About: Arms Race between Enveloped Viruses and the Host ERAD Machinery

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Arms Race between Enveloped Viruses and the Host ERAD Machinery
Creator	Zheng, Yong-Hui Frabutt, Dylan
Source	Medline; PMC
abstract	Enveloped viruses represent a significant category of pathogens that cause serious diseases in animals. These viruses express envelope glycoproteins that are singularly important during the infection of host cells by mediating fusion between the viral envelope and host cell membranes. Despite low homology at protein levels, three classes of viral fusion proteins have, as of yet, been identified based on structural similarities. Their incorporation into viral particles is dependent upon their proper sub-cellular localization after being expressed and folded properly in the endoplasmic reticulum (ER). However, viral protein expression can cause stress in the ER, and host cells respond to alleviate the ER stress in the form of the unfolded protein response (UPR); the effects of which have been observed to potentiate or inhibit viral infection. One important arm of UPR is to elevate the capacity of the ER-associated protein degradation (ERAD) pathway, which is comprised of host quality control machinery that ensures proper protein folding. In this review, we provide relevant details regarding viral envelope glycoproteins, UPR, ERAD, and their interactions in host cells.
has issue date	2016-09-19(xsd:dateTime)
bibo:doi	10.3390/v8090255
bibo:pmid	27657106
has license	cc-by
sha1sum (hex)	8befe1b5905e502b127ae478f3b9de1d6e25e317
schema:url	https://doi.org/10.3390/v8090255
resource representing a document's title	Arms Race between Enveloped Viruses and the Host ERAD Machinery
has PubMed Central identifier	PMC5035969
has PubMed identifier	27657106
schema:publication	Viruses
resource representing a document's body	covid:8befe1b5905e502b127ae478f3b9de1d6e25e317#body_text
is schema:about of	named entity 'endoplasmic reticulum' named entity 'viral envelope' named entity 'stress' named entity 'cells' named entity 'pathogens' named entity 'cell membranes' covid:arg/8befe1b5905e502b127ae478f3b9de1d6e25e317 named entity 'host' named entity 'proteasome' named entity 'N-glycans' named entity 'viral envelope' named entity 'protein structure' named entity 'UPR' named entity 'N-linked glycosylation' named entity 'transducin' named entity 'HIV-1' named entity 'transmembrane' named entity 'enzyme' named entity 'HBV' named entity 'quality control' named entity 'UPR' named entity 'ERAD' named entity 'glycoproteins' named entity 'UPR' named entity 'sub-cellular localization' named entity 'quality control' named entity 'infection' named entity 'viral protein' named entity 'UPR' named entity 'protein degradation' named entity 'Enveloped Viruses' named entity 'ERAD' named entity 'CNX' named entity 'IRE1' named entity 'ERAD' named entity 'cytosol' named entity 'Env' named entity 'Japan' named entity 'encephalitis' named entity 'LC3-I' named entity 'threonine' named entity 'viral proteins' named entity 'SCF' named entity 'THBD' named entity 'virus infections' named entity 'Derlin-1' named entity 'C-terminal region' named entity 'binding protein' named entity 'nuclei' named entity 'glycosylation' named entity 'outer membrane protein' named entity 'oligosaccharide' named entity 'glycoside hydrolase' named entity 'HCV' named entity 'N-glycan' named entity 'mannosidases' named entity 'UPR' named entity 'gene' named entity 'CD4' named entity 'virions' named entity 'chronic liver' named entity 'HIV-1' named entity 'homology domain' named entity 'ERAD' named entity 'osteosarcoma' named entity 'Env' named entity 'oligosaccharide' named entity 'E330' named entity 'thrombomodulin' named entity 'lectins' named entity 'ortholog' named entity 'transcription factor' named entity 'glycoprotein' named entity 'substrates' named entity 'glycans' named entity 'mPTP' named entity 'dolichol' named entity 'apoptosis' named entity 'transactivated' named entity 'Golgi complex'

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