About: Pleiotropic roles of the ubiquitin-proteasome system during viral propagation

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About: Pleiotropic roles of the ubiquitin-proteasome system during viral propagation 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	Pleiotropic roles of the ubiquitin-proteasome system during viral propagation
Creator	Wu, Peng Tang, Qi Chen, Huiqing Li, Guohui
Source	Elsevier; Medline; PMC
abstract	Abstract Protein ubiquitination is a highly conserved post-translational modification affecting various biological processes including viral propagation. Ubiquitination has multiple effects on viral propagation, including viral genome uncoating, viral replication, and immune evasion. Ubiquitination of viral proteins is triggered by the ubiquitin-proteasome system (UPS). This involves the covalent attachment of the highly conserved 76 amino acid residue ubiquitin protein to target proteins by the consecutive actions of E1, E2 and E3 enzymes, and the 26S proteasome that together form a multiprotein complex that degrades target proteins. The UPS is the primary cytosolic proteolytic machinery for the selective degradation of various forms of proteins including viral proteins, thereby limiting viral growth in host cells. To combat this host anti-viral machinery, viruses have evolved the ability to employ or subvert the UPS to inactivate or degrade cellular proteins to favour viral propagation. This review highlights our current knowledge on the different roles of the UPS during viral propagation.
has issue date	2018-08-15(xsd:dateTime)
bibo:doi	10.1016/j.lfs.2018.06.014
bibo:pmid	29913185
has license	els-covid
sha1sum (hex)	95d699a680efeea93de467496b23eed470998d95
schema:url	https://doi.org/10.1016/j.lfs.2018.06.014
resource representing a document's title	Pleiotropic roles of the ubiquitin-proteasome system during viral propagation
has PubMed Central identifier	PMC7094228
has PubMed identifier	29913185
schema:publication	Life Sciences
resource representing a document's body	covid:95d699a680efeea93de467496b23eed470998d95#body_text
is schema:about of	named entity 'amino acid' named entity 'enzymes' named entity 'combat' named entity 'IMMUNE EVASION' named entity 'AMINO ACID RESIDUE' named entity 'UBIQUITINATION' named entity 'EFFECTS' named entity 'TARGET' named entity 'EVOLVED' named entity 'KNOWLEDGE' named entity 'LIMITING' named entity 'POST-TRANSLATIONAL MODIFICATION' named entity 'VARIOUS' named entity 'COMBAT' named entity 'DEGRADATION' named entity 'UPS' named entity 'MULTIPLE' named entity 'VIRAL' named entity 'UBIQUITIN-PROTEASOME SYSTEM' named entity 'TRIGGERED BY' named entity 'HOST CELLS' named entity 'CONSECUTIVE' named entity 'ROLES' named entity 'COVALENT ATTACHMENT' named entity 'BIOLOGICAL PROCESSES' named entity 'PROTEINS' named entity 'SELECTIVE' named entity 'FORM' named entity 'VIRAL GENOME' named entity 'VIRAL PROTEINS' named entity 'OUR' named entity 'CELLULAR' named entity 'FORMS' named entity 'PRIMARY' named entity 'CURRENT' named entity 'MULTIPROTEIN COMPLEX' named entity 'PROPAGATION' named entity 'VIRAL' named entity 'VIRUSES' named entity 'INCLUDING' named entity 'CONSERVED' named entity 'ACTIONS' named entity 'ENZYMES' named entity 'UNCOATING' named entity 'UBIQUITIN PROTEIN' named entity 'PROTEIN ' named entity 'AFFECTING' named entity 'HIGHLY' named entity 'EMPLOY' named entity 'GROWTH' named entity 'PROTEOLYTIC' named entity 'IS A' named entity '26S PROTEASOME' named entity 'HOST' named entity 'PROPAGATION' named entity 'UBIQUITIN-PROTEASOME SYSTEM' named entity 'PROTEIN UBIQUITINATION' named entity 'VIRAL REPLICATION' named entity 'REVIEW' named entity 'MACHINERY' named entity 'CYTOSOLIC' named entity 'ROLES' named entity 'HAVE' named entity 'DIFFERENT' named entity 'host' named entity 'protein' named entity 'subvert' named entity 'degrades' named entity 'Protein' named entity 'host' named entity 'primary' named entity 'biological processes' named entity 'target' named entity 'proteins' named entity 'viruses' named entity '26S proteasome' named entity 'amino acid residue' named entity 'UPS'

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