A Brief Introduction to the Eukaryotic Cell Stress Proteins

  • Brian Henderson
Part of the Heat Shock Proteins book series (HESP, volume 7)


The discovery of the heat shock response in Drosophila in the early 1960s led on to the elucidation of the cell stress response and the discovery of proteins of molecular mass of 10, 20, 40, 60, 70 and 90 kDa, amongst others, and which were termed the heat shock proteins. Beginning in the late 1970s, and continuing up to the present day, has been the identification of these heat shock/cell stress proteins and their mechanism of action, both as protein-folding proteins and as proteins with a range of other functions in various compartments of the cell and in the intercellular space. In addition to functioning as molecular chaperones, the heat shock/cell stress proteins can also function as cell surface receptors and as intercellular signalling molecules. This growing diversity of the biological functions of the cell stress proteins reveals that these proteins play roles in all aspects of cellular physiology and that these functions also contribute to whole body homeostatic control and to the dark side of human pathophysiology.


Heat Shock Unfold Protein Response Molecular Chaperone Cell Stress Heat Shock Response 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Springer Science+Business Media Dordrecht 2013

Authors and Affiliations

  1. 1.Division of Microbial Diseases, UCL-Eastman Dental InstituteUniversity College LondonLondonUK

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