Hdl Handle:
http://hdl.handle.net/10675.2/570
Title:
Targeting HSP90 for cancer therapy
Authors:
Mahalingam, D; Swords, R; Carew, Jennifer S; Nawrocki, S T; Bhalla, Kapil N.; Giles, F J
Abstract:
Heat-shock proteins (HSPs) are molecular chaperones that regulate protein folding to ensure correct conformation and translocation and to avoid protein aggregation. Heat-shock proteins are increased in many solid tumours and haematological malignancies. Many oncogenic proteins responsible for the transformation of cells to cancerous forms are client proteins of HSP90. Targeting HSP90 with chemical inhibitors would degrade these oncogenic proteins, and thus serve as useful anticancer agents. This review provides an overview of the HSP chaperone machinery and the structure and function of HSP90. We also highlight the key oncogenic proteins that are regulated by HSP90 and describe how inhibition of HSP90 could alter the activity of multiple signalling proteins, receptors and transcriptional factors implicated in carcinogenesis.
Citation:
Br J Cancer. 2009 May 19; 100(10):1523-1529
Issue Date:
28-Apr-2009 ; 19-May-2009
URI:
http://hdl.handle.net/10675.2/570
DOI:
10.1038/sj.bjc.6605066
PubMed ID:
19401686
PubMed Central ID:
PMC2696754
Type:
Article
ISSN:
1532-1827
Appears in Collections:
Georgia Cancer Center: Faculty Research and Presentations

Full metadata record

DC FieldValue Language
dc.contributor.authorMahalingam, Den_US
dc.contributor.authorSwords, Ren_US
dc.contributor.authorCarew, Jennifer Sen_US
dc.contributor.authorNawrocki, S Ten_US
dc.contributor.authorBhalla, Kapil N.en_US
dc.contributor.authorGiles, F Jen_US
dc.date.accessioned2012-10-26T16:26:43Z-
dc.date.available2012-10-26T16:26:43Z-
dc.date.issued2009-04-28en_US
dc.date.issued2009-05-19en_US
dc.identifier.citationBr J Cancer. 2009 May 19; 100(10):1523-1529en_US
dc.identifier.issn1532-1827en_US
dc.identifier.pmid19401686en_US
dc.identifier.doi10.1038/sj.bjc.6605066en_US
dc.identifier.urihttp://hdl.handle.net/10675.2/570-
dc.description.abstractHeat-shock proteins (HSPs) are molecular chaperones that regulate protein folding to ensure correct conformation and translocation and to avoid protein aggregation. Heat-shock proteins are increased in many solid tumours and haematological malignancies. Many oncogenic proteins responsible for the transformation of cells to cancerous forms are client proteins of HSP90. Targeting HSP90 with chemical inhibitors would degrade these oncogenic proteins, and thus serve as useful anticancer agents. This review provides an overview of the HSP chaperone machinery and the structure and function of HSP90. We also highlight the key oncogenic proteins that are regulated by HSP90 and describe how inhibition of HSP90 could alter the activity of multiple signalling proteins, receptors and transcriptional factors implicated in carcinogenesis.en_US
dc.rightsCopyright 2009, Cancer Research UKen_US
dc.subjectMinireviewsen_US
dc.titleTargeting HSP90 for cancer therapyen_US
dc.typeArticleen_US
dc.identifier.pmcidPMC2696754en_US
dc.contributor.corporatenameGHSU Cancer Center-

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