Taking aim at a moving target-inhibitors of influenza virus Part 1 : virus adsorption, entry and uncoating
Identifieur interne : 001310 ( Istex/Curation ); précédent : 001309; suivant : 001311Taking aim at a moving target-inhibitors of influenza virus Part 1 : virus adsorption, entry and uncoating
Auteurs : Nicholas A. Meanwell ; Mark KrystalSource :
- Drug Discovery Today [ 1359-6446 ] ; 1996.
English descriptors
- Teeft :
- Acid changes, Agents chemother, Amantadine, Analogous protein, Antigenic, Antigenic drift, Antigenic shift, August, Bicyclic amines, Cell surface receptors, Channel protein, Chem, Chemother, Clinical trials, Conformational, Conformational change, Conformational rearrangement, Crystal structure, Drug design, Drug discovery, Effective sialic acid receptor antagonists, Endosomal, Endosomal acidification, Endosomal membrane, Endosomal membranes, Endosomal pathway, Essential step, Etal, Fusion peptide, Host cell membranes, Immune system, Influenza, Influenza infections, Influenza infectivity, Influenza virus, Influenza virus hemagglutinin binding, Influenza virus infection, Influenza viruses, Inhibitor, Liposomal preparations, Many details, Membrane, Membrane fusion, Nat1 acad, Native state, Polymeric species, Potential drug candidates, Recent years, Receptor, Rimantadine, Second part, Second reading frame, Sialic, Sialic acid, Sialic acid binding site, Sialic acid moieties, Sialic acid residues, Structural composition, Therapeutic intervention, Therapeutic treatment, Transmembrane domain, Uncoating, Vaccination program, Viral, Viral entry, Viral membrane, Viral membranes, Viral strains, Viral uncoating, Virus.
Abstract
Annual epidemics of influenza virus infection are responsible for considerable morbidity and mortality, and pandemics are much more devastating. Considerable knowledge of viral infectivity and replication has been acquired, but many details have yet to be elucidated and the virus remains a particularly challenging target for drug design and development. In this two part review, the current status of influenza research is summarized in the context of inhibitor design and discovery, and recent advances in the search for clinically effective drug therapy are detailed. The first part addresses virus adsorption, entry and uncoating; the second part, to be published in the September issue of Drug Discovery Today, discusses aspects of virus replication, packaging and release.
Url:
DOI: 10.1016/1359-6446(96)10029-5
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Nicholas A. Meanwell<affiliation><mods:affiliation>E-mail: nicholasa.meanwell@ccmail.bms.com</mods:affiliation>
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<affiliation><mods:affiliation>Departments of Chemistry and Virology, The Bristol-Myers Squibb Pharmaceutical Research Institute, 5 Research Parkway, Wallingford, CT 06492, USA. tel: +1 203 284 6679, fax: +1 203 284 7702</mods:affiliation>
<wicri:noCountry code="subField">7702</wicri:noCountry>
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Le document en format XML
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<term>Amantadine</term>
<term>Analogous protein</term>
<term>Antigenic</term>
<term>Antigenic drift</term>
<term>Antigenic shift</term>
<term>August</term>
<term>Bicyclic amines</term>
<term>Cell surface receptors</term>
<term>Channel protein</term>
<term>Chem</term>
<term>Chemother</term>
<term>Clinical trials</term>
<term>Conformational</term>
<term>Conformational change</term>
<term>Conformational rearrangement</term>
<term>Crystal structure</term>
<term>Drug design</term>
<term>Drug discovery</term>
<term>Effective sialic acid receptor antagonists</term>
<term>Endosomal</term>
<term>Endosomal acidification</term>
<term>Endosomal membrane</term>
<term>Endosomal membranes</term>
<term>Endosomal pathway</term>
<term>Essential step</term>
<term>Etal</term>
<term>Fusion peptide</term>
<term>Host cell membranes</term>
<term>Immune system</term>
<term>Influenza</term>
<term>Influenza infections</term>
<term>Influenza infectivity</term>
<term>Influenza virus</term>
<term>Influenza virus hemagglutinin binding</term>
<term>Influenza virus infection</term>
<term>Influenza viruses</term>
<term>Inhibitor</term>
<term>Liposomal preparations</term>
<term>Many details</term>
<term>Membrane</term>
<term>Membrane fusion</term>
<term>Nat1 acad</term>
<term>Native state</term>
<term>Polymeric species</term>
<term>Potential drug candidates</term>
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<term>Rimantadine</term>
<term>Second part</term>
<term>Second reading frame</term>
<term>Sialic</term>
<term>Sialic acid</term>
<term>Sialic acid binding site</term>
<term>Sialic acid moieties</term>
<term>Sialic acid residues</term>
<term>Structural composition</term>
<term>Therapeutic intervention</term>
<term>Therapeutic treatment</term>
<term>Transmembrane domain</term>
<term>Uncoating</term>
<term>Vaccination program</term>
<term>Viral</term>
<term>Viral entry</term>
<term>Viral membrane</term>
<term>Viral membranes</term>
<term>Viral strains</term>
<term>Viral uncoating</term>
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<front><div type="abstract" xml:lang="en">Annual epidemics of influenza virus infection are responsible for considerable morbidity and mortality, and pandemics are much more devastating. Considerable knowledge of viral infectivity and replication has been acquired, but many details have yet to be elucidated and the virus remains a particularly challenging target for drug design and development. In this two part review, the current status of influenza research is summarized in the context of inhibitor design and discovery, and recent advances in the search for clinically effective drug therapy are detailed. The first part addresses virus adsorption, entry and uncoating; the second part, to be published in the September issue of Drug Discovery Today, discusses aspects of virus replication, packaging and release.</div>
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