Hsp70 molecular chaperone

Brodsky JL, Chiosis G (2006) Hsp70 molecular chaperones emerging roles in human disease and identification of small molecule modulators. Curr Top Med Chem 6 1215-1225... 

In conclusion, the biochemical properties of the APIase function of hsp70 molecular chaperones allow kinetic proofreading of folding by rapid scanning of APIase-sensitive sites of unfolded polypeptide chains. 

Meimaridou, E., Gooljar, S.B., and Chappie, J.P. 2009. From hatching to dispatching the multiple cellular roles of the Hsp70 molecular chaperone machinery. Journal of Molecular Endocrinology, 42 1-9. doi 10.1677/JME-08-0116. 

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. 

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. 

Other proteins also participate in the integration process. One class is composed of molecular chaperones such as SecA in bacteria and Hsp70 or BiP in eukaryotes (Qi and Bernstein, 1999 Schekman, 1994 Mothes et al., 1997 Hamman et al., 1998 Pilon and Schekman, 1999). Another important player in the eukaryotic system is TRAM (translocating chain-associating membrane protein) (Walter, 1992). 

Ludees, J., Demand, J., and Hoheeld, J. The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome. J. Biol. Chem. 2000, 275, 4613-4617. 

Bajj3 Regulate Hsp70 family molecular chaperones KO Myofibrillar myopathy... 

These apoprotein-specific molecular chaperones target only their particular apoprotein partners, but otherwise resemble in function the well-studied molecular chaperones such as GroEL, Hsp70, and Hsp40 that bind to and prevent misfolding or stimulate refolding of a wide range of proteins. ... 

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