About: Can’t RIDD off viruses

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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	Can’t RIDD off viruses
Creator	Bhattacharyya, Sankar Shuda, Masa
Source	PMC
abstract	The mammalian genome has evolved to encode a battery of mechanisms, to mitigate a progression in the life cycle of an invasive viral pathogen. Although apparently disadvantaged by their dependence on the host biosynthetic processes, an immensely faster rate of evolution provides viruses with an edge in this conflict. In this review, I have discussed the potential anti-virus activity of inositol-requiring enzyme 1 (IRE1), a well characterized effector of the cellular homeostatic response to an overloading of the endoplasmic reticulum (ER) protein-folding capacity. IRE1, an ER-membrane-resident ribonuclease (RNase), upon activation catalyses regulated cleavage of select protein-coding and non-coding host RNAs, using an RNase domain which is homologous to that of the known anti-viral effector RNaseL. The latter operates as part of the Oligoadenylate synthetase OAS/RNaseL system of anti-viral defense mechanism. Protein-coding RNA substrates are differentially treated by the IRE1 RNase to either augment, through cytoplasmic splicing of an intron in the Xbp1 transcript, or suppress gene expression. This referred suppression of gene expression is mediated through degradative cleavage of a select cohort of cellular RNA transcripts, initiating the regulated IRE1-dependent decay (RIDD) pathway. The review first discusses the anti-viral mechanism of the OAS/RNaseL system and evasion tactics employed by different viruses. This is followed by a review of the RIDD pathway and its potential effect on the stability of viral RNAs. I conclude with a comparison of the enzymatic activity of the two RNases followed by deliberations on the physiological consequences of their activation.
has issue date	2014-06-18(xsd:dateTime)
bibo:doi	10.3389/fmicb.2014.00292
bibo:pmid	24995003
has license	cc-by
sha1sum (hex)	ef58c6e2790539f30df14acc260ae2af4b5f3d1f
schema:url	https://doi.org/10.3389/fmicb.2014.00292
resource representing a document's title	Can’t RIDD off viruses
has PubMed Central identifier	PMC4061530
has PubMed identifier	24995003
schema:publication	Front Microbiol
resource representing a document's body	covid:ef58c6e2790539f30df14acc260ae2af4b5f3d1f#body_text
is schema:about of	named entity 'INITIATING' named entity 'EMPLOYED' named entity 'COHORT' named entity 'EVOLUTION' named entity 'CLEAVAGE' named entity 'FASTER' named entity 'CHARACTERIZED' named entity 'DISADVANTAGED' named entity 'USING' named entity 'THEIR' named entity 'SYSTEM' named entity 'MECHANISMS' named entity 'RIBONUCLEASE' named entity 'FOLLOWED BY' named entity 'PROTEIN-CODING' named entity 'TREATED' named entity 'IRE1' named entity 'CAPACITY' named entity 'POTENTIAL' named entity 'ACTIVITY' named entity 'MITIGATE' named entity 'EFFECT' named entity 'EITHER' named entity 'VIRUSES' named entity 'RNase' named entity 'enzymatic activity' named entity 'splicing' named entity 'overloading' named entity 'activation' named entity 'RNase' named entity 'Can't' named entity 'REGULATED' named entity 'KNOWN' named entity 'COMPARISON' named entity 'PROGRESSION' named entity 'VIRAL PATHOGEN' named entity 'SYNTHETASE' named entity 'HAVE' named entity 'AUGMENT' named entity 'MECHANISM' named entity 'DOMAIN' named entity 'VIRUS' named entity 'RATE' named entity 'CATALYSES' named entity 'CODING' named entity 'REVIEW' named entity 'DECAY' named entity 'MEDIATED' named entity 'BIOSYNTHETIC' named entity 'HOST' named entity 'DEPENDENCE ON' named entity 'DIFFERENT' named entity 'PHYSIOLOGICAL' named entity 'APPARENTLY' named entity 'ITS' named entity 'ENZYMATIC ACTIVITY' named entity 'MAMMALIAN' named entity 'CODING RNA' named entity 'EDGE' named entity 'ENDOPLASMIC RETICULUM' named entity 'ACTIVATION' named entity 'CELLULAR' named entity 'OAS' named entity 'SUPPRESS' named entity 'CONFLICT' named entity 'RNASEL' named entity 'CONCLUDE' named entity 'RNA' named entity 'RESPONSE TO' named entity 'XBP1' named entity 'VIRAL' named entity 'CYTOPLASMIC' named entity 'RESIDENT' named entity 'DEPENDENT' named entity 'PATHWAY' named entity 'VIRUSES' named entity 'PROCESSES' named entity 'EVOLVED' named entity 'HOMOLOGOUS' named entity 'GENE EXPRESSION'

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