoforms and Their Conformationally Restricted Mutants
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Publisher
United States: Public Library of Science
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Language
English
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Publisher
United States: Public Library of Science
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Scope and Contents
Contents
The two cytosolic/nuclear isoforms of the molecular chaperone HSP90, stress-inducible HSP90α and constitutively expressed HSP90β, fold, assemble and maintain the three-dimensional structure of numerous client proteins. Because many HSP90 clients are important in cancer, several HSP90 inhibitors have been evaluated in the clinic. However, little is...
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Full title
Client Proteins and Small Molecule Inhibitors Display Distinct Binding Preferences for Constitutive and Stress-Induced HSP90 Isoforms and Their Conformationally Restricted Mutants
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TN_cdi_plos_journals_1728400167
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1728400167
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ISSN
1932-6203
E-ISSN
1932-6203
DOI
10.1371/journal.pone.0141786
