About: Put a cork in it: Plugging the M2 viral ion channel to sink influenza

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An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Put a cork in it: Plugging the M2 viral ion channel to sink influenza
Creator	Wang, Jun Duncan, M Duncan, Maggie Fedida, D Fedida, David Jalily, P Jalily, Pouria Tietjen, Ian
Source	Elsevier; Medline; PMC
abstract	Abstract The ongoing threat of seasonal and pandemic influenza to human health requires antivirals that can effectively supplement existing vaccination strategies. The M2 protein of influenza A virus (IAV) is a proton-gated, proton-selective ion channel that is required for virus replication and is an established antiviral target. While licensed adamantane-based M2 antivirals have been historically used, M2 mutations that confer major adamantane resistance are now so prevalent in circulating virus strains that these drugs are no longer recommended. Here we review the current understanding of IAV M2 structure and function, mechanisms of inhibition, the rise of drug resistance mutations, and ongoing efforts to develop new antivirals that target resistant forms of M2.
has issue date	2020-03-27(xsd:dateTime)
bibo:doi	10.1016/j.antiviral.2020.104780
bibo:pmid	32229237
has license	els-covid
sha1sum (hex)	c9b5c243c70a4e61bd44cdcfe6ed29c8d9be4949
schema:url	https://doi.org/10.1016/j.antiviral.2020.104780
resource representing a document's title	Put a cork in it: Plugging the M2 viral ion channel to sink influenza
has PubMed Central identifier	PMC7102647
has PubMed identifier	32229237
schema:publication	Antiviral Res
resource representing a document's body	covid:c9b5c243c70a4e61bd44cdcfe6ed29c8d9be4949#body_text
is schema:about of	named entity 'strains' named entity 'THERAPIES' named entity 'REQUIRED' named entity 'CURRENT' named entity 'MUTATIONS' named entity 'RISE' named entity 'STRATEGIES' named entity 'IS A' named entity 'DRUG RESISTANCE' named entity 'VIRAL REPLICATION' named entity 'STRUCTURE' named entity 'INFLUENZA' named entity 'CORK' named entity 'M2 PROTEIN' named entity 'FUNCTION' named entity 'NEW' named entity 'ANTIVIRAL' named entity '80%' named entity 'STRAINS' named entity 'ION CHANNEL' named entity 'VIRAL' named entity 'PROTON CHANNEL' named entity 'INFLUENZA A' named entity 'PRE' named entity 'JOURNAL ' named entity 'SINK' named entity 'INFLUENZA' named entity 'LICENSED' named entity 'ANTIVIRALS' named entity 'TARGET' named entity 'PLUGGING' named entity 'PROOF' named entity 'PROTEIN ' named entity 'RESISTANT TO' named entity 'NEEDED' named entity 'GATED' named entity 'PROTON' named entity 'proton' named entity 'function' named entity 'current' named entity 'M2 protein' named entity 'ion' named entity 'influenza' named entity 'proton' named entity 'ion channel' named entity 'binding site' named entity 'Trp' named entity 'amantadine' named entity 'proton' named entity 'high throughput screening' named entity 'PDB' named entity 'amantadine' named entity 'drug molecule' named entity 'loss-of-function' named entity 'oseltamivir' named entity 'NIH' named entity 'moiety' named entity 'mutation' named entity 'binding mechanism' named entity 'hydronium ion' named entity 'nickel' named entity 'molecular dynamics' named entity 'low pH' named entity 'methylated' named entity 'high-throughput screening' named entity 'micelles' named entity 'IAV' named entity 'Casarotto' named entity 'PDB' named entity 'drug-resistant' named entity 'follow-up studies' named entity 'nonpolar' named entity 'virology' named entity 'adamantane'

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