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- W2023261559 abstract "Geldanamycin is a benzoquinone ansamycin antibiotic that manifests anti-cancer activity through the inhibition of HSP90-chaperone function. The HSP90 molecular chaperone is expressed at high levels in a wide variety of human cancers including melanoma, leukemia, and cancers in colon, prostate, lung, and breast. In cancer cells dependent upon mutated and/or over-expressed oncogene proteins, HSP90 is thought to have a critical role in regulating the stability, folding, and activity of HSP90-associated proteins, so-called “client proteins”. These client proteins include the growth-stimulating proteins and kinases that support malignant transformation. Recently, oncogenic activating BRAF mutants have been identified in variety of cancers where constitutive activation of the MEK/ERK MAPK signaling pathway is the key for tumorigenesis, and they have been shown to be client proteins for HSP90. Accordingly, HSP90 inhibition can suppress certain cancer-causing client proteins and therefore represents an important therapeutic target. The molecular mechanism underlying the anti-cancer effect of HSP90 inhibition is complicated. Geldanamycin and its derivatives have been shown to induce the depletion of mutationally-activated BRAF through several mechanisms. In this review, we will describe the HSP90-inhibitory mechanism, focusing on recent progress in understanding HSP90 chaperone structure–function relationships, the identification of new HSP90 client proteins and the development of HSP90 inhibitors for clinical applications." @default.
- W2023261559 created "2016-06-24" @default.
- W2023261559 creator A5012402474 @default.
- W2023261559 creator A5038084628 @default.
- W2023261559 creator A5075844121 @default.
- W2023261559 date "2010-04-01" @default.
- W2023261559 modified "2023-10-17" @default.
- W2023261559 title "Geldanamycin and its anti-cancer activities" @default.
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