Quantifying Correlations Between Allosteric Sites in Thermodynamic Ensembles - Wikidata - awgldk - TriplyDB

Quantifying Correlations Between Allosteric Sites in Thermodynamic Ensembles

Quantifying Correlations Between Allosteric Sites in Thermodynamic Ensembles

http://www.wikidata.org/entity/Q28392472

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Correlation as a determinant of configurational entropy in supramolecular and protein systems Revealing Atomic-Level Mechanisms of Protein Allostery with Molecular Dynamics Simulations Principles and Overview of Sampling Methods for Modeling Macromolecular Structure and Dynamics Small Molecule Targeting of Protein-Protein Interactions through Allosteric Modulation of Dynamics Novel allosteric sites on Ras for lead generation Two polymorphisms facilitate differences in plasticity between two chicken major histocompatibility complex class I proteins Modeling conformational ensembles of slow functional motions in Pin1-WW Synergistic Allostery, a Sophisticated Regulatory Network for the Control of Aromatic Amino Acid Biosynthesis in Mycobacterium tuberculosis Automated identification of functional dynamic contact networks from X-ray crystallography Dynamics-Driven Allostery in Protein Kinases The role of oligomerization and cooperative regulation in protein function: the case of tryptophan synthase Accelerated convergence of molecular free energy via superposition approximation-based reference states Efficient calculation of molecular configurational entropies using an information theoretic approximation Nonlinear backbone torsional pair correlations in proteins Identification of potential small molecule binding pockets on Rho family GTPases Utilizing a dynamical description of IspH to aid in the development of novel antimicrobial drugs NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional Dynamics Disulfide-Trapping Identifies a New, Effective Chemical Probe for Activating the Nuclear Receptor Human LRH-1 (NR5A2)Decoding the Interactions Regulating the Active State Mechanics of Eukaryotic Protein Kinases Entropy Transfer between Residue Pairs and Allostery in Proteins: Quantifying Allosteric Communication in Ubiquitin Emerging Computational Methods for the Rational Discovery of Allosteric Drugs.Application of information theory to a three-body coarse-grained representation of proteins in the PDB: insights into the structural and evolutionary roles of residues in protein structure.Mutations in Antibody Fragments Modulate Allosteric Response Via Hydrogen-Bond Network Fluctuations.Gorge Motions of Acetylcholinesterase Revealed by Microsecond Molecular Dynamics Simulations.Investigating the mutation resistance of nonnucleoside inhibitors of HIV-RT using multiple microsecond atomistic simulations.Computational approaches to mapping allosteric pathways.Extensive conformational heterogeneity within protein cores.Computational and Experimental Characterization of Patient Derived Mutations Reveal an Unusual Mode of Regulatory Spine Assembly and Drug Sensitivity in EGFR Kinase.Dynamically-driven enhancement of the catalytic machinery of the SARS 3C-like protease by the S284-T285-I286/A mutations on the extra domain.Differences in allosteric communication pipelines in the inactive and active states of a GPCR.A-site residues move independently from P-site residues in all-atom molecular dynamics simulations of the 70S bacterial ribosome.T-Analyst: a program for efficient analysis of protein conformational changes by torsion angles Exploring residue component contributions to dynamical network models of allostery Equilibrium fluctuations of a single folded protein reveal a multitude of potential cryptic allosteric sites.Dynamic architecture of a protein kinase.Ab initio modeling and experimental assessment of Janus Kinase 2 (JAK2) kinase-pseudokinase complex structure.Active-site residues move independently from the rest of the protein in a 200 ns molecular dynamics simulation of cytochrome P450 CYP119.Discovery of multiple hidden allosteric sites by combining Markov state models and experiments Achieving peptide binding specificity and promiscuity by loops: case of the forkhead-associated domain.A Fragment-Based Ligand Screen Against Part of a Large Protein Machine: The ND1 Domains of the AAA+ ATPase p97/VCP.

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P2860

Quantifying Correlations Between Allosteric Sites in Thermodynamic Ensembles

http://www.wikidata.org/entity/Q28392472

description

2009 nî lūn-bûn

@nan

2009 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2009年の論文

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2009年学术文章

@wuu

2009年学术文章

@zh-cn

2009年学术文章

@zh-hans

2009年学术文章

@zh-my

2009年学术文章

@zh-sg

2009年學術文章

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name

Quantifying Correlations Between Allosteric Sites in Thermodynamic Ensembles

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Quantifying Correlations Between Allosteric Sites in Thermodynamic Ensembles

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Quantifying Correlations Between Allosteric Sites in Thermodynamic Ensembles

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type

label

Quantifying Correlations Between Allosteric Sites in Thermodynamic Ensembles

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Quantifying Correlations Between Allosteric Sites in Thermodynamic Ensembles

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Quantifying Correlations Between Allosteric Sites in Thermodynamic Ensembles

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prefLabel

Quantifying Correlations Between Allosteric Sites in Thermodynamic Ensembles

@ast

Quantifying Correlations Between Allosteric Sites in Thermodynamic Ensembles

@en

Quantifying Correlations Between Allosteric Sites in Thermodynamic Ensembles

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Journal of Chemical Theory and Computation

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Quantifying Correlations Between Allosteric Sites in Thermodynamic Ensembles

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P2093

Christopher L McClendon

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David L Mobley

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Gregory Friedland

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Homeira Amirkhani

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P2860

Nearest-neighbor nonparametric method for estimating the configurational entropy of complex molecules

Efficient calculation of configurational entropy from molecular simulations by combining the mutual-information expansion and nearest-neighbor methods

The association of tetrameric acetylcholinesterase with ColQ tail: a block normal mode analysis.

Allosteric communication occurs via networks of tertiary and quaternary motions in proteins

Binding of small molecules to an adaptive protein-protein interface

Discovery and characterization of cooperative ligand binding in the adaptive region of interleukin-2

Engineering Protein Allostery: 1.05 Å Resolution Structure and Enzymatic Properties of a Na+-activated Trypsin

GROMACS: fast, flexible, and free

Probing the flexibility of large conformational changes in protein structures through local perturbations

A simple model of backbone flexibility improves modeling of side-chain conformational variability

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2486-2502

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scholarly article

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877406

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10.1021/CT9001812

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9

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5

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Matthew P. Jacobson

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2009-09-08T00:00:00Z

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41453248

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20161451

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2790287

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