Heat shock protein 40 (Hsp40) plays a key role in the virus life cycle

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Knox, Caroline, Luke, Garry, Blatch, Gregory ORCID: 0000-0003-0778-8577 and Pesce, Eve-Rachele (2011) Heat shock protein 40 (Hsp40) plays a key role in the virus life cycle. Virus Research, 160 (1-2). pp. 15-24. ISSN 0168-1702

Abstract

The heat shock proteins (Hsps) are a diverse subset of molecular chaperones that generally promote the proper folding of proteins after translation and also prevent their aggregation during cellular stress. Paradoxically, cellular chaperones might perform important antiviral functions for host cells, yet, at the same time, might be beneficial for virus replication. Among them, Hsp40 is a specialized co-chaperone that has recently received much attention for its crucial role in both constitutive cellular functions and virus pathogenicity. The aim of this review is to raise awareness of its importance in the life cycles of a wide range of viruses.

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Item type	Article
URI	https://vuir.vu.edu.au/id/eprint/8881
DOI	10.1016/j.virusres.2011.06.013
Official URL	http://www.sciencedirect.com/science/article/pii/S...
Subjects	Historical > Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences Historical > FOR Classification > 1108 Medical Microbiology Historical > SEO Classification > 970111 Expanding Knowledge in the Medical and Health Sciences
Keywords	ResPubID22937, J-proteins, Hsp40, chaperone, heat shock
Citations in Scopus	35 - View on Scopus
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