Hsp90 Chaperones Bluetongue Virus Proteins and Prevents Proteasomal Degradation.


Journal

Journal of virology
ISSN: 1098-5514
Titre abrégé: J Virol
Pays: United States
ID NLM: 0113724

Informations de publication

Date de publication:
15 10 2019
Historique:
received: 29 05 2019
accepted: 19 07 2019
pubmed: 4 8 2019
medline: 9 6 2020
entrez: 4 8 2019
Statut: epublish

Résumé

The molecular chaperone machinery is important for the maintenance of protein homeostasis within the cells. The principle activities of the chaperone machinery are to facilitate protein folding and organize conformationally dynamic client proteins. Prominent among the members of the chaperone family are heat shock protein 70 (Hsp70) and 90 (Hsp90). Like cellular proteins, viral proteins depend upon molecular chaperones to mediate their stabilization and folding. Bluetongue virus (BTV), which is a model system for the

Identifiants

pubmed: 31375577
pii: JVI.00898-19
doi: 10.1128/JVI.00898-19
pmc: PMC6798104
pii:
doi:

Substances chimiques

HSP90 Heat-Shock Proteins 0
Molecular Chaperones 0
RNA, Small Interfering 0
Viral Proteins 0
Proteasome Endopeptidase Complex EC 3.4.25.1

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 100218/Z/12/Z
Pays : United Kingdom

Informations de copyright

Copyright © 2019 Mohl and Roy.

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Auteurs

Bjorn-Patrick Mohl (BP)

Department of Pathogen Molecular Biology, Faculty of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, London, United Kingdom.

Polly Roy (P)

Department of Pathogen Molecular Biology, Faculty of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, London, United Kingdom polly.roy@lshtm.ac.uk.

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Classifications MeSH