Chaperones heat-shock proteins

Dutta D et al (2009) The molecular chaperone heat shock protein-90 positively regulates rotavims infectionx. Virology 391(2) 325—333... 

Gorre ME, Ellwood-Yen K, Chiosis G et al. (2002) BCR-ABL point mutants isolated from patients with imatinib mesylate-resistant chronic myeloid leukemia remain sensitive to inhibitors of the BCR-ABL chaperone heat shock protein 90. Blood 100 3041-3044... 

Molecular chaperone (relative molecular mass 78 K) found in the lumen of the ER. BiP is related to the Hsp70 family of heat-shock proteins and was originally described as immunoglobulin heavy chain binding protein. 

Molecular chaperones, stress proteins (note not all stress proteins are molecular chaperones and not all molecular chaperones are stress proteins) Heat shock proteins (Hsp) Polypeptide chain binding proteins... 

Hsp70 is a molecular chaperone (relative molecular mass 70 kD) found in different compartments of eucaryotic cells. Hsp70 was originally described as heat shock protein 70. 

Welch, W.J. (1991). The role of heat shock proteins as molecular chaperones Curr. Opin. Cell Biol. 3, 1033-1038. 

Most medical students look askance at thermobiology. We think this is a mistake hence, we have included a section dealing with this subject. This brings us to the chapter on the heat shock response which at the very outset makes clear that many stressors besides heat are known to result in heat shock gene expression. Many of the heat shock proteins occur in unstressed cells and some of them behave as chaperones. These proteins also reach high levels in a wide range of diseases... 

Both the heat and cold shock response are universal and have been studied extensively. The major heat shock proteins (HSPs) are highly conserved. They are involved in the homeostatic adaptation of cells to harsh environmental conditions. Some act as molecular chaperones for protein folding, while others are involved in the processing of denatured polypeptides whose accumulation would be deleterious. The cold shock results in the transient induction of cold shock proteins (CSPs), which include a family of small acidic proteins carrying the cold shock domain. The CSPs appear to be involved in various cellular functions such as transcription, translation and DNA recombination. 

Chow, A. M. Brown, I. R. Induction of heat shock proteins in differentiated human and rodent neurons by celastrol. Cell Stress Chaperones 2007, 12, 237-244. 

Folding chaperons Prefolding as in eukaryotes Different heat shock proteins (chaperones)... 

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