dc.contributor.author | Evans, LE | |
dc.contributor.author | Cheeseman, MD | |
dc.contributor.author | Yahya, N | |
dc.contributor.author | Jones, K | |
dc.date.accessioned | 2020-07-24T14:57:55Z | |
dc.date.issued | 2015-10-12 | |
dc.identifier.citation | PloS one, 2015, 10 (10), pp. e0140006 - ? | |
dc.identifier.issn | 1932-6203 | |
dc.identifier.uri | https://repository.icr.ac.uk/handle/internal/3861 | |
dc.identifier.eissn | 1932-6203 | |
dc.identifier.doi | 10.1371/journal.pone.0140006 | |
dc.description.abstract | The 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.format | Electronic-eCollection | |
dc.format.extent | e0140006 - ? | |
dc.language | eng | |
dc.language.iso | eng | |
dc.publisher | PUBLIC LIBRARY SCIENCE | |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0 | |
dc.subject | Animals | |
dc.subject | Humans | |
dc.subject | Rats | |
dc.subject | Benzamides | |
dc.subject | Imidazoles | |
dc.subject | Protein Isoforms | |
dc.subject | Adenosine Triphosphate | |
dc.subject | Antineoplastic Agents | |
dc.subject | Fluorescent Dyes | |
dc.subject | Surface Plasmon Resonance | |
dc.subject | Binding Sites | |
dc.subject | Protein Binding | |
dc.subject | HSP70 Heat-Shock Proteins | |
dc.subject | HSC70 Heat-Shock Proteins | |
dc.subject | Dynamic Light Scattering | |
dc.title | Investigating Apoptozole as a Chemical Probe for HSP70 Inhibition. | |
dc.type | Journal Article | |
dcterms.dateAccepted | 2015-09-02 | |
rioxxterms.versionofrecord | 10.1371/journal.pone.0140006 | |
rioxxterms.licenseref.uri | https://creativecommons.org/licenses/by/4.0 | |
rioxxterms.licenseref.startdate | 2015-01 | |
rioxxterms.type | Journal Article/Review | |
dc.relation.isPartOf | PloS one | |
pubs.issue | 10 | |
pubs.notes | Not 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-status | Published | |
pubs.volume | 10 | |
pubs.embargo.terms | Not known | |
icr.researchteam | Medicinal Chemistry 3 | |
dc.contributor.icrauthor | Cheeseman, Matthew | |
dc.contributor.icrauthor | Jones, Keith | |