About: Chapter Three The Nonstructural Proteins Directing Coronavirus RNA Synthesis and Processing

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

About: Chapter Three The Nonstructural Proteins Directing Coronavirus RNA Synthesis and Processing 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
has title	Chapter Three The Nonstructural Proteins Directing Coronavirus RNA Synthesis and Processing
Creator	Ziebuhr, J Decroly, E Snijder, E
Source	Elsevier; Medline; PMC
abstract	Abstract Coronaviruses are animal and human pathogens that can cause lethal zoonotic infections like SARS and MERS. They have polycistronic plus-stranded RNA genomes and belong to the order Nidovirales, a diverse group of viruses for which common ancestry was inferred from the common principles underlying their genome organization and expression, and from the conservation of an array of core replicase domains, including key RNA-synthesizing enzymes. Coronavirus genomes (~26–32 kilobases) are the largest RNA genomes known to date and their expansion was likely enabled by acquiring enzyme functions that counter the commonly high error frequency of viral RNA polymerases. The primary functions that direct coronavirus RNA synthesis and processing reside in nonstructural protein (nsp) 7 to nsp16, which are cleavage products of two large replicase polyproteins translated from the coronavirus genome. Significant progress has now been made regarding their structural and functional characterization, stimulated by technical advances like improved methods for bioinformatics and structural biology, in vitro enzyme characterization, and site-directed mutagenesis of coronavirus genomes. Coronavirus replicase functions include more or less universal activities of plus-stranded RNA viruses, like an RNA polymerase (nsp12) and helicase (nsp13), but also a number of rare or even unique domains involved in mRNA capping (nsp14, nsp16) and fidelity control (nsp14). Several smaller subunits (nsp7–nsp10) act as crucial cofactors of these enzymes and contribute to the emerging “nsp interactome.” Understanding the structure, function, and interactions of the RNA-synthesizing machinery of coronaviruses will be key to rationalizing their evolutionary success and the development of improved control strategies.
has issue date	2016-12-31(xsd:dateTime)
bibo:doi	10.1016/bs.aivir.2016.08.008
bibo:pmid	27712628
has license	els-covid
sha1sum (hex)	2f907204bfc5354c091a17133e85c41e50a0b8d7
schema:url	https://doi.org/10.1016/bs.aivir.2016.08.008
resource representing a document's title	Chapter Three The Nonstructural Proteins Directing Coronavirus RNA Synthesis and Processing
has PubMed Central identifier	PMC7112286
has PubMed identifier	27712628
schema:publication	Advances in Virus Research
resource representing a document's body	covid:2f907204bfc5354c091a17133e85c41e50a0b8d7#body_text
is schema:about of	named entity 'NONSTRUCTURAL PROTEINS' named entity 'RNA SYNTHESIS' named entity 'PROCESSING' named entity 'RNA' named entity 'protein' named entity 'replicase' named entity 'RNA helicases' named entity 'X-ray structure' named entity 'to-3' named entity 'nidoviruses' named entity 'ExoN' named entity 'acidic residues' named entity 'RNA' named entity 'helicase' named entity 'enzyme' named entity 'nidoviruses' named entity 'organelles' named entity 'β-strands' named entity 'nonsense-mediated mRNA decay' named entity 'CoV' named entity 'sequence motif' named entity 'SARS-CoV' named entity 'substrates' named entity 'reaction intermediate' named entity 'ExoN' named entity 'genomes' named entity 'IFIT2' named entity 'conserved residues' named entity 'SARS-CoV' named entity 'RNA' named entity 'MERS-CoV' named entity 'MHV' named entity 'nucleotide' named entity 'single-stranded' named entity 'pathogenesis' named entity 'genomes' named entity 'nidovirus' named entity 'coronavirus' named entity 'nucleotide' named entity 'Mda5' named entity 'nucleotides' named entity 'lethal mutagenesis' named entity 'conserved domain' named entity 'arterivirus' named entity 'reverse genetics' named entity 'RNA' named entity 'nucleotidyl transferase' named entity 'common ancestry' named entity 'nucleotides' named entity 'coding sequence' named entity 'invertebrate' named entity 'amide' named entity 'zinc' named entity 'polyprotein' named entity 'substrates' named entity 'replication cycle' named entity 'helicase' named entity 'Marseille' named entity 'RdRp' named entity 'coding sequence' named entity 'infectious bronchitis virus' named entity 'RNA' named entity 'helicase' named entity 'Protein' named entity 'virus replication' named entity 'subgenomic' named entity 'endonuclease' named entity 'van Vliet' named entity 'nucleotides' named entity 'nucleic acid' named entity 'RNA' named entity 'polyprotein' named entity 'arterivirus' named entity 'acidic residues' named entity 'RNA viruses' named entity 'cryoelectron microscopy' named entity 'mRNA capping' named entity 'nidovirus' named entity 'nucleocapsid'

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