H2N2V1, Istex, Checkpoint, bibRecord, 000A28

Taking aim at a moving target-inhibitors of influenza virus Part 1 : virus adsorption, entry and uncoating

Identifieur interne : 000A28 ( Istex/Checkpoint ); précédent : 000A27; suivant : 000A29

Taking aim at a moving target-inhibitors of influenza virus Part 1 : virus adsorption, entry and uncoating

Auteurs : Nicholas A. Meanwell ; Mark Krystal

Source :

Drug Discovery Today [ 1359-6446 ] ; 1996.

RBID : ISTEX:996DD2E52B46FFCEAC953A306F4E69327EBB887B

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:

https://api.istex.fr/ark:/67375/6H6-F4PRZ8B7-6/fulltext.pdf

DOI: 10.1016/1359-6446(96)10029-5

Affiliations:

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ISTEX:996DD2E52B46FFCEAC953A306F4E69327EBB887B

Le document en format XML

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<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>
<term>Recent years</term>
<term>Receptor</term>
<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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Taking aim at a moving target-inhibitors of influenza virus Part 1 : virus adsorption, entry and uncoating

Taking aim at a moving target-inhibitors of influenza virus Part 1 : virus adsorption, entry and uncoating

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri