dc.contributor.author |
Mak, Oi Wei |
|
dc.contributor.author |
Sharma, Nabangshu |
|
dc.contributor.author |
Reynisson, Jóhannes |
|
dc.contributor.author |
Leung, Ivanhoe KH |
|
dc.coverage.spatial |
England |
|
dc.date.accessioned |
2021-10-05T04:10:17Z |
|
dc.date.available |
2021-10-05T04:10:17Z |
|
dc.date.issued |
2021-4 |
|
dc.identifier.issn |
0960-894X |
|
dc.identifier.uri |
https://hdl.handle.net/2292/56764 |
|
dc.description.abstract |
Heat shock protein 90 (Hsp90) is an essential molecular chaperone that performs vital stress-related and housekeeping functions in cells and is a current therapeutic target for diseases such as cancers. Particularly, the development of Hsp90 C-terminal domain (CTD) inhibitors is highly desirable as inhibitors that target the N-terminal nucleotide-binding domain may cause unwanted biological effects. Herein, we report on the discovery of two drug-like novel Hsp90 CTD inhibitors by using virtual screening and intrinsic protein fluorescence quenching binding assays, paving the way for future development of new therapies that employ molecular chaperone inhibitors. |
|
dc.format.medium |
Print-Electronic |
|
dc.language |
eng |
|
dc.publisher |
Elsevier BV |
|
dc.relation.ispartofseries |
Bioorganic & medicinal chemistry letters |
|
dc.rights |
Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. |
|
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
|
dc.subject |
Humans |
|
dc.subject |
Molecular Chaperones |
|
dc.subject |
Binding Sites |
|
dc.subject |
Molecular Structure |
|
dc.subject |
Structure-Activity Relationship |
|
dc.subject |
Dose-Response Relationship, Drug |
|
dc.subject |
Models, Molecular |
|
dc.subject |
HSP90 Heat-Shock Proteins |
|
dc.subject |
Drug Discovery |
|
dc.subject |
Cancer |
|
dc.subject |
Hsp90 |
|
dc.subject |
Inhibitor |
|
dc.subject |
Molecular chaperone |
|
dc.subject |
Virtual screening |
|
dc.subject |
Binding Sites |
|
dc.subject |
Dose-Response Relationship, Drug |
|
dc.subject |
Drug Discovery |
|
dc.subject |
HSP90 Heat-Shock Proteins |
|
dc.subject |
Humans |
|
dc.subject |
Models, Molecular |
|
dc.subject |
Molecular Chaperones |
|
dc.subject |
Molecular Structure |
|
dc.subject |
Structure-Activity Relationship |
|
dc.subject |
Science & Technology |
|
dc.subject |
Life Sciences & Biomedicine |
|
dc.subject |
Physical Sciences |
|
dc.subject |
Chemistry, Medicinal |
|
dc.subject |
Chemistry, Organic |
|
dc.subject |
Pharmacology & Pharmacy |
|
dc.subject |
Chemistry |
|
dc.subject |
Hsp90 |
|
dc.subject |
Molecular chaperone |
|
dc.subject |
Virtual screening |
|
dc.subject |
Inhibitor |
|
dc.subject |
Cancer |
|
dc.subject |
EMPIRICAL SCORING FUNCTIONS |
|
dc.subject |
PROTEIN-LIGAND DOCKING |
|
dc.subject |
ATP-BINDING |
|
dc.subject |
CONFORMATIONAL DYNAMICS |
|
dc.subject |
BIOLOGICAL EVALUATION |
|
dc.subject |
TARGETING HSP90 |
|
dc.subject |
IN-SILICO |
|
dc.subject |
CANCER |
|
dc.subject |
IDENTIFICATION |
|
dc.subject |
SPECIFICITY |
|
dc.subject |
0304 Medicinal and Biomolecular Chemistry |
|
dc.subject |
0305 Organic Chemistry |
|
dc.subject |
1115 Pharmacology and Pharmaceutical Sciences |
|
dc.title |
Discovery of novel Hsp90 C-terminal domain inhibitors that disrupt co-chaperone binding. |
|
dc.type |
Journal Article |
|
dc.identifier.doi |
10.1016/j.bmcl.2021.127857 |
|
pubs.begin-page |
127857 |
|
pubs.volume |
38 |
|
dc.date.updated |
2021-09-07T02:42:18Z |
|
dc.rights.holder |
Copyright: The author |
en |
pubs.author-url |
https://www.ncbi.nlm.nih.gov/pubmed/33609661 |
|
pubs.publication-status |
Published |
|
dc.rights.accessrights |
http://purl.org/eprint/accessRights/RestrictedAccess |
en |
pubs.subtype |
Research Support, Non-U.S. Gov't |
|
pubs.subtype |
Journal Article |
|
pubs.elements-id |
842253 |
|
dc.identifier.eissn |
1464-3405 |
|
dc.identifier.pii |
S0960-894X(21)00083-4 |
|
pubs.number |
127857 |
|