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Hsp70 molecular chaperone system

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). [Pg.292]

Hsp70 proteins with their co-chaperones and cooperating chaperones thus constitute a complex network of folding machines. This chapter describes the molecular basis of this network. Particular emphasis is given to the DnaK system of Escherichia coli as it is the best understood Hsp70 system, and to the mechanistic differences between Hsp70 family members. [Pg.2]


See other pages where Hsp70 molecular chaperone system is mentioned: [Pg.505]    [Pg.494]    [Pg.349]    [Pg.215]    [Pg.28]    [Pg.349]    [Pg.2057]    [Pg.482]    [Pg.395]    [Pg.1305]    [Pg.283]    [Pg.286]    [Pg.354]    [Pg.354]    [Pg.594]    [Pg.160]    [Pg.227]    [Pg.495]    [Pg.132]    [Pg.231]    [Pg.395]    [Pg.16]    [Pg.81]   
See also in sourсe #XX -- [ Pg.494 , Pg.495 ]




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