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DnaK

Zhu, X., et al. Structural analysis of substrate binding by the molecular chaperone DnaK. Science 272 1606-1614, 1996. [Pg.120]

Clarke, C.F., Cheng, K., Frey, A.B., Stein, R., Hinds, P.W.. Levine, A.J. (1988). Purification of complexes of nuclear oncogene p53 with rat and E. coli heat shock protein In vitro dissociation of hsc70 and dnaK from murine p53 by ATP. Mol. Cell. Biol. 8, 1206-1215. [Pg.452]

Gamer, J., Bujard, H., Bukua, B. (1992). Physical interaction between heat shock proteins DnaK, DnaJ, CJtpE the bacterial heat shock transcription factor sigma 32. Cell 69, 833-842. [Pg.453]

Langer, T., Lu., C, Echols, H., Flanagan, J, Hayer, M.K., Hartl, F.-U. (1992). Successive action of Dnak, DnaJ, GroEL along the pathway of chaperone mediated protein folding. Nature 356, 683-689. [Pg.456]

It is generally believed that energy-independent chaperones are unable to allow refolding of non-native proteins. They bind to hydrophobic surfaces of denatured proteins to prevent aggregation and pass them to energy-dependent chaperones such as the DnaK or the GroE chaperone machines. [Pg.10]

Zhang, J., and Walker, G.C. (1996) Identification of elements of the peptide binding site of dnaK by peptide cross-linking./. Biol. Chem. 271, 19668. [Pg.1132]

Gautschi M, Lilie H, Ftinfschilling U, Mun A, Ross S, Lithgow T, Riicknagel P, Rospert S (2001) RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Sszlp and zuotin. Proc Natl Acad Sci USA 98 3762-3767... [Pg.24]

DnaK/Hsp70 MLSSVARSTSSLFSRG()FAAG our unpublished data Bui et al. (1996) Germot et al. (1996) ... [Pg.37]

DnaK/Hsp70 Giardia intestinalis MFLSTLAKKSTTFGVSNVVKNALSSKVMRTTPRMFQRF ESSK van der Giezen et al. (2003)... [Pg.38]

E. cuniculi and N. ovalis (Katinka et al. 2001 Boxma et al. 2005 Carlton et al. 2007). All the components of the DnaK-type machinery have been localized... [Pg.58]

Falah M, Gupta RS (1994) Cloning of the hsp70 (dnaK) genes from Rhizobium meliloti and Pseudomonas cepacia phylogenetic analyses of mitochondrial origin based on a highly conserved protein sequence. J Bacteriol 176 7748-7753 Ferro M et al. (2003) Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana. Mol Cell Proteomics 2 325-345... [Pg.65]


See other pages where DnaK is mentioned: [Pg.100]    [Pg.436]    [Pg.444]    [Pg.6]    [Pg.6]    [Pg.6]    [Pg.7]    [Pg.7]    [Pg.8]    [Pg.13]    [Pg.14]    [Pg.14]    [Pg.14]    [Pg.15]    [Pg.18]    [Pg.19]    [Pg.19]    [Pg.20]    [Pg.21]    [Pg.22]    [Pg.22]    [Pg.23]    [Pg.25]    [Pg.326]    [Pg.409]    [Pg.305]    [Pg.187]    [Pg.52]    [Pg.157]    [Pg.19]    [Pg.95]    [Pg.39]    [Pg.53]    [Pg.54]    [Pg.54]    [Pg.58]    [Pg.58]   
See also in sourсe #XX -- [ Pg.182 , Pg.187 , Pg.188 , Pg.189 , Pg.190 , Pg.191 , Pg.192 , Pg.193 , Pg.194 ]




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Chaperones DnaK/DnaJ

DnaK protein

DnaK protein model

DnaK protein vitro

DnaK, Hsp70-protein complexes

Escherichia coli dnaK protein

Molecular chaperones DnaK/DnaJ

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