Functional characterization of heat shock protein 90 targeted compounds
| Autor: | Yixi Zhang, Andreas G. Schätzlein, Min Yang, Maria de la Fuente, Isa N. Cruz |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
Adenosine Triphosphatases
ATPase Biophysics food and beverages Antineoplastic Agents Cell Biology Plasma protein binding Biology Biochemistry Hsp90 Inhibitory Concentration 50 In vivo Heat shock protein biology.protein medicine Chaperone complex Bioassay Biological Assay HSP90 Heat-Shock Proteins Molecular Biology Novobiocin Protein Binding medicine.drug |
| Zdroj: | Analytical Biochemistry. 438:107-109 |
| ISSN: | 0003-2697 |
| DOI: | 10.1016/j.ab.2013.03.026 |
| Popis: | Heat shock protein 90 (Hsp90) is an attractive cancer target that possesses two potential binding domains at the C and N termini. Nevertheless, assays that can reliably distinguish between the C- and N-terminal Hsp90 inhibitors and quantitatively characterize candidate drugs are limited. Here we report an Hsp90 binding assay and ATPase inhibition assay that can not only separate the C- and N-terminal inhibitors but also quantitatively determine their respective IC50 values. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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