Structure-Based Statistical Mechanical Model Accounts for the Causality and Energetics of Allosteric Communication (Q28550501)

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English	Structure-Based Statistical Mechanical Model Accounts for the Causality and Energetics of Allosteric Communication	scientific article

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instance of

scholarly article

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title

Structure-Based Statistical Mechanical Model Accounts for the Causality and Energetics of Allosteric Communication (English)

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main subject

statistics

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author

Enrico Guarnera

object named as

Enrico Guarnera

series ordinal

1

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author name string

Igor N Berezovsky

series ordinal

2

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language of work or name

English

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publication date

March 2016

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published in

PLOS Computational Biology

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volume

12

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issue

3

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page(s)

e1004678

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copyright license

Creative Commons Attribution 4.0 International

start time

3 March 2016

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April 2022 Public Data File from Crossref

copyright status

copyrighted

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cites work

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Modulation of Global Low-Frequency Motions Underlies Allosteric Regulation: Demonstration in CRP/FNR Family Transcription Factors

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Turning a protein kinase on or off from a single allosteric site via disulfide trapping

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Allostery at G Protein-Coupled Receptor Homo- and Heteromers: Uncharted Pharmacological Landscapes

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Structural basis for a reciprocating mechanism of negative cooperativity in dimeric phosphagen kinase activity

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Structural basis for cAMP-mediated allosteric control of the catabolite activator protein.

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ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

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19 March 2017

Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation

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Molecular mechanism for the regulation of human mitochondrial NAD(P)+-dependent malic enzyme by ATP and fumarate

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The structure of apo human glutamate dehydrogenase details subunit communication and allostery

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The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan

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The allosteric transition of glucosamine-6-phosphate deaminase: the structure of the T state at 2.3 A resolution

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Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution

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19 March 2017

The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase

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Structural basis of the allosteric behaviour of phosphofructokinase

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Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits*

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The Energy Landscapes and Motions of Proteins

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Allosteric sites: remote control in regulation of protein activity

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29 September 2017

Unraveling structural mechanisms of allosteric drug action

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29 September 2017

Frequency response of a protein to local conformational perturbations

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29 September 2017

SPACER: Server for predicting allosteric communication and effects of regulation.

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29 September 2017

Thermodynamics of allostery paves a way to allosteric drugs

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29 September 2017

The energy and work of a ligand-gated ion channel

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29 September 2017

Structure and allostery of the chaperonin GroEL.

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29 September 2017

Coherent conformational degrees of freedom as a structural basis for allosteric communication

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Protein dynamics and allostery: an NMR view

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The origin of allosteric functional modulation: multiple pre-existing pathways

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29 September 2017

Allostery and cooperativity revisited

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29 September 2017

Dynamically driven protein allostery.

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29 September 2017

Quantifying allosteric effects in proteins.

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29 September 2017

Searching for new allosteric sites in enzymes

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29 September 2017

Bulk-solvent and hydration-shell fluctuations, similar to alpha- and beta-fluctuations in glasses, control protein motions and functions

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29 September 2017

Is allostery an intrinsic property of all dynamic proteins?

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Allosteric proteins and cellular control systems

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29 September 2017

Normal modes for specific motions of macromolecules: application to the hinge-bending mode of lysozyme

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Temperature-dependent X-ray diffraction as a probe of protein structural dynamics

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How well can we understand large-scale protein motions using normal modes of elastic network models?

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3 June 2018

Site-directed mutagenesis in Bacillus stearothermophilus fructose-6-phosphate 1-kinase. Mutation at the substrate-binding site affects allosteric behavior.

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Allosteric regulation and communication between subunits in uracil phosphoribosyltransferase from Sulfolobus solfataricus

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Allosteric threonine synthase. Reorganization of the pyridoxal phosphate site upon asymmetric activation through S-adenosylmethionine binding to a novel site

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Large Amplitude Elastic Motions in Proteins from a Single-Parameter, Atomic Analysis

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Allostery without conformation change: modelling protein dynamics at multiple scales

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Analysis of domain motions by approximate normal mode calculations

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Structure of Hæmoglobin : An X-ray Examination of Reduced Horse Hæmoglobin

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Allostery without conformational change. A plausible model

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Analysis of the low-frequency normal modes of the R state of aspartate transcarbamylase and a comparison with the T state modes

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Dynamics of ligand binding to myoglobin

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based on heuristic

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Network of dynamically important residues in the open/closed transition in polymerases is strongly conserved

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Identifiers

DOI

10.1371/JOURNAL.PCBI.1004678

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1083236

DBLP publication ID

journals/ploscb/GuarneraB16

1 reference

stated in

DBLP Dataset 2021-01-02

retrieved

28 January 2021

OpenCitations bibliographic resource ID

1083236

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1083236

PMC publication ID

4777440

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1083236

PubMed publication ID

26939022

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1083236

ResearchGate publication ID

296699243

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