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The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171.
Buchberger A, Valencia A, McMacken R, Sander C, Bukau B. Buchberger A, et al. Among authors: bukau b. EMBO J. 1994 Apr 1;13(7):1687-95. EMBO J. 1994. PMID: 7908876 Free PMC article.
Physical interaction between heat shock proteins DnaK, DnaJ, and GrpE and the bacterial heat shock transcription factor sigma 32.
Gamer J, Bujard H, Bukau B. Gamer J, et al. Among authors: bukau b. Cell. 1992 May 29;69(5):833-42. doi: 10.1016/0092-8674(92)90294-m. Cell. 1992. PMID: 1534276
A module of the DnaJ heat shock proteins found in malaria parasites.
Bork P, Sander C, Valencia A, Bukau B. Bork P, et al. Among authors: bukau b. Trends Biochem Sci. 1992 Apr;17(4):129. doi: 10.1016/0968-0004(92)90319-5. Trends Biochem Sci. 1992. PMID: 1585456 No abstract available.
Mutations altering heat shock specific subunit of RNA polymerase suppress major cellular defects of E. coli mutants lacking the DnaK chaperone.
Bukau B, Walker GC. Bukau B, et al. EMBO J. 1990 Dec;9(12):4027-36. EMBO J. 1990. PMID: 2249663 Free PMC article.
Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock protein in normal metabolism.
Bukau B, Walker GC. Bukau B, et al. J Bacteriol. 1989 May;171(5):2337-46. doi: 10.1128/jb.171.5.2337-2346.1989. J Bacteriol. 1989. PMID: 2651398 Free PMC article.
Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication.
Buchberger A, Theyssen H, Schröder H, McCarty JS, Virgallita G, Milkereit P, Reinstein J, Bukau B. Buchberger A, et al. Among authors: bukau b. J Biol Chem. 1995 Jul 14;270(28):16903-10. doi: 10.1074/jbc.270.28.16903. J Biol Chem. 1995. PMID: 7622507
Conserved ATPase and luciferase refolding activities between bacteria and yeast Hsp70 chaperones and modulators.
Levy EJ, McCarty J, Bukau B, Chirico WJ. Levy EJ, et al. Among authors: bukau b. FEBS Lett. 1995 Jul 24;368(3):435-40. doi: 10.1016/0014-5793(95)00704-d. FEBS Lett. 1995. PMID: 7635193
A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE.
Buchberger A, Schröder H, Büttner M, Valencia A, Bukau B. Buchberger A, et al. Among authors: bukau b. Nat Struct Biol. 1994 Feb;1(2):95-101. doi: 10.1038/nsb0294-95. Nat Struct Biol. 1994. PMID: 7656024
The role of ATP in the functional cycle of the DnaK chaperone system.
McCarty JS, Buchberger A, Reinstein J, Bukau B. McCarty JS, et al. Among authors: bukau b. J Mol Biol. 1995 May 26;249(1):126-37. doi: 10.1006/jmbi.1995.0284. J Mol Biol. 1995. PMID: 7776367
Escherichia coli FtsH is a membrane-bound, ATP-dependent protease which degrades the heat-shock transcription factor sigma 32.
Tomoyasu T, Gamer J, Bukau B, Kanemori M, Mori H, Rutman AJ, Oppenheim AB, Yura T, Yamanaka K, Niki H, et al. Tomoyasu T, et al. Among authors: bukau b. EMBO J. 1995 Jun 1;14(11):2551-60. EMBO J. 1995. PMID: 7781608 Free PMC article.
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