(Q51556401)

7 April 2018

title

Protein regulation: the statistical theory of allostery. (English)

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7 April 2018

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Michele Vendruscolo

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7 April 2018

publication date

17 June 2011

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7 April 2018

published in

Nature Chemical Biology

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7 April 2018

volume

7

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7 April 2018

issue

7

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7 April 2018

page(s)

411-412

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7 April 2018

https://scigraph.springernature.com/pub.10.1038/nchembio.603

exact match

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cites work

ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

1 reference

https://api.crossref.org/works/10.1038%2FNCHEMBIO.603

Allostery and cooperativity revisited

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCHEMBIO.603

The role of dynamic conformational ensembles in biomolecular recognition

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCHEMBIO.603

NMR reveals novel mechanisms of protein activity regulation

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCHEMBIO.603

New tools provide new insights in NMR studies of protein dynamics

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCHEMBIO.603

Dynamics connect substrate recognition to catalysis in protein kinase A

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCHEMBIO.603

Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCHEMBIO.603

Mapping allostery through the covariance analysis of NMR chemical shifts

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCHEMBIO.603

Protein structure determination from NMR chemical shifts

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCHEMBIO.603

Consistent blind protein structure generation from NMR chemical shift data

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCHEMBIO.603

21 January 2018

Identifiers

DOI

10.1038/NCHEMBIO.603

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7 April 2018

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7 April 2018