About: Resources to Discover and Use Short Linear Motifs in Viral Proteins

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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
title	Resources to Discover and Use Short Linear Motifs in Viral Proteins
Creator	Generous, Nicholas Fair, Jeanne Davis-Anderson, Katie Hraber, Peter Mcmahon, Benjamin O'maille, Paul Silberfarb, Andrew
source	Elsevier; Medline; PMC
abstract	Viral proteins evade host immune function by molecular mimicry, often achieved by short linear motifs (SLiMs) of three to ten consecutive amino acids (AAs). Motif mimicry tolerates mutations, evolves quickly to modify interactions with the host, and enables modular interactions with protein complexes. Host cells cannot easily coordinate changes to conserved motif recognition and binding interfaces under selective pressure to maintain critical signaling pathways. SLiMs offer potential for use in synthetic biology, such as better immunogens and therapies, but may also present biosecurity challenges. We survey viral uses of SLiMs to mimic host proteins, and information resources available for motif discovery. As the number of examples continues to grow, knowledge management tools are essential to help organize and compare new findings.
has issue date	2020-01-31(xsd:dateTime)
bibo:doi	10.1016/j.tibtech.2019.07.004
bibo:pmid	31427097
has license	els-covid
sha1sum (hex)	d1ff5b3f3f46093b23efa3c3f1f89dc39fd47720
schema:url	https://doi.org/10.1016/j.tibtech.2019.07.004
resource representing a document's title	Resources to Discover and Use Short Linear Motifs in Viral Proteins
has PubMed Central identifier	PMC7114124
has PubMed identifier	31427097
schema:publication	Trends in Biotechnology
resource representing a document's body	covid:d1ff5b3f3f46093b23efa3c3f1f89dc39fd47720#body_text
is schema:about of	named entity 'biology' named entity 'mimicry' named entity 'continues' named entity 'host' named entity 'compare' named entity 'viral' covid:arg/d1ff5b3f3f46093b23efa3c3f1f89dc39fd47720 named entity 'motif' named entity 'tools' named entity 'critical' named entity 'conserved' named entity 'SLiMs' named entity 'SLiMs' named entity 'type I interferon' named entity 'evolution' named entity 'SLiM' named entity 'Beclin-1' named entity 'host' named entity 'proteins' named entity 'mutations' named entity 'organize' named entity 'Host' named entity 'molecular mimicry' named entity 'Viral' named entity 'signaling pathways' named entity 'amino acids' named entity 'motif discovery' named entity 'biosecurity' named entity 'protein complexes' named entity 'binding' named entity 'eIF2a' named entity 'isoforms' named entity 'O-linked' named entity 'binding domain' named entity 'regular expressions' named entity 'cellular trafficking' named entity 'transcription' named entity 'ICP34.5' named entity 'orthologs' named entity 'genomics' named entity 'pathogen' named entity 'Viruses' named entity 'targeted drug delivery' named entity 'gene products' named entity 'virus' named entity 'motif' named entity 'proteome' named entity 'interact' named entity 'Glycosylation' named entity 'motif' named entity 'SLiM' named entity 'protein-protein interaction' named entity 'synthetic biology' named entity 'MEME' named entity 'virus' named entity 'HSV-2' named entity 'Enzyme' named entity 'virion' named entity 'false negatives' named entity 'glycosylated' named entity 'immune recognition' named entity 'primary sequence' named entity 'protein structure' named entity 'nitrogen' named entity 'evolution' named entity 'immunogens' named entity 'influenza' named entity 'AAs' named entity 'motif' named entity 'antigen' named entity 'motif discovery' named entity 'macromolecular' named entity 'HSV-1' named entity 'virulence factor' named entity 'interact with other proteins'

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