DOI . ORG {
}
Title[redir]:
Heat shock proteins as targets in oncology | Clinical and Translational Oncology
Description:
Heat shock proteins are ubiquitous molecular chaperones involved in posttranslational folding, stability, activation and maturation of many proteins that are essential mediators of signal transduction and cell cycle progression. Hsp90 proteins are the best studied proteins of this family. A growing number of Hsp90 client proteins have been shown to be important for the development, proliferation and survival of several types of cancer. Inhibition of Hsp90 leads to the degradation of known oncogene products, such as Her2, BRAF and others, leading to the simultaneous blockade of multiple oncogenic transduction pathways. Hsp90 inhibitors, derived from the natural compound geldanamycin, are attractive targets for anticancer drug development. We will review the clinical data on Hsp90 inhibitors in different malignancies. The best known of them, 17-AAG, has shown significant antitumour activity against a broad variety of cancers in preclinical studies, including breast, myeloma, melanoma, prostate and lung cancers. Hsp90 inhibitors can be used as single agents or in combination with other targeted treatments or chemotherapy and radiotherapy. The results of clinical phase II and III trials evaluating the efficacy of these drugs in different types of tumours are awaited.
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Keywords {🔍}
google, scholar, article, cas, pubmed, hsp, cancer, proteins, protein, clin, heat, shock, cell, phase, molecular, inhibitors, oncol, chaperone, inhibitor, biol, res, patients, clinical, geldanamycin, cancers, allylaminodemethoxygeldanamycin, study, privacy, cookies, content, oncology, aag, chem, nature, cells, data, publish, search, targets, montalar, salcedo, abstract, chaperones, access, role, treatment, chapter, heatshock, annu, nat,
Topics {✒️}
month download article/chapter hypoxia-inducible factor anti-tumor antibiotics radicicol atp/adp-binding site joaquín montalar salcedo small-molecule inhibitors hsp90-related protein trap1 nucleophosmin-anaplastic lymphoma kinase cell cycle progression disrupt hsp90/cdc37 complex heat-shock proteins heat shock proteins hsp90-client tyrosine kinase tumor cell sensitivity hsp90 client proteins geldanamycin inhibits migration cell cycle 3 targeted treatments v-src proteins full article pdf hsp90 antagonist 17-allylamino molecular chaperone functions hsp90 molecular chaperone oncogene products multiple genome abnormalities privacy choices/manage cookies hypoxia-induced transcription tyrosine kinase inhibitors translational oncology aims dt-diaphorase expression montalar salcedo kinase-dependent cancers colon cancer cells pancreatic cancer cells related subjects identification ansamycin hsp90 inhibitor cancer chemotherapeutic agents npm-alk expression european economic area iii trials evaluating distinct functional properties tumour tactics puffing pattern induced ch/downloads/hsp90interactors potent antitumor activity high-affinity conformation hsp90 proteins glioma cell invasion natural compound geldanamycin
Questions {❓}
- Workman P (2003) Strategies for treating cancers caused by multiple genome abnormalities: from concepts to cures?
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headline:Heat shock proteins as targets in oncology
description:Heat shock proteins are ubiquitous molecular chaperones involved in posttranslational folding, stability, activation and maturation of many proteins that are essential mediators of signal transduction and cell cycle progression. Hsp90 proteins are the best studied proteins of this family. A growing number of Hsp90 client proteins have been shown to be important for the development, proliferation and survival of several types of cancer. Inhibition of Hsp90 leads to the degradation of known oncogene products, such as Her2, BRAF and others, leading to the simultaneous blockade of multiple oncogenic transduction pathways. Hsp90 inhibitors, derived from the natural compound geldanamycin, are attractive targets for anticancer drug development. We will review the clinical data on Hsp90 inhibitors in different malignancies. The best known of them, 17-AAG, has shown significant antitumour activity against a broad variety of cancers in preclinical studies, including breast, myeloma, melanoma, prostate and lung cancers. Hsp90 inhibitors can be used as single agents or in combination with other targeted treatments or chemotherapy and radiotherapy. The results of clinical phase II and III trials evaluating the efficacy of these drugs in different types of tumours are awaited.
datePublished:2010-03-27T00:00:00Z
dateModified:2010-03-27T00:00:00Z
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HSP
Hsp90 inhibitors
Chaperones
Cancer
17-AAG
Oncology
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headline:Heat shock proteins as targets in oncology
description:Heat shock proteins are ubiquitous molecular chaperones involved in posttranslational folding, stability, activation and maturation of many proteins that are essential mediators of signal transduction and cell cycle progression. Hsp90 proteins are the best studied proteins of this family. A growing number of Hsp90 client proteins have been shown to be important for the development, proliferation and survival of several types of cancer. Inhibition of Hsp90 leads to the degradation of known oncogene products, such as Her2, BRAF and others, leading to the simultaneous blockade of multiple oncogenic transduction pathways. Hsp90 inhibitors, derived from the natural compound geldanamycin, are attractive targets for anticancer drug development. We will review the clinical data on Hsp90 inhibitors in different malignancies. The best known of them, 17-AAG, has shown significant antitumour activity against a broad variety of cancers in preclinical studies, including breast, myeloma, melanoma, prostate and lung cancers. Hsp90 inhibitors can be used as single agents or in combination with other targeted treatments or chemotherapy and radiotherapy. The results of clinical phase II and III trials evaluating the efficacy of these drugs in different types of tumours are awaited.
datePublished:2010-03-27T00:00:00Z
dateModified:2010-03-27T00:00:00Z
pageStart:166
pageEnd:173
sameAs:https://doi.org/10.1007/s12094-010-0486-8
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HSP
Hsp90 inhibitors
Chaperones
Cancer
17-AAG
Oncology
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1699-3055
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