Regulation of Hsp90 ATPase Activity by the Co-chaperone Cdc37p/p50-Reference-Cited by-同舟云学术

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Regulation of Hsp90 ATPase Activity by the Co-chaperone Cdc37p/p50

Published:2002-06 Issue:23 Volume:277 Page:20151-20159
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Siligardi Giuliano,Panaretou Barry,Meyer Philippe,Singh Shradha,Woolfson Derek N.,Piper Peter W.,Pearl Laurence H.,Prodromou Chrisostomos

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference39 articles.

1. Structure, function, and mechanism of the Hsp90 molecular chaperone

2. The Importance of ATP Binding and Hydrolysis by Hsp90 in Formation and Function of Protein Heterocomplexes

3. ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone invivo

4. In Vivo Function of Hsp90 Is Dependent on ATP Binding and ATP Hydrolysis

5. Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence

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1. Establishing Order Through Disorder by the Hsp90 Molecular Chaperone;Journal of Molecular Biology;2024-07

2. Cochaperones convey the energy of ATP hydrolysis for directional action of Hsp90;Nature Communications;2024-01-17

3. The HSP40 family chaperone isoform DNAJB6b prevents neuronal cells from tau aggregation;BMC Biology;2023-12-18

4. Probing the substrate binding modes and catalytic mechanisms of BLEG-1, a promiscuous B3 metallo-β-lactamase with glyoxalase II properties;PLOS ONE;2023-09-06

5. Interaction of Blenoxane and Congeners Bleomycins A2 and B2 with Human Plasma Proteins Using Circular Dichroism Spectroscopy;International Journal of Molecular Sciences;2023-09-02

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