MCR-1: a promising target for structure-based design of inhibitors to tackle polymyxin resistance.

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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


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