dc.contributor.author |
Son, Soo |
en |
dc.contributor.author |
Huang, Renjie |
en |
dc.contributor.author |
Squire, Christopher |
en |
dc.contributor.author |
Leung, Ka Ho Ivanhoe |
en |
dc.date.accessioned |
2018-12-06T02:02:09Z |
en |
dc.date.issued |
2019-01 |
en |
dc.identifier.citation |
Drug discovery today 24(1):206-216 Jan 2019 |
en |
dc.identifier.issn |
1359-6446 |
en |
dc.identifier.uri |
http://hdl.handle.net/2292/44893 |
en |
dc.description.abstract |
The spread of a novel mobile colistin resistance gene (mcr1) has jeopardised the use of polymyxins, last-resort antibiotics that are used increasingly to treat infections caused by multidrug-resistant (MDR) Gram-negative pathogens. In early 2017, the WHO reported the global spread of mcr1 within a few years after its initial discovery in China. The protein encoded by mcr1 is a putative 60-kDa phosphoethanolamine (pEtN) transferase, MCR-1, and has been studied extensively since its discovery. Herein, we present a comprehensive review of MCR-1 covering its structure, function, and mechanism, to call for the rational drug design of molecular inhibitors of MCR-1 to use in colistin-based combination therapies. |
en |
dc.format.medium |
Print-Electronic |
en |
dc.language |
eng |
en |
dc.relation.ispartofseries |
Drug discovery today |
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. |
en |
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
en |
dc.rights.uri |
http://creativecommons.org/licenses/by-nc-nd/4.0 |
en |
dc.subject |
Bacteria |
en |
dc.subject |
Polymyxins |
en |
dc.subject |
Transferases |
en |
dc.subject |
Escherichia coli Proteins |
en |
dc.subject |
Anti-Bacterial Agents |
en |
dc.subject |
Microbial Sensitivity Tests |
en |
dc.subject |
Drug Resistance, Bacterial |
en |
dc.subject |
Protein Conformation |
en |
dc.title |
MCR-1: a promising target for structure-based design of inhibitors to tackle polymyxin resistance. |
en |
dc.type |
Journal Article |
en |
dc.identifier.doi |
10.1016/j.drudis.2018.07.004 |
en |
pubs.issue |
1 |
en |
pubs.begin-page |
206 |
en |
pubs.volume |
24 |
en |
dc.rights.holder |
Copyright: Elsevier |
en |
pubs.end-page |
216 |
en |
pubs.publication-status |
Published |
en |
dc.rights.accessrights |
http://purl.org/eprint/accessRights/OpenAccess |
en |
pubs.subtype |
Research Support, Non-U.S. Gov't |
en |
pubs.subtype |
Review |
en |
pubs.subtype |
Journal Article |
en |
pubs.elements-id |
750413 |
en |
pubs.org-id |
Science |
en |
pubs.org-id |
Biological Sciences |
en |
pubs.org-id |
Chemistry |
en |
pubs.org-id |
Science Research |
en |
pubs.org-id |
Maurice Wilkins Centre (2010-2014) |
en |
dc.identifier.eissn |
1878-5832 |
en |
pubs.record-created-at-source-date |
2018-07-24 |
en |
pubs.dimensions-id |
30036574 |
en |