Modulation of chaperone function and cochaperone interaction by novobiocin in the C-terminal domain of Hsp90: evidence that coumarin antibiotics disrupt Hsp90 dimerization. [electronic resource]
Producer: 20060510Description: 7161-71 p. digitalISSN:- 0021-9258
- Alanine -- chemistry
- Amino Acid Sequence
- Aminocoumarins -- chemistry
- Anti-Bacterial Agents -- chemistry
- Binding Sites
- Coumarins -- chemistry
- DNA, Complementary -- metabolism
- Dimerization
- Dose-Response Relationship, Drug
- Enzyme Inhibitors -- chemistry
- Enzyme-Linked Immunosorbent Assay
- Glutathione Transferase -- metabolism
- HSP90 Heat-Shock Proteins -- chemistry
- HeLa Cells
- Humans
- Immunophilins -- chemistry
- Molecular Chaperones -- chemistry
- Molecular Conformation
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Novobiocin -- chemistry
- Plasmids -- metabolism
- Point Mutation
- Protein Binding
- Protein Conformation
- Protein Structure, Tertiary
- Steroids -- chemistry
- Substrate Specificity
- Tacrolimus Binding Proteins -- chemistry
- Time Factors
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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