Small Molecule Modulators of Endogenous and Co-chaperone-stimulated Hsp70 ATPase Activity-Reference-Cited by-同舟云学术

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Small Molecule Modulators of Endogenous and Co-chaperone-stimulated Hsp70 ATPase Activity

Published:2004-12 Issue:49 Volume:279 Page:51131-51140
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Fewell Sheara W.,Smith Christine M.,Lyon Michael A.,Dumitrescu Teodora Pene,Wipf Peter,Day Billy W.,Brodsky Jeffrey L.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference84 articles.

1. The ATPase core of a clathrin uncoating protein.

2. Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein

3. The Peptide-Binding Domain of the Chaperone Protein Hsc70 Has an Unusual Secondary Structure Topology

4. Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK

5. Identification of the peptide binding domain of hsc70. 18-Kilodalton fragment located immediately after ATPase domain is sufficient for high affinity binding.

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