Macrocyclic Inhibitors of Hsp90
نویسندگان
چکیده
منابع مشابه
Maximizing the Therapeutic Potential of HSP90 Inhibitors.
HSP90 is required for maintaining the stability and activity of a diverse group of client proteins, including protein kinases, transcription factors, and steroid hormone receptors involved in cell signaling, proliferation, survival, oncogenesis, and cancer progression. Inhibition of HSP90 alters the HSP90-client protein complex, leading to reduced activity, misfolding, ubiquitination, and, ulti...
متن کاملDevelopment and application of Hsp90 inhibitors.
Heat shock protein 90 has emerged as an important target in several diseases. The present review will discuss our understanding of the role played by Hsp90 in regulating and maintaining the transformed phenotype in cancers and neurodegenerative diseases, as well as recent findings on its roles in fungal and viral infections. It will also update the reader on the preclinical development and clin...
متن کاملGeldanamycin and its derivatives as Hsp90 inhibitors.
The Hsp90 molecule, one of the most abundant heat shock proteins in mammalian cells, maintains homeostasis and prevents stress-induced cellular damage. Hsp90 is expressed under normal conditions at a level of about 1-2 Percent of total proteins, while its expression increases 2-10 fold in cancer cells. The two main constitutively expressed isoforms of Hsp90 are known as Hsp90-alpha and Hsp90-be...
متن کاملCircumventing HSP90 inhibitors via apoptosis block
Heat shock protein 90 (HSP90) is a phylogenetically conserved molecular chaperone that plays a crucial role in regulating cancer cell signalling client networks, and has been described as an evolutionary capacitor that buffers genome variation under normal conditions [1]. Consequently HSP90 inhibition is pleiotropic in its targeting, effectively inhibiting critical cancer networks. Personalizin...
متن کاملMps1 Mediated Phosphorylation of Hsp90 Confers Renal Cell Carcinoma Sensitivity and Selectivity to Hsp90 Inhibitors
The molecular chaperone Hsp90 protects deregulated signaling proteins that are vital for tumor growth and survival. Tumors generally display sensitivity and selectivity toward Hsp90 inhibitors; however, the molecular mechanism underlying this phenotype remains undefined. We report that the mitotic checkpoint kinase Mps1 phosphorylates a conserved threonine residue in the amino-domain of Hsp90. ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Current Topics in Medicinal Chemistry
سال: 2010
ISSN: 1568-0266
DOI: 10.2174/156802610792232088