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Please use this identifier to cite or link to this item: https://hdl.handle.net/1959.11/5654
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dc.contributor.authorShipp, Christopheren
dc.contributor.authorWatson, Kennethen
dc.contributor.authorJones, Graham Len
dc.date.accessioned2010-04-20T10:04:00Z-
dc.date.issued2009-
dc.identifier.citationPresented at the International Meeting on Signal Transduction Diseaseen
dc.identifier.urihttps://hdl.handle.net/1959.11/5654-
dc.description.abstractThis study investigated the interaction of heat shock proteins (hsps) and their client proteins in tumour and normal human breast tissue. The objective of the study was to discover hsp interactions specific to cancer cells. Hsps have been observed to be over-expressed in a range of human cancers. Of which hsps 70, 90 and others have been noted to be up-regulated in breast cancer. Up-regulation of these hsps has been shown to predict patient prognosis and response to therapies [1, 2]. The majority of hsp90's client proteins are signal transduction proteins. In addition, hsp90 is essential for cellular survival and has been proposed to participate in all 6 "hallmarks of cancer" [3]. Hsp90 inhibitors are under intense investigation and are currently in phase III clinical trials for the treatment of cancer. Hsp90 is known to associate with other hsps in the assembly and function of chaperone complexes. These experiments examined the hsp chaperone complexes and the effect of geldanamycin (an hsp90 inhibitor) on these complexes in human breast cancer.en
dc.languageenen
dc.relation.ispartofPresented at the International Meeting on Signal Transduction Diseaseen
dc.titleHsps 70 and 105 associate with a group of hsp90 client proteins that are selectively found in human breast canceren
dc.typeConference Publicationen
dc.relation.conferenceInternational Meeting on Signal Transduction Disease and Trinational Fall Meeting of the Societies of Biochemistry and Molecular Biologyen
dc.identifier.doi10.3288/contoo.paper.295en
dc.subject.keywordsMolecular Targetsen
local.contributor.firstnameChristopheren
local.contributor.firstnameKennethen
local.contributor.firstnameGraham Len
local.subject.for2008111207 Molecular Targetsen
local.subject.seo2008920102 Cancer and Related Disordersen
local.profile.schoolAdministrationen
local.profile.schoolSchool of Science and Technologyen
local.profile.emailcshipp2@une.edu.auen
local.profile.emailkwatson2@une.edu.auen
local.profile.emailgjones2@une.edu.auen
local.output.categoryE3en
local.record.placeauen
local.record.institutionUniversity of New Englanden
local.identifier.epublicationsrecordune-20091102-11173en
local.date.conference27th - 30th September, 2009en
local.conference.placeAachen, Germanyen
local.publisher.placeOnlineen
local.contributor.lastnameShippen
local.contributor.lastnameWatsonen
local.contributor.lastnameJonesen
dc.identifier.staffune-id:cshipp2en
dc.identifier.staffune-id:kwatson2en
dc.identifier.staffune-id:gjones2en
local.profile.orcid0000-0002-6435-1542en
local.profile.roleauthoren
local.profile.roleauthoren
local.profile.roleauthoren
local.identifier.unepublicationidune:5788en
dc.identifier.academiclevelAcademicen
dc.identifier.academiclevelAcademicen
dc.identifier.academiclevelAcademicen
local.title.maintitleHsps 70 and 105 associate with a group of hsp90 client proteins that are selectively found in human breast canceren
local.output.categorydescriptionE3 Extract of Scholarly Conference Publicationen
local.conference.detailsInternational Meeting on Signal Transduction Disease and Trinational Fall Meeting of the Societies of Biochemistry and Molecular Biology, Aachen, Germany, 27th - 30th September, 2009en
local.search.authorShipp, Christopheren
local.search.authorWatson, Kennethen
local.search.authorJones, Graham Len
local.uneassociationUnknownen
local.year.published2009en
local.date.start2009-09-27-
local.date.end2009-09-30-
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