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- Publisher Website: 10.1021/acsinfecdis.7b00265
- Scopus: eid_2-s2.0-85043464032
- PMID: 29355011
- WOS: WOS:000427443200002
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Article: Inhibitors of Influenza A Virus Polymerase
Title | Inhibitors of Influenza A Virus Polymerase |
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Authors | |
Issue Date | 2018 |
Publisher | American Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/aidcbc |
Citation | ACS Infectious Diseases, 2018, v. 4 n. 3, p. 218-223 How to Cite? |
Abstract | The propensity of influenza virus to develop resistance to commonly prescribed drugs highlights the need for continuing development of new therapeutics. Biological and structural investigations of the enzymatic and interaction domains among influenza A virus polymerase subunits have broadened the target reservoir for drug screening. With the wealth of knowledge from these studies, identification of small-molecule and peptidic inhibitors that specifically abrogate polymerase activity or disrupt the polymerase assembly has emerged as an innovative and promising approach. Importantly, those domains are highly conserved among influenza subtypes and thus minimize the emergence of drug resistant mutants. An overview of the reported enzymatic inhibitors and protein-protein disruptors has been provided, in our effort to facilitate the development of next-generation anti-influenza therapeutics. © 2018 American Chemical Society. |
Persistent Identifier | http://hdl.handle.net/10722/276334 |
ISSN | 2023 Impact Factor: 4.0 2023 SCImago Journal Rankings: 1.179 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Yuan, S | - |
dc.contributor.author | Wen, L | - |
dc.contributor.author | Zhou, J | - |
dc.date.accessioned | 2019-09-10T03:00:59Z | - |
dc.date.available | 2019-09-10T03:00:59Z | - |
dc.date.issued | 2018 | - |
dc.identifier.citation | ACS Infectious Diseases, 2018, v. 4 n. 3, p. 218-223 | - |
dc.identifier.issn | 2373-8227 | - |
dc.identifier.uri | http://hdl.handle.net/10722/276334 | - |
dc.description.abstract | The propensity of influenza virus to develop resistance to commonly prescribed drugs highlights the need for continuing development of new therapeutics. Biological and structural investigations of the enzymatic and interaction domains among influenza A virus polymerase subunits have broadened the target reservoir for drug screening. With the wealth of knowledge from these studies, identification of small-molecule and peptidic inhibitors that specifically abrogate polymerase activity or disrupt the polymerase assembly has emerged as an innovative and promising approach. Importantly, those domains are highly conserved among influenza subtypes and thus minimize the emergence of drug resistant mutants. An overview of the reported enzymatic inhibitors and protein-protein disruptors has been provided, in our effort to facilitate the development of next-generation anti-influenza therapeutics. © 2018 American Chemical Society. | - |
dc.language | eng | - |
dc.publisher | American Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/aidcbc | - |
dc.relation.ispartof | ACS Infectious Diseases | - |
dc.title | Inhibitors of Influenza A Virus Polymerase | - |
dc.type | Article | - |
dc.identifier.email | Yuan, S: yuansf@hku.hk | - |
dc.identifier.email | Zhou, J: jiezhou@hku.hk | - |
dc.identifier.authority | Zhou, J=rp01412 | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1021/acsinfecdis.7b00265 | - |
dc.identifier.pmid | 29355011 | - |
dc.identifier.scopus | eid_2-s2.0-85043464032 | - |
dc.identifier.hkuros | 302709 | - |
dc.identifier.volume | 4 | - |
dc.identifier.issue | 3 | - |
dc.identifier.spage | 218 | - |
dc.identifier.epage | 223 | - |
dc.identifier.isi | WOS:000427443200002 | - |
dc.publisher.place | United States | - |
dc.identifier.issnl | 2373-8227 | - |