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Items: 1 to 20 of 1163

1.

Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain.

Sriram M, Osipiuk J, Freeman B, Morimoto R, Joachimiak A.

Structure. 1997 Mar 15;5(3):403-14.

PMID:
9083109
2.

Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ.

Suh WC, Burkholder WF, Lu CZ, Zhao X, Gottesman ME, Gross CA.

Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15223-8.

3.

Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors.

Sondermann H, Scheufler C, Schneider C, Hohfeld J, Hartl FU, Moarefi I.

Science. 2001 Feb 23;291(5508):1553-7.

5.

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.

6.

Kinetic characterization of the ATPase cycle of the DnaK molecular chaperone.

Russell R, Jordan R, McMacken R.

Biochemistry. 1998 Jan 13;37(2):596-607.

PMID:
9425082
7.

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
8.

Interdomain communication in the molecular chaperone DnaK.

Han W, Christen P.

Biochem J. 2003 Feb 1;369(Pt 3):627-34.

9.

Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK.

Harrison CJ, Hayer-Hartl M, Di Liberto M, Hartl F, Kuriyan J.

Science. 1997 Apr 18;276(5311):431-5.

10.

The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family.

Shaner L, Trott A, Goeckeler JL, Brodsky JL, Morano KA.

J Biol Chem. 2004 May 21;279(21):21992-2001. Epub 2004 Mar 17.

12.

Conformations of the nucleotide and polypeptide binding domains of a cytosolic Hsp70 molecular chaperone are coupled.

Fung KL, Hilgenberg L, Wang NM, Chirico WJ.

J Biol Chem. 1996 Aug 30;271(35):21559-65.

13.

Dissection of the ATP-binding domain of the chaperone hsc70 for interaction with the cofactor Hap46.

Petersen G, Hahn C, Gehring U.

J Biol Chem. 2001 Mar 30;276(13):10178-84. Epub 2000 Dec 19.

14.
15.

ATPase domain of Hsp70 exhibits intrinsic ATP-ADP exchange activity.

Mao Y, Deng A, Qu N, Wu X.

Biochemistry (Mosc). 2006 Nov;71(11):1222-9.

PMID:
17140383
16.
17.

The carboxyl-terminal lobe of Hsc70 ATPase domain is sufficient for binding to BAG1.

Brive L, Takayama S, Briknarová K, Homma S, Ishida SK, Reed JC, Ely KR.

Biochem Biophys Res Commun. 2001 Dec 21;289(5):1099-105.

PMID:
11741305
18.
19.

Multistep mechanism of substrate binding determines chaperone activity of Hsp70.

Mayer MP, Schröder H, Rüdiger S, Paal K, Laufen T, Bukau B.

Nat Struct Biol. 2000 Jul;7(7):586-93.

PMID:
10876246
20.

The J-domain of Hsp40 couples ATP hydrolysis to substrate capture in Hsp70.

Wittung-Stafshede P, Guidry J, Horne BE, Landry SJ.

Biochemistry. 2003 May 6;42(17):4937-44.

PMID:
12718535
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