Minimum free energy path of ligand-induced transition in adenylate kinase - Wikidata - thesis-toulmin - TriplyDB

Minimum free energy path of ligand-induced transition in adenylate kinase

Minimum free energy path of ligand-induced transition in adenylate kinase

http://www.wikidata.org/entity/Q27330358

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Extended Phase-Space Methods for Enhanced Sampling in Molecular Simulations: A Review Exploring the conformational transitions of biomolecular systems using a simple two-state anisotropic network model P-loop conformation governed crizotinib resistance in G2032R-mutated ROS1 tyrosine kinase: clues from free energy landscape ClustENM: ENM-Based Sampling of Essential Conformational Space at Full Atomic Resolution.Fast exploration of an optimal path on the multidimensional free energy surface Identification and biochemical characterization of adenylate kinase 1 from Clonorchis sinensis.Conformational dynamics of a ligand-free adenylate kinase.Energetics and structural characterization of the large-scale functional motion of adenylate kinase Free energy landscape of activation in a signalling protein at atomic resolution.The allosteric switching mechanism in bacteriophage MS2.Coarse-grained molecular dynamics simulations of protein-ligand binding.Simple, yet powerful methodologies for conformational sampling of proteins.Use of Integrated Computational Approaches in the Search for New Therapeutic Agents.Parsimony in Protein Conformational Change.Global transitions of proteins explored by a multiscale hybrid methodology: application to adenylate kinase.Fast sampling of A-to-B protein global conformational transitions: from Galileo Galilei to Monte Carlo anisotropic network modeling.Substrate Binding Specifically Modulates Domain Arrangements in Adenylate Kinase.Minimum action transition paths connecting minima on an energy surface.Ab initio sampling of transition paths by conditioned Langevin dynamics.Hybrid All-Atom/Coarse-Grained Simulations of Proteins by Direct Coupling of CHARMM and PRIMO Force Fields.On the induced-fit mechanism of substrate-enzyme binding structures of nylon-oligomer hydrolase.Engineering Biomolecular Switches for Dynamic Metabolic Control.Multiscale enhanced path sampling based on the Onsager-Machlup action: application to a model polymer.Energetics and conformational pathways of functional rotation in the multidrug transporter AcrB.Sampling large conformational transitions: adenylate kinase as a testing ground

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P2860

Minimum free energy path of ligand-induced transition in adenylate kinase

http://www.wikidata.org/entity/Q27330358

description

2012 nî lūn-bûn

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2012 թուականին հրատարակուած գիտական յօդուած

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2012 թվականին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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name

Minimum free energy path of ligand-induced transition in adenylate kinase

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Minimum free energy path of ligand-induced transition in adenylate kinase

@en

Minimum free energy path of ligand-induced transition in adenylate kinase

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type

label

Minimum free energy path of ligand-induced transition in adenylate kinase

@ast

Minimum free energy path of ligand-induced transition in adenylate kinase

@en

Minimum free energy path of ligand-induced transition in adenylate kinase

@nl

prefLabel

Minimum free energy path of ligand-induced transition in adenylate kinase

@ast

Minimum free energy path of ligand-induced transition in adenylate kinase

@en

Minimum free energy path of ligand-induced transition in adenylate kinase

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JOURNAL.PCBI.1002555

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PLOS Computational Biology

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Minimum free energy path of ligand-induced transition in adenylate kinase

@en

P2093

Akinori Kidera

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

Hiroshi Fujisaki

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

Kei Moritsugu

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

Tohru Terada

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

P2860

Some Studies Concerning Rotating Axes and Polyatomic Molecules

Application of a Theory of Enzyme Specificity to Protein Synthesis

Conformational transitions of adenylate kinase: switching by cracking

Comparison of simple potential functions for simulating liquid water

Intrinsic motions along an enzymatic reaction trajectory

Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding

PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations

ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

Mechanism of adenylate kinase. The "essential lysine" helps to orient the phosphates and the active site residues to proper conformations

Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state

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e1002555

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scholarly article

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10.1371/JOURNAL.PCBI.1002555

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6

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8

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Yasuhiro Matsunaga

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2012-01-01T00:00:00Z

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225290881

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22685395

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3369945

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