Heat shock protein 90: its inhibition and function
نویسندگان
چکیده
منابع مشابه
Antimyeloma activity of heat shock protein-90 inhibition.
We show that multiple myeloma (MM), the second most commonly diagnosed hematologic malignancy, is responsive to hsp90 inhibitors in vitro and in a clinically relevant orthotopic in vivo model, even though this disease does not depend on HER2/neu, bcr/abl, androgen or estrogen receptors, or other hsp90 chaperoning clients which are hallmarks of tumor types traditionally viewed as attractive clin...
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The phosphatidylinositol 3'-kinase/Akt pathway is activated frequently in human cancer, and has been implicated in tumor proliferation, cell survival, and resistance to apoptotic stimuli. Akt forms a complex with heat shock protein (Hsp) 90 and Cdc37, and inhibitors of Hsp90 cause Akt degradation. 17-allylamino-17-demethoxygeldanamycin (17-AGG) is an Hsp90 inhibitor currently in Phase I clinica...
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Alzheimer's disease (AD) is the first most common neurodegenerative disease. Despite a large amount of research, the pathogenetic mechanism of AD has not yet been clarified. The two hallmarks of the pathology of AD are the extracellular senile plaques (SPs) of aggregated amyloid-beta (Aβ) peptide and the accumulation of the intracellular microtubule-associated protein tau into fibrillar aggrega...
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Volume 3 • Issue 2 • 1000e109 Adv Tech Biol Med ISSN: 2379-1764 ATBM, an open access journal Hsp70 (70 kDa) and Hsp90 (90 kDa) are important members of the chaperone protein family. They are over-expressed in a wide range of tumor types (both solid tumors and hematological malignancies), and play essential roles in apoptosis, cell proliferation, metastases, angiogenesis, and invasion pathways i...
متن کاملInhibition of heat shock protein 90 function by ansamycins causes the morphological and functional differentiation of breast cancer cells.
17-(Allylamino)-17-demethoxygeldanamycin (17-AAG) is an ansamycin antibiotic that binds to a conserved pocket in Hsp90 and induces the degradation of proteins that require this chaperone for conformational maturation. 17-AAG causes a retinoblastoma (RB)-dependent G1 block in cancer cells and is now in clinical trial. In breast cancer cells, G1 block is accompanied by differentiation and followe...
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ژورنال
عنوان ژورنال: Philosophical Transactions of the Royal Society B: Biological Sciences
سال: 2017
ISSN: 0962-8436,1471-2970
DOI: 10.1098/rstb.2016.0527