About: Synthesis, proteolytic processing and complex formation of N-terminally nested precursor proteins of the Rift Valley fever virus glycoproteins

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

About: Synthesis, proteolytic processing and complex formation of N-terminally nested precursor proteins of the Rift Valley fever virus glycoproteins 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	Synthesis, proteolytic processing and complex formation of N-terminally nested precursor proteins of the Rift Valley fever virus glycoproteins
Creator	Nichol, Stuart Gerrard, Sonja
Source	Elsevier; Medline; PMC
abstract	Abstract The genomic M RNA segment of Rift Valley fever virus is transcribed to produce a single mRNA with multiple translation initiation sites. The products of translation are an N-terminal nested series of polyproteins. These polyproteins enter the secretory system of the host cell and are proteolytically processed to yield the mature virion glycoproteins, Gn and Gc, and two non-structural glycoproteins. By means of pulse-chase immune precipitation experiments we identify the Gn and Gc precursor molecules and also show that signal peptidase cleavage is required for mature Gn and Gc production. We also demonstrate that a hydrophobic domain at the N-terminus of Gn acts as a signal peptide only in the context of the polyprotein precursors that initiate at the second, fourth or fifth AUGs. In addition, we document that formation of Gn/Gc heteromeric complexes occur rapidly (<5 min) and can occur prior to signal peptidase processing of Gn, suggesting that this complex forms in the endoplasmic reticulum. Interestingly, Gc can form a complex with a glycoprotein that has been considered nonstructural, a discovery that has implications for both the topology and potential packaging of this glycoprotein.
has issue date	2007-01-20(xsd:dateTime)
bibo:doi	10.1016/j.virol.2006.08.002
bibo:pmid	16963099
has license	els-covid
sha1sum (hex)	6b82beaa3301bef2fdd29e5abe1c690c2611be7e
schema:url	https://doi.org/10.1016/j.virol.2006.08.002
resource representing a document's title	Synthesis, proteolytic processing and complex formation of N-terminally nested precursor proteins of the Rift Valley fever virus glycoproteins
has PubMed Central identifier	PMC7172627
has PubMed identifier	16963099
schema:publication	Virology
resource representing a document's body	covid:6b82beaa3301bef2fdd29e5abe1c690c2611be7e#body_text
is schema:about of	named entity 'virion' named entity 'precipitation' named entity 'min' named entity 'translation' named entity 'precursor proteins' named entity 'ADDITION' named entity 'FORMATION' named entity 'SECOND' named entity 'NESTED' named entity 'multiple' named entity 'demonstrate' named entity 'hydrophobic' named entity 'mature' named entity 'complex' named entity 'products' named entity 'discovery' named entity 'polyproteins' named entity 'production' named entity 'precursor molecules' named entity 'virion' named entity 'polyprotein' named entity 'cleavage' named entity 'AUGs' named entity 'topology' named entity 'complex formation' named entity 'Rift Valley fever virus' named entity 'glycoproteins' named entity 'signal peptidase' named entity 'precursor proteins' named entity 'proteolytically processed' named entity 'signal peptidase' named entity 'hydrophobic' named entity 'precursor molecules' named entity 'genomic' named entity 'initiation' named entity 'N-terminally' named entity 'VIRION' named entity 'MIN' named entity 'IMMUNE PRECIPITATION' named entity 'RAPIDLY' named entity 'INITIATE' named entity 'CLEAVAGE' named entity 'TO PRODUCE' named entity 'COMPLEX' named entity 'NESTED' named entity 'SYNTHESIS' named entity 'RIFT VALLEY FEVER VIRUS' named entity 'PROTEOLYTIC PROCESSING' named entity 'host cell' named entity 'Elsevier Inc.' named entity 'signal peptide' named entity 'glycoprotein' named entity 'proteolytic processing' named entity 'translation initiation' named entity 'Rift Valley fever virus' named entity 'PRIOR TO' named entity 'YIELD' named entity 'MOLECULES' named entity 'RIFT VALLEY FEVER VIRUS' named entity 'DOMAIN' named entity 'NON-' named entity 'N-TERMINUS' named entity 'TO SIGNAL' named entity 'THESE' named entity 'PACKAGING' named entity 'PRECURSOR' named entity 'DISCOVERY' named entity 'SITES' named entity 'N-terminus' named entity 'IDENTIFY' named entity 'PROCESSED' named entity 'STRUCTURAL' named entity 'N-TERMINAL ' named entity 'HYDROPHOBIC' named entity 'OCCUR' named entity 'MULTIPLE' named entity 'EXPERIMENTS' named entity 'PROTEINS' named entity 'precipitation' named entity 'N-terminal'

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 © 2009-2024 OpenLink Software