Heat Shock Proteins; An Overview
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Date
2010
Authors
Journal Title
Journal ISSN
Volume Title
Publisher
BENTHAM SCIENCE PUBL LTD
Access Rights
info:eu-repo/semantics/openAccess
Abstract
Heat shock proteins (Hsps) protect protein substrates against conformational damage to promote the function of the proteins, prevent aggregation and prevent formation of toxic inclusion bodies. Protein aggregates and fibrils have been associated with neurodegenerative diseases and with inclusion bodies. High-level expression of recombinant protein for biotechnological purposes often leads to insoluble inclusion bodies. Therefore, misfolded proteins must be properly folded or must be degraded through heat shock protein action. This function protects cells against cytotoxic outcomes. In addition to their cytoprotective roles, Hsps are involved in other functions since Hsps exist in all types of cells and tissues. Therefore, several diseases are associated with alterations of these biochemical functions. This first review of the theme issue will discuss general properties of Hsps concisely along with their potential use in pharmaceutical and biotechnological applications.
Description
Keywords
Heat Shock Protein, Biotechnology, Pharmacology
Journal or Series
Current Pharmaceutical Biotechnology
WoS Q Value
Q1
Scopus Q Value
Q2
Volume
11
Issue
2
Citation
Tutar, L., Tutar, Y., (2010). Heat Shock Proteins; An Overview. Current Pharmaceutical Biotechnology, 11(2), 216-222.
DOI: 10.2174/138920110790909632
