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Different combinations of the heat-shock cognate protein 70 (hsc70) C-terminal functional groups are utilized to interact with distinct tetratricopeptide repeat-containing proteins.
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The amino-terminal transforming region of simian virus 40 large T and small t antigens functions as a J domain.
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The cysteine string secretory vesicle protein activates Hsc70 ATPase.
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Involvement of the 10-kDa C-terminal fragment of hsc70 in complexing with unfolded protein.
Arch Biochem Biophys. 1996 Aug 1;332(1):163-9. doi: 10.1006/abbi.1996.0328.
4
NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone.
J Mol Biol. 1996 Jul 12;260(2):236-50. doi: 10.1006/jmbi.1996.0395.
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Identification of elements of the peptide binding site of DnaK by peptide cross-linking.
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Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog, Hsp40.
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Structure-function analysis of the zinc finger region of the DnaJ molecular chaperone.
J Biol Chem. 1996 Jun 21;271(25):14840-8. doi: 10.1074/jbc.271.25.14840.
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Structural analysis of substrate binding by the molecular chaperone DnaK.
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A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates.
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Rat kidney glutathione S-transferase 1 subunits have C-terminal truncations.
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