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Items: 1 to 20 of 35

1.

ATP-induced protein-Hsp70 complex dissociation requires K+ but not ATP hydrolysis.

Palleros DR, Reid KL, Shi L, Welch WJ, Fink AL.

Nature. 1993 Oct 14;365(6447):664-6.

PMID:
8413631
2.

Kinetics of molecular chaperone action.

Schmid D, Baici A, Gehring H, Christen P.

Science. 1994 Feb 18;263(5149):971-3.

PMID:
8310296
3.

Autoregulation of the Escherichia coli heat shock response by the DnaK and DnaJ heat shock proteins.

Liberek K, Georgopoulos C.

Proc Natl Acad Sci U S A. 1993 Dec 1;90(23):11019-23.

5.

Molecular chaperone functions of heat-shock proteins.

Hendrick JP, Hartl FU.

Annu Rev Biochem. 1993;62:349-84. Review. No abstract available.

PMID:
8102520
6.
7.

The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE.

Szabo A, Langer T, Schröder H, Flanagan J, Bukau B, Hartl FU.

Proc Natl Acad Sci U S A. 1994 Oct 25;91(22):10345-9.

8.

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.

EMBO J. 1994 Apr 1;13(7):1687-95.

9.

Regulation of the Escherichia coli heat-shock response.

Bukau B.

Mol Microbiol. 1993 Aug;9(4):671-80.

PMID:
7901731
10.
11.

The DnaK chaperone system of Escherichia coli: quaternary structures and interactions of the DnaK and GrpE components.

Schönfeld HJ, Schmidt D, Schröder H, Bukau B.

J Biol Chem. 1995 Feb 3;270(5):2183-9.

13.

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.

EMBO J. 1995 Jun 1;14(11):2551-60.

14.

The role of ATP in the functional cycle of the DnaK chaperone system.

McCarty JS, Buchberger A, Reinstein J, Bukau B.

J Mol Biol. 1995 May 26;249(1):126-37.

PMID:
7776367
15.

Degradation of sigma 32, the heat shock regulator in Escherichia coli, is governed by HflB.

Herman C, Thévenet D, D'Ari R, Bouloc P.

Proc Natl Acad Sci U S A. 1995 Apr 11;92(8):3516-20.

16.

Biospecific interaction analysis using biosensor technology.

Malmqvist M.

Nature. 1993 Jan 14;361(6408):186-7. Review.

PMID:
7678451
17.

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.

Nat Struct Biol. 1994 Feb;1(2):95-101.

PMID:
7656024
19.

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.

J Biol Chem. 1995 Jul 14;270(28):16903-10.

20.
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