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dc.date.accessioned2018-06-05T14:50:02Z
dc.date.issued2011-01en_US
dc.identifierhttp://publications.icr.ac.uk/10309/en_US
dc.identifier.citation2011, pp. 328 - 345en_US
dc.identifier.issn0007-1188en_US
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/1723
dc.description.abstractCytosolic heat shock proteins have received significant attention as emerging therapeutic targets. Much of this excitement has been triggered by the discovery that HSP90 plays a central role in the maintenance and stability of multifarious oncogenic membrane receptors and their resultant tyrosine kinase activity. Numerous studies have dealt with the effects of small molecules on chaperone- and stress-related pathways of the endoplasmic reticulum (ER). However, unlike cytosolic chaperones, relatively little emphasis has been placed upon translational avenues towards targeting of the ER for inhibition of folding/secretion of disease-promoting proteins. Here, we summarise existing small molecule inhibitors and potential future targets of ER chaperone-mediated inhibition. Client proteins of translational relevance in disease treatment are outlined, alongside putative future disease treatment modalities based on ER-centric targeted therapies. Particular attention is paid to cancer and autoimmune disorders via the effects of the GRP94 inhibitor geldanamycin and its population of client proteins, overloading of the unfolded protein response, and inhibition of members of the IL-12 family of cytokines by celecoxib and non-coxib analogues.en_US
dc.format.extent328 - 345en_US
dc.publisherWILEY-BLACKWELL PUBLISHING, INCen_US
dc.subjectGRP94; heat shock proteins; calreticulin; geldanamycin; celecoxib; glucosidase; unfolded protein response; cancer; autoimmunity; IL-12;VIRAL DIARRHEA VIRUS; OXYGEN-REGULATED PROTEIN; HEAT-SHOCK-PROTEIN; HEPATITIS-C VIRUS; N-BUTYL-DEOXYNOJIRIMYCIN; GROWTH-FACTOR RECEPTOR; ALPHA-GLUCOSIDASE INHIBITORS; NUCLEOTIDE EXCHANGE FACTOR; STRESS-RESPONSE ELEMENT; PROSTATE-CANCER CELLSen_US
dc.titleThe endoplasmic reticulum protein folding factory and its chaperones: new targets for drug discovery?en_US
dc.typeOther
rioxxterms.licenseref.startdate2011-01en_US
rioxxterms.typeotheren_US
pubs.notesNot knownen_US
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Cancer Biology
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Cancer Biology/Targeted Therapy
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Radiotherapy and Imaging
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Radiotherapy and Imaging/Targeted Therapy
pubs.place-of-publicationCOMMERCE PLACE, 350 MAIN ST, MALDEN 02148, MA USAen_US
pubs.embargo.termsNot knownen_US
icr.researchteamTargeted Therapyen_US
dc.contributor.icrauthorMcLaughlin, Martinen_US


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