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The role of HSP70 and its co-chaperones in protein misfolding, aggregation and disease

Duncan, EJ; Cheetham, ME; Chapple, JP; van der Spuy, J; (2015) The role of HSP70 and its co-chaperones in protein misfolding, aggregation and disease. Subcellular Biochemistry , 78 pp. 243-273. 10.1007/978-3-319-11731-7_12.

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Abstract

Molecular chaperones and their associated co-chaperones are essential in health and disease as they are key facilitators of protein folding, quality control and function. In particular, the HSP70 molecular chaperone networks have been associated with neurodegenerative diseases caused by aberrant protein folding. The pathogenesis of these disorders usually includes the formation of deposits of misfolded, aggregated protein. HSP70 and its co-chaperones have been recognised as potent modulators of inclusion formation and cell survival in cellular and animal models of neurodegenerative disease. In has become evident that the HSP70 chaperone machine functions not only in folding, but also in proteasome mediated degradation of neurodegenerative disease proteins. Thus, there has been a great deal of interest in the potential manipulation of molecular chaperones as a therapeutic approach for many neurodegenerations. Furthermore, mutations in several HSP70 co-chaperones and putative co-chaperones have been identified as causing inherited neurodegenerative and cardiac disorders, directly linking the HSP70 chaperone system to human disease.

Type: Article
Title: The role of HSP70 and its co-chaperones in protein misfolding, aggregation and disease
Location: United States
DOI: 10.1007/978-3-319-11731-7_12
Publisher version: http://dx.doi.org/10.1007/978-3-319-11731-7_12
Language: English
Additional information: This version is the author accepted manuscript. For information on re-use, please refer to the publisher’s terms and conditions.
Keywords: Animals, Genetic Predisposition to Disease, HSP70 Heat-Shock Proteins, Humans, Neurodegenerative Diseases, Phenotype, Protein Aggregates, Protein Aggregation, Pathological, Protein Conformation, Protein Folding, Proteostasis Deficiencies, Signal Transduction
UCL classification: UCL
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences > Institute of Ophthalmology
URI: https://discovery.ucl.ac.uk/id/eprint/1494115
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