About: The Proteolytic Regulation of Virus Cell Entry by Furin and Other Proprotein Convertases

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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
title	The Proteolytic Regulation of Virus Cell Entry by Furin and Other Proprotein Convertases
Creator	Izaguirre, Gonzalo
source	Medline; PMC
abstract	A wide variety of viruses exploit furin and other proprotein convertases (PCs) of the constitutive protein secretion pathway in order to regulate their cell entry mechanism and infectivity. Surface proteins of enveloped, as well as non-enveloped, viruses become processed by these proteases intracellularly during morphogenesis or extracellularly after egress and during entry in order to produce mature virions activated for infection. Although viruses also take advantage of other proteases, it is when some viruses become reactive with PCs that they may develop high pathogenicity. Besides reacting with furin, some viruses may also react with the PCs of the other specificity group constituted by PC4/PC5/PACE4/PC7. The targeting of PCs for inhibition may result in a useful strategy to treat infections with some highly pathogenic viruses. A wide variety of PC inhibitors have been developed and tested for their antiviral activity in cell-based assays.
has issue date	2019-09-09(xsd:dateTime)
bibo:doi	10.3390/v11090837
bibo:pmid	31505793
has license	cc-by
sha1sum (hex)	f7453f0f1f131d4f8603bf708f8c08d9b9e8806f
schema:url	https://doi.org/10.3390/v11090837
resource representing a document's title	The Proteolytic Regulation of Virus Cell Entry by Furin and Other Proprotein Convertases
has PubMed Central identifier	PMC6784293
has PubMed identifier	31505793
schema:publication	Viruses
resource representing a document's body	covid:f7453f0f1f131d4f8603bf708f8c08d9b9e8806f#body_text
is schema:about of	named entity 'ENTRY' named entity 'INFECTIVITY' named entity 'PATHWAY' named entity 'MECHANISM' named entity 'FURIN' named entity 'VARIETY' named entity 'ORDER' named entity 'ENTRY' named entity 'CELL' named entity 'FURIN' named entity 'EXPLOIT' named entity 'TO REGULATE' named entity 'THEIR' named entity 'PROTEIN SECRETION' named entity 'VIRUS' named entity 'VIRUSES' named entity 'CELL' named entity 'PROTEOLYTIC REGULATION' named entity 'WIDE' named entity 'PROPROTEIN CONVERTASES' named entity 'PROPROTEIN CONVERTASES' named entity 'VIRUSES' named entity 'cleavage site' named entity 'endosomal' named entity 'cell tropism' named entity 'proteolytic processing' named entity 'cell entry' named entity 'viruses' named entity 'furin' named entity 'Proteolytic' named entity 'viruses' named entity 'H9N2' named entity 'precursor protein' named entity 'EBOV' named entity 'substrates' named entity 'proteases' named entity 'infectivity' named entity 'infectivity' named entity 'PC4' named entity 'furin' named entity 'hepatitis B virus' named entity 'glycoprotein' named entity 'cell entry' named entity 'larynx' named entity 'glycoprotein' named entity 'amino acid sequence' named entity 'hepadnavirus' named entity 'mutation' named entity 'antiviral' named entity 'Clostridium' named entity 'HPV16' named entity 'high-throughput screening' named entity 'bovine' named entity 'proteases' named entity 'proteases' named entity 'HPV' named entity 'proteolytic' named entity 'basal cells' named entity 'HPV16' named entity 'furin' named entity 'tropism' named entity 'infection' named entity 'proteolytic' named entity 'active site' named entity 'trypsin' named entity 'Kexin' named entity 'α1-antitrypsin' named entity 'gp120' named entity 'trimer' named entity 'TMPRSS2' named entity 'H5N1' named entity 'cell lines' named entity 'conformation' named entity 'sialic acid' named entity 'glycoprotein' named entity 'peptide' named entity 'antiviral therapy' named entity 'furin' named entity 'TGN' named entity 'proteases' named entity 'furin'

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