How does each substituent functional group of oseltamivir lose its activity against virulent H5N1 influenza mutants?
- 30 November 2009
- journal article
- Published by Elsevier in Biophysical Chemistry
- Vol. 145 (1) , 29-36
- https://doi.org/10.1016/j.bpc.2009.08.006
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Crystal structures of oseltamivir-resistant influenza virus neuraminidase mutantsNature, 2008
- Mutations of neuraminidase implicated in neuraminidase inhibitors resistanceJournal of Clinical Virology, 2008
- Neuraminidase Inhibitor-Resistant Recombinant A/Vietnam/1203/04 (H5N1) Influenza Viruses Retain Their Replication Efficiency and Pathogenicity In Vitro and In VivoJournal of Virology, 2007
- Antiviral agents active against influenza A virusesNature Reviews Drug Discovery, 2006
- Oseltamivir Resistance during Treatment of Influenza A (H5N1) InfectionNew England Journal of Medicine, 2005
- Susceptibilities of Antiviral-Resistant Influenza Viruses to Novel Neuraminidase InhibitorsAntimicrobial Agents and Chemotherapy, 2005
- Isolation of drug-resistant H5N1 virusNature, 2005
- Resistant influenza A viruses in children treated with oseltamivir: descriptive studyPublished by Elsevier ,2004
- Mechanism by Which Mutations at His274 Alter Sensitivity of Influenza A Virus N1 Neuraminidase to Oseltamivir Carboxylate and ZanamivirAntimicrobial Agents and Chemotherapy, 2002
- The H274Y mutation in the influenza A/H1N1 neuraminidase active site following oseltamivir phosphate treatment leave virus severely compromised both in vitro and in vivoAntiviral Research, 2002