Show simple item record

dc.contributor.authorEvans, LE
dc.contributor.authorCheeseman, MD
dc.contributor.authorYahya, N
dc.contributor.authorJones, K
dc.date.accessioned2020-07-24T14:57:55Z
dc.date.issued2015-10-12
dc.identifier.citationPloS one, 2015, 10 (10), pp. e0140006 - ?
dc.identifier.issn1932-6203
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/3861
dc.identifier.eissn1932-6203
dc.identifier.doi10.1371/journal.pone.0140006
dc.description.abstractThe use of chemical tools to validate clinical targets has gained in popularity over recent years and the importance of understanding the activity, selectivity and mechanism of action of these compounds is well recognized. Dysregulation of the HSP70 protein family has been linked to multiple cancer types and drug resistance, highlighting their importance as popular targets for anti-cancer drug development. Apoptozole is a recently identified small molecule, which has been reported to possess strong affinity for the HSP70 isoforms HSP72 and HSC70. We investigated apoptozole as a potential chemical tool for HSP70 inhibition. Unfortunately, using both biochemical and biophysical techniques, we were unable to find any experimental evidence that apoptozole binds to HSP70 in a specific and developable way. Instead, we provide experimental evidence that apoptozole forms aggregates under aqueous conditions that could interact with HSP70 proteins in a non-specific manner.
dc.formatElectronic-eCollection
dc.format.extente0140006 - ?
dc.languageeng
dc.language.isoeng
dc.publisherPUBLIC LIBRARY SCIENCE
dc.rights.urihttps://creativecommons.org/licenses/by/4.0
dc.subjectAnimals
dc.subjectHumans
dc.subjectRats
dc.subjectBenzamides
dc.subjectImidazoles
dc.subjectProtein Isoforms
dc.subjectAdenosine Triphosphate
dc.subjectAntineoplastic Agents
dc.subjectFluorescent Dyes
dc.subjectSurface Plasmon Resonance
dc.subjectBinding Sites
dc.subjectProtein Binding
dc.subjectHSP70 Heat-Shock Proteins
dc.subjectHSC70 Heat-Shock Proteins
dc.subjectDynamic Light Scattering
dc.titleInvestigating Apoptozole as a Chemical Probe for HSP70 Inhibition.
dc.typeJournal Article
dcterms.dateAccepted2015-09-02
rioxxterms.versionofrecord10.1371/journal.pone.0140006
rioxxterms.licenseref.urihttps://creativecommons.org/licenses/by/4.0
rioxxterms.licenseref.startdate2015-01
rioxxterms.typeJournal Article/Review
dc.relation.isPartOfPloS one
pubs.issue10
pubs.notesNot known
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 Therapeutics
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Cancer Therapeutics/Medicinal Chemistry 3
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 Therapeutics
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Cancer Therapeutics/Medicinal Chemistry 3
pubs.publication-statusPublished
pubs.volume10
pubs.embargo.termsNot known
icr.researchteamMedicinal Chemistry 3
dc.contributor.icrauthorCheeseman, Matthew
dc.contributor.icrauthorJones, Keith


Files in this item

Thumbnail

This item appears in the following collection(s)

Show simple item record

https://creativecommons.org/licenses/by/4.0
Except where otherwise noted, this item's license is described as https://creativecommons.org/licenses/by/4.0