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2000
Volume 9, Issue 7
  • ISSN: 1566-5240
  • E-ISSN: 1875-5666

Abstract

The heat shock protein (HSP) family has long been associated with a generalized cellular stress response, particularly in terms of recognizing and chaperoning misfolded proteins. While HSPs in general appear to be protective, HSP27 has recently emerged as a particularly potent neuroprotectant in a number of diverse neurological disorders, ranging from ALS to stroke. Although its robust protective effect on a number of insults has been recognized, the mechanisms and regulation of HSP27's protective actions are still undergoing intense investigation. On the basis of recent studies, HSP27 appears to have a dynamic and diverse range of function in cellular survival. This review provides a forum to compare and contrast recent literature exploring the protective mechanism and regulation of HSP27, focusing on neurological disorders in particular, as they represent a range from protein aggregate-associated diseases to acute stress.

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/content/journals/cmm/10.2174/156652409789105561
2009-09-01
2025-09-07
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/content/journals/cmm/10.2174/156652409789105561
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  • Article Type:
    Research Article
Keyword(s): aggregates; chaperones; heat shock proteins; HSP27; injury; ischemia
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