Detecting Posttranslational Modifications of Hsp90.

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Detecting Posttranslational Modifications of Hsp90.

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年學術文章

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2018年學術文章

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Detecting Posttranslational Modifications of Hsp90.

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Detecting Posttranslational Modifications of Hsp90.

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label

Detecting Posttranslational Modifications of Hsp90.

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Detecting Posttranslational Modifications of Hsp90.

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Detecting Posttranslational Modifications of Hsp90.

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Detecting Posttranslational Modifications of Hsp90.

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P1476

Detecting Posttranslational Modifications of Hsp90

@en

P2093

Len Neckers

http://www.w3.org/2001/XMLSchema#string

Mehdi Mollapour

http://www.w3.org/2001/XMLSchema#string

Rebecca A Sager

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P2860

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

Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone

Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1

Mechanisms of Hsp90 regulation

The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop

Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase

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

Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone

Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin

Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional properties.

P304

209-219

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P31

scholarly article

P356

10.1007/978-1-4939-7477-1_16

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P407

English

P478

1709

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P50

Mark R Woodford

P577

2018-01-01T00:00:00Z

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P698

29177662

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P932

6376113

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