Hsp90 Sensitivity to ADP Reveals Hidden Regulation Mechanisms.

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Hsp90 Sensitivity to ADP Reveals Hidden Regulation Mechanisms.

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年學術文章

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2017年學術文章

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Hsp90 Sensitivity to ADP Reveals Hidden Regulation Mechanisms.

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Hsp90 Sensitivity to ADP Reveals Hidden Regulation Mechanisms.

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Hsp90 Sensitivity to ADP Reveals Hidden Regulation Mechanisms.

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Hsp90 Sensitivity to ADP Reveals Hidden Regulation Mechanisms.

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Hsp90 Sensitivity to ADP Reveals Hidden Regulation Mechanisms.

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Hsp90 Sensitivity to ADP Reveals Hidden Regulation Mechanisms.

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P1476

Hsp90 Sensitivity to ADP Reveals Hidden Regulation Mechanisms.

@en

P2093

Jackson C Halpin

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Timothy O Street

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P2860

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

Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones

Structural Asymmetry in the Closed State of Mitochondrial Hsp90 (TRAP1) Supports a Two-Step ATP Hydrolysis Mechanism

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

Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones.

Robust, high-throughput solution structural analyses by small angle X-ray scattering (SAXS)

New developments in the ATSAS program package for small-angle scattering data analysis

Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex

Implementation and performance of SIBYLS: a dual endstation small-angle X-ray scattering and macromolecular crystallography beamline at the Advanced Light Source.

Molecular chaperone functions in protein folding and proteostasis.

P304

2918-2930

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P31

scholarly article

P356

10.1016/J.JMB.2017.08.005

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P407

English

P433

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

P478

429

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P577

2017-08-16T00:00:00Z

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P698

28822683

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P932

5610941

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