(Q27677156)

2

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Chunyan Xu

3

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Feng Yu

4

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Huan Zhou

5

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Yanlong Zhao

6

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Jian Zhang

7

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Jianhua Cai

8

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Cheney Mao

9

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Lin Tang

10

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Yechun Xu

11

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Jianhua He

Acta Biochimica et Biophysica Sinica

12

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language of work or name

1 reference

April 2012

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published in

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volume

44

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issue

4

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page(s)

300-6

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cites work

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Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle

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Independent ATPase activity of Hsp90 subunits creates a flexible assembly platform

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Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements

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Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23.

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N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle

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Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent

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In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis

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Crystal structure and molecular modeling of 17-DMAG in complex with human Hsp90

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Novel, potent small-molecule inhibitors of the molecular chaperone Hsp90 discovered through structure-based design

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Identifying the catalytic residue of the ATPase reaction of DNA gyrase

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Comparative genomics and evolution of the HSP90 family of genes across all kingdoms of organisms

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Structure of the ATP-binding domain of Plasmodium falciparum Hsp90

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Crystal structure of an N-terminal fragment of the DNA gyrase B protein.

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Intrinsic inhibition of the Hsp90 ATPase activity

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