dc.contributor.author |
Fung, Sai |
en |
dc.contributor.author |
Wang, H |
en |
dc.contributor.author |
Tomek, Petr |
en |
dc.contributor.author |
Squire, Christopher |
en |
dc.contributor.author |
Flanagan, Jack |
en |
dc.contributor.author |
Palmer, Brian |
en |
dc.contributor.author |
Bridewell, DJA |
en |
dc.contributor.author |
Tijono, Sofian |
en |
dc.contributor.author |
Jamie, JF |
en |
dc.contributor.author |
Ching, Lai-Ming |
en |
dc.date.accessioned |
2015-12-01T22:08:39Z |
en |
dc.date.issued |
2013-12-15 |
en |
dc.identifier.citation |
Bioorganic and Medicinal Chemistry, 2013, 21 (24), pp. 7595 - 7603 |
en |
dc.identifier.issn |
0968-0896 |
en |
dc.identifier.uri |
http://hdl.handle.net/2292/27625 |
en |
dc.description.abstract |
Screening of a fragment library identified 2-hydrazinobenzothiazole as a potent inhibitor of indoleamine 2,3-dioxygenase 1 (IDO1), an enzyme expressed by tumours that suppresses the immune system. Spectroscopic studies indicated that 2-hydrazinobenzothiazole interacted with the IDO1 haem and in silico docking predicted that the interaction was through hydrazine. Subsequent studies of hydrazine derivatives identified phenylhydrazine (IC50=0.25 ± 0.07 μM) to be 32-fold more potent than 2-hydrazinobenzothiazole (IC50=8.0 ± 2.3 μM) in inhibiting rhIDO1 and that it inhibited cellular IDO1 at concentrations that were noncytotoxic to cells. Here, phenylhydrazine is shown to inhibit IDO1 through binding to haem. |
en |
dc.description.uri |
http://www.ncbi.nlm.nih.gov/pubmed/24262887 |
en |
dc.format.medium |
Print-Electronic |
en |
dc.language |
eng |
en |
dc.publisher |
Elsevier |
en |
dc.relation.ispartofseries |
Bioorganic and Medicinal Chemistry |
en |
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. Details obtained from http://www.sherpa.ac.uk/romeo/issn/0968-0896/
https://www.elsevier.com/about/company-information/policies/sharing |
en |
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
en |
dc.subject |
Cell Line, Tumor |
en |
dc.subject |
Immune System |
en |
dc.subject |
Animals |
en |
dc.subject |
Humans |
en |
dc.subject |
Mice |
en |
dc.subject |
Hydrazines |
en |
dc.subject |
Recombinant Proteins |
en |
dc.subject |
Enzyme Inhibitors |
en |
dc.subject |
Molecular Structure |
en |
dc.subject |
Structure-Activity Relationship |
en |
dc.subject |
Dose-Response Relationship, Drug |
en |
dc.subject |
Models, Molecular |
en |
dc.subject |
Indoleamine-Pyrrole 2,3,-Dioxygenase |
en |
dc.subject |
Drug Discovery |
en |
dc.title |
Discovery and characterisation of hydrazines as inhibitors of the immune suppressive enzyme, indoleamine 2,3-dioxygenase 1 (IDO1) |
en |
dc.type |
Journal Article |
en |
dc.identifier.doi |
10.1016/j.bmc.2013.10.037 |
en |
pubs.issue |
24 |
en |
pubs.begin-page |
7595 |
en |
pubs.volume |
21 |
en |
dc.rights.holder |
Copyright:
Elsevier |
en |
dc.identifier.pmid |
24262887 |
en |
pubs.author-url |
http://www.sciencedirect.com/science/article/pii/S0968089613009115 |
en |
pubs.end-page |
7603 |
en |
pubs.publication-status |
Published |
en |
dc.rights.accessrights |
http://purl.org/eprint/accessRights/RestrictedAccess |
en |
pubs.subtype |
Article |
en |
pubs.elements-id |
410443 |
en |
pubs.org-id |
Medical and Health Sciences |
en |
pubs.org-id |
Medical Sciences |
en |
pubs.org-id |
Auckland Cancer Research |
en |
pubs.org-id |
Pharmacology |
en |
pubs.org-id |
Science |
en |
pubs.org-id |
Biological Sciences |
en |
pubs.org-id |
Science Research |
en |
pubs.org-id |
Maurice Wilkins Centre (2010-2014) |
en |
dc.identifier.eissn |
1464-3391 |
en |
pubs.record-created-at-source-date |
2015-12-02 |
en |
pubs.dimensions-id |
24262887 |
en |