(Q46113732)

19 December 2017

title

The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis (English)

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19 December 2017

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Moritz Mickler

1

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19 December 2017

Martin Hessling

2

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19 December 2017

Christoph Ratzke

3

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19 December 2017

Johannes Buchner

4

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19 December 2017

Thorsten Hugel

5

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19 December 2017

publication date

22 February 2009

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19 December 2017

Nature Structural & Molecular Biology

published in

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19 December 2017

volume

16

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19 December 2017

issue

3

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19 December 2017

page(s)

281-286

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19 December 2017

https://scigraph.springernature.com/pub.10.1038/nsmb.1557

exact match

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cites work

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Hsp90 structure: when two ends meet

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Direct visualization of asymmetric adenine-nucleotide-induced conformational changes in MutL alpha

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A practical guide to single-molecule FRET

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The solution to multiple structures

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Dimerization of Hsp90 is required for in vivo function. Design and analysis of monomers and dimers

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A Reducing and Oxidizing System Minimizes Photobleaching and Blinking of Fluorescent Dyes

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Measuring the rate of intramolecular contact formation in polypeptides

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Folding at the speed limit

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31 March 2020

Identifiers

DOI

10.1038/NSMB.1557

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19 December 2017

Dimensions Publication ID

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19 December 2017