About: Conventional and unconventional mechanisms for capping viral mRNA

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Conventional and unconventional mechanisms for capping viral mRNA Goto Sponge NotDistinct Permalink

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	Conventional and unconventional mechanisms for capping viral mRNA
Creator	Canard, Bruno Decroly, Etienne Ferron, François Lescar, Julien
source	Medline; PMC
abstract	In the eukaryotic cell, capping of mRNA 5′ ends is an essential structural modification that allows efficient mRNA translation, directs pre-mRNA splicing and mRNA export from the nucleus, limits mRNA degradation by cellular 5′–3′ exonucleases and allows recognition of foreign RNAs (including viral transcripts) as 'non-self'. However, viruses have evolved mechanisms to protect their RNA 5′ ends with either a covalently attached peptide or a cap moiety (7-methyl-Gppp, in which p is a phosphate group) that is indistinguishable from cellular mRNA cap structures. Viral RNA caps can be stolen from cellular mRNAs or synthesized using either a host- or virus-encoded capping apparatus, and these capping assemblies exhibit a wide diversity in organization, structure and mechanism. Here, we review the strategies used by viruses of eukaryotic cells to produce functional mRNA 5′-caps and escape innate immunity.
has issue date	2011-12-05(xsd:dateTime)
bibo:doi	10.1038/nrmicro2675
bibo:pmid	22138959
has license	no-cc
sha1sum (hex)	60a37c1bf5a320b0db55a51c2cb4c9b69f9ecff7
schema:url	https://doi.org/10.1038/nrmicro2675
resource representing a document's title	Conventional and unconventional mechanisms for capping viral mRNA
has PubMed Central identifier	PMC7097100
has PubMed identifier	22138959
schema:publication	Nat Rev Microbiol
resource representing a document's body	covid:60a37c1bf5a320b0db55a51c2cb4c9b69f9ecff7#body_text
is schema:about of	named entity 'called' named entity 'degraded' named entity 'capping' named entity 'viral' named entity 'eukaryotic translation initiation factor' named entity 'linked' named entity 'export' named entity 'viral' named entity 'eukaryotic' named entity '7-methylguanosine' named entity 'moiety' named entity 'mRNAs' named entity 'antiviral' named entity 'Pre-mRNA' named entity 'mRNA' named entity 'inorganic phosphate' named entity 'electrostatically' named entity 'poxviruses' named entity 'moiety' named entity 'guanine' named entity 'l-homocysteine' named entity 'murine' named entity 'NSP2' named entity 'FIG' named entity 'Japanese encephalitis virus' named entity 'RNA' named entity 'viral RNAs' named entity 'RNA' named entity 'RNA-dependent RNA polymerase' named entity 'guanosine' named entity 'quaternary' named entity 'VSV' named entity 'cysteine' named entity 'glutamate' named entity 'Orbivirus' named entity 'covalent link' named entity 'inorganic phosphate' named entity 'viruses' named entity 'enzymatic reactions' named entity 'decapping' named entity 'S. cerevisiae' named entity 'FIG' named entity 'phenylalanine' named entity 'KXDG' named entity 'Cysteine' named entity 'RNA' named entity 'hydrophilic' named entity 'FIG' named entity 'hydrolysis' named entity 'oligonucleotides' named entity '7-methylguanosine' named entity 'tetratricopeptide repeats' named entity 'mRNAs' named entity 'ssRNA' named entity 'P-body' named entity 'biosynthetic pathways' named entity 'positive-sense RNA' named entity 'orthomyxoviruses' named entity 'Non-self' named entity 'G3BP' named entity 'MDA5' named entity 'mRNA' named entity 'ping-pong' named entity 'DNA viruses' named entity 'AdoHcy' named entity 'motif' named entity 'cytoplasm' named entity 'IFNβ' named entity 'kinase' named entity 'guanylyltransferase' named entity 'non-self' named entity 'orthoreoviruses' named entity 'consensus sequence' named entity 'genus' named entity 'methylation' named entity 'S. cerevisiae' named entity 'enzyme complex' named entity 'cap-snatching'

Faceted Search & Find service v1.13.91 as of Mar 24 2020

Alternative Linked Data Documents: Sponger | ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3229 as of Jul 10 2020, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (94 GB total memory)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2025 OpenLink Software