Synthesis and Evaluation of a Novel Deguelin Derivative, L80, which Disrupts ATP Binding to the C-terminal Domain of Heat Shock Protein 90
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Synthesis and Evaluation of a Novel Deguelin Derivative, L80, which Disrupts ATP Binding to the C-terminal Domain of Heat Shock Protein 90.
The clinical benefit of current anticancer regimens for lung cancer therapy is still limited due to moderate efficacy, drug resistance, and recurrence. Therefore, the development of effective anticancer drugs for first-line therapy and for optimal second-line treatment is necessary. Because the 90-kDa molecular chaperone heat shock protein (Hsp90) contributes to the maturation of numerous mutat...
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Coumarine (2H-1-benzopyran-2-ones) is benzopyrone class compounds and its derivatives are shown a wide spectrum of biological activity. Particularly, coumarine derivative compounds (novobiocin, coumermycin A1, KU135, and chlorobiocin) have an affinity for binding to the CTD and disrupting Hsp90 dimerization. Consequently, these compounds inhibit proper folding of oncogenic client proteins and c...
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The 90-kDa heat shock protein (hsp-90) is an abundant cytosolic protein believed to play a role in maintenance of protein trafficking and closely associated with several steroid hormone receptors. Incubation of highly purified hsp-90 with [gamma-32P]ATP results in its autophosphorylation on serine residues. There are several lines of evidence which suggest that this activity is due to a kinase ...
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ژورنال
عنوان ژورنال: Molecular Pharmacology
سال: 2015
ISSN: 0026-895X,1521-0111
DOI: 10.1124/mol.114.096883