Chemical shift imprint of intersubunit communication in a symmetric homodimer. - Wikidata - awgldk - TriplyDB

Chemical shift imprint of intersubunit communication in a symmetric homodimer.

Chemical shift imprint of intersubunit communication in a symmetric homodimer.

http://www.wikidata.org/entity/Q37213768

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Cracking the allosteric code of NMR chemical shifts Widespread Perturbation of Function, Structure, and Dynamics by a Conservative Single-Atom Substitution in Thymidylate Synthase.Thermodynamic and NMR Assessment of Ligand Cooperativity and Intersubunit Communication in Symmetric Dimers: Application to Thymidylate Synthase.

P2860

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P2860

Chemical shift imprint of intersubunit communication in a symmetric homodimer.

http://www.wikidata.org/entity/Q37213768

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 27 July 2016

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Chemical shift imprint of intersubunit communication in a symmetric homodimer.

@en

Chemical shift imprint of intersubunit communication in a symmetric homodimer.

@nl

type

label

Chemical shift imprint of intersubunit communication in a symmetric homodimer.

@en

Chemical shift imprint of intersubunit communication in a symmetric homodimer.

@nl

prefLabel

Chemical shift imprint of intersubunit communication in a symmetric homodimer.

@en

Chemical shift imprint of intersubunit communication in a symmetric homodimer.

@nl

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PNAS.1604748113

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Chemical shift imprint of intersubunit communication in a symmetric homodimer.

@en

P2093

Andrew L Lee

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

Bradley T Falk

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

Paul J Sapienza

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

P2860

The structural mechanism for half-the-sites reactivity in an enzyme, thymidylate synthase, involves a relay of changes between subunits

Cooperative inhibition of human thymidylate synthase by mixtures of active site binding and allosteric inhibitors.

Use of strain in a stereospecific catalytic mechanism: crystal structures of Escherichia coli thymidylate synthase bound to FdUMP and methylenetetrahydrofolate

Allostery without a conformational change? Revisiting the paradigm.

Protein allostery, signal transmission and dynamics: a classification scheme of allosteric mechanisms.

Allostery and cooperativity revisited.

Mapping allostery through the covariance analysis of NMR chemical shifts

Conformational dynamics along an enzymatic reaction pathway: thymidylate synthase, "the movie".

Mapping the Free Energy Landscape of PKA Inhibition and Activation: A Double-Conformational Selection Model for the Tandem cAMP-Binding Domains of PKA RIα.

Solution NMR Spectroscopy for the Study of Enzyme Allostery.

P304

9533-9538

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scholarly article

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10.1073/PNAS.1604748113

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34

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113

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2016-07-27T00:00:00Z

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27466406

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5003262

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