- Title
- Hsp40 Co-chaperones as drug targets: towards the development of specific inhibitors
- Creator
- Pesce, Eva-Rachele, Blatch, Gregory L, Edkins, Adrienne L
- Date
- 2016
- Type
- text
- Type
- article
- Identifier
- http://hdl.handle.net/10962/66335
- Identifier
- vital:28937
- Identifier
- https://doi.org/10.1007/7355_2015_92
- Description
- publisher version
- Description
- The heat shock protein 40 (Hsp40/DNAJ) family of co-chaperones modulates the activity of the major molecular chaperone heat shock protein 70 (Hsp70) protein group. Hsp40 stimulates the basal ATPase activity of Hsp70 and hence regulates the affinity of Hsp70 for substrate proteins. The number of Hsp40 genes in most organisms is substantially greater than the number of Hsp70 genes. Therefore, different Hsp40 family members may regulate different activities of the same Hsp70. This fact, along with increasing knowledge of the function of Hsp40 in diseases, has led to certain Hsp40 isoforms being considered promising drug targets. Here we review the role of Hsp40 in human disease and recent developments towards the creation of Hsp40-specific inhibitors.
- Format
- Publisher
- Springer International Publishing Switzerland
- Language
- English
- Relation
- Topics in Medicinal Chemistry, Pesce, E-R., Blatch G.L., Edkins A.L. (2015) Hsp40 Co-chaperones as Drug Targets: Towards the Development of Specific Inhibitors. In: McAlpine S., Edkins A. (eds) Heat Shock Protein Inhibitors. Topics in Medicinal Chemistry, vol 19. Springer, Cham, Topics in Medicinal Chemistry volume 19 number 163 195 2015 978-3-319-32607-8
- Rights
- Springer International Publishing Switzerland
- Rights
- Use of this resource is governed by the terms and conditions of the National Library of South Africa Copyright Act (http://www.nlsa.ac.za/downloads/Copyright Act.pdf)
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Edkins, Adrienne Lesley (Associate Prof)
RU Department of Biochemistry, Microbiology and Bioinformatics
SDG 03. Good Health and Well-Being
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