The intrinsic dynamics of enzymes plays a dominant role in determining the structural changes induced upon inhibitor binding
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Druggability Assessment of Allosteric Proteins by Dynamics Simulations in the Presence of Probe MoleculesReverse engineering the cooperative machinery of human hemoglobinReaction trajectory revealed by a joint analysis of protein data bankChanges in dynamics upon oligomerization regulate substrate binding and allostery in amino acid kinase family membersModeling conformational ensembles of slow functional motions in Pin1-WWDiscovering conformational sub-states relevant to protein functionPlasticity of Cytochrome P450 2B4 as Investigated by Hydrogen-Deuterium Exchange Mass Spectrometry and X-ray CrystallographyTyrosine Latching of a Regulatory Gate Affords Allosteric Control of Aromatic Amino Acid BiosynthesisDistinct States of Methionyl-tRNA Synthetase Indicate Inhibitor Binding by Conformational SelectionSolution NMR of a 463-residue phosphohexomutase: domain 4 mobility, substates, and phosphoryl transfer defect.Spatial elucidation of motion in proteins by ensemble-based structure calculation using exact NOEsAtomic-level characterization of the activation mechanism of SERCA by calciumA role for both conformational selection and induced fit in ligand binding by the LAO proteinMutation D816V alters the internal structure and dynamics of c-KIT receptor cytoplasmic region: implications for dimerization and activation mechanismsQuantitatively characterizing the ligand binding mechanisms of choline binding protein using Markov state model analysisHow Intrinsic Molecular Dynamics Control Intramolecular Communication in Signal Transducers and Activators of Transcription Factor STAT5Prediction of mutational tolerance in HIV-1 protease and reverse transcriptase using flexible backbone protein designAdaptability in protein structures: structural dynamics and implications in ligand design.The glassy state of crambin and the THz time scale protein-solvent fluctuations possibly related to protein function.Comparison of the Internal Dynamics of Metalloproteases Provides New Insights on Their Function and Evolution.Vibrational resonance, allostery, and activation in rhodopsin-like G protein-coupled receptors.Predicting Protein Dynamics and Allostery Using Multi-Protein Atomic Distance Constraints.Protein structure along the order-disorder continuumPre-existing soft modes of motion uniquely defined by native contact topology facilitate ligand binding to proteinsPaths of long-range communication in the E2 enzymes of family 3: a molecular dynamics investigation.Investigating the mutation resistance of nonnucleoside inhibitors of HIV-RT using multiple microsecond atomistic simulations.ClustENM: ENM-Based Sampling of Essential Conformational Space at Full Atomic Resolution.On the conservation of the slow conformational dynamics within the amino acid kinase family: NAGK the paradigm.Global Conformational Dynamics of HIV-1 Reverse Transcriptase Bound to Non-Nucleoside Inhibitors.Chromosomal dynamics predicted by an elastic network model explains genome-wide accessibility and long-range couplingsUsing entropy maximization to understand the determinants of structural dynamics beyond native contact topologyBiophysical Insights into the Inhibitory Mechanism of Non-Nucleoside HIV-1 Reverse Transcriptase Inhibitors.Role of Hsp70 ATPase domain intrinsic dynamics and sequence evolution in enabling its functional interactions with NEFs.Normal mode analysis of biomolecular structures: functional mechanisms of membrane proteins.THz time scale structural rearrangements and binding modes in lysozyme-ligand interactionsTwo-dimensional NMR and all-atom molecular dynamics of cytochrome P450 CYP119 reveal hidden conformational substatesProDy: protein dynamics inferred from theory and experiments.Substrate-induced changes in protease active site conformation impact on subsequent reactions with substrates.Rationale for more diverse inhibitors in competition with substrates in HIV-1 protease.Evol and ProDy for bridging protein sequence evolution and structural dynamics
P2860
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P2860
The intrinsic dynamics of enzymes plays a dominant role in determining the structural changes induced upon inhibitor binding
description
2009 nî lūn-bûn
@nan
2009 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
The intrinsic dynamics of enzy ...... induced upon inhibitor binding
@ast
The intrinsic dynamics of enzy ...... induced upon inhibitor binding
@en
type
label
The intrinsic dynamics of enzy ...... induced upon inhibitor binding
@ast
The intrinsic dynamics of enzy ...... induced upon inhibitor binding
@en
prefLabel
The intrinsic dynamics of enzy ...... induced upon inhibitor binding
@ast
The intrinsic dynamics of enzy ...... induced upon inhibitor binding
@en
P2860
P356
P1476
The intrinsic dynamics of enzy ...... induced upon inhibitor binding
@en
P2093
Ahmet Bakan
P2860
P304
14349-14354
P356
10.1073/PNAS.0904214106
P407
P50
P577
2009-08-17T00:00:00Z