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Amino Acid Networks in a (β/α)8 Barrel Enzyme Change during Catalytic Turnover

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/prot.340110305openalex-snapshot
Collective motions in proteins: A covariance analysis of atomic fluctuations in molecular dynamics and normal mode simulations
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A Critical Evaluation of Correlated Mutation Algorithms and Coevolution Within Allosteric Mechanisms
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T-Analyst: a program for efficient analysis of protein conformational changes by torsion angles
inferredcites →https://doi.org/10.1016/b978-0-12-394292-0.00010-2openalex-snapshot
Evolution-Based Design of Proteins
inferredcites →https://doi.org/10.1016/j.abb.2012.01.016openalex-snapshot
Allosteric regulation of substrate channeling and catalysis in the tryptophan synthase bienzyme complex
inferredcites →https://doi.org/10.1016/j.bbrc.2004.08.222openalex-snapshot
Structures of wild-type and P28L/Y173F tryptophan synthase α-subunits from Escherichia coli
inferredcites →https://doi.org/10.1016/j.cbpa.2010.08.007openalex-snapshot
Choreographing an enzyme's dance
inferredcites →https://doi.org/10.1016/j.jmb.2004.10.055openalex-snapshot
Network Analysis of Protein Structures Identifies Functional Residues
inferredcites →https://doi.org/10.1016/j.jmb.2006.08.076openalex-snapshot
Evaluation of Energetic and Dynamic Coupling Networks in a PDZ Domain Protein
inferredcites →https://doi.org/10.1016/j.jmb.2013.01.030openalex-snapshot
Long-Range Interactions in the Alpha Subunit of Tryptophan Synthase Help to Coordinate Ligand Binding, Catalysis, and Substrate Channeling
inferredcites →https://doi.org/10.1021/bi952506dopenalex-snapshot
Exchange of K+ or Cs+ for Na+ Induces Local and Long-Range Changes in the Three-Dimensional Structure of the Tryptophan Synthase α2β2 Complex
inferredcites →https://doi.org/10.1038/nature04105openalex-snapshot
Intrinsic dynamics of an enzyme underlies catalysis
inferredcites →https://doi.org/10.1038/nature08560openalex-snapshot
Dynamic activation of an allosteric regulatory protein
inferredcites →https://doi.org/10.1038/nature13001openalex-snapshot
The ensemble nature of allostery
inferredcites →https://doi.org/10.1038/nchembio.98openalex-snapshot
Allosteric regulation and catalysis emerge via a common route
inferredcites →https://doi.org/10.1038/nmeth.2592openalex-snapshot
Automated identification of functional dynamic contact networks from X-ray crystallography
inferredcites →https://doi.org/10.1038/nsb881openalex-snapshot
Evolutionarily conserved networks of residues mediate allosteric communication in proteins
inferredcites →https://doi.org/10.1038/nsb991openalex-snapshot
Covariation of backbone motion throughout a small protein domain
inferredcites →https://doi.org/10.1038/nsmb1132openalex-snapshot
Dynamically driven protein allostery
inferredcites →https://doi.org/10.1038/nsmb821openalex-snapshot
Linkage between dynamics and catalysis in a thermophilic-mesophilic enzyme pair
inferredcites →https://doi.org/10.1039/c4cp00110aopenalex-snapshot
NMR mapping of protein conformational landscapes using coordinated behavior of chemical shifts upon ligand binding
inferredcites →https://doi.org/10.1073/pnas.1017311108openalex-snapshot
Mapping allostery through the covariance analysis of NMR chemical shifts
inferredcites →https://doi.org/10.1073/pnas.1120536109openalex-snapshot
Allosteric pathways in imidazole glycerol phosphate synthase
inferredcites →https://doi.org/10.1073/pnas.1312644110openalex-snapshot
Signaling through dynamic linkers as revealed by PKA
inferredcites →https://doi.org/10.1073/pnas.161239298openalex-snapshot
Propagating conformational changes over long (and short) distances in proteins
inferredcites →https://doi.org/10.1074/jbc.273.15.8553openalex-snapshot
Cryo-crystallography of a True Substrate, Indole-3-glycerol Phosphate, Bound to a Mutant (αD60N) Tryptophan Synthase α2β2 Complex Reveals the Correct Orientation of Active Site αGlu49
inferredcites →https://doi.org/10.1074/jbc.m111285200openalex-snapshot
Crystal Structures of a New Class of Allosteric Effectors Complexed to Tryptophan Synthase
inferredcites →https://doi.org/10.1074/jbc.m112.394866openalex-snapshot
Conservation of Flexible Residue Clusters among Structural and Functional Enzyme Homologues
inferredcites →https://doi.org/10.1093/nar/gki398openalex-snapshot
SPACE: a suite of tools for protein structure prediction and analysis based on complementarity and environment
inferredcites →https://doi.org/10.1110/ps.0221103openalex-snapshot
Partial NMR assignments and secondary structure mapping of the isolated α subunit of Escherichia coli tryptophan synthase, a 29‐kD TIM barrel protein
inferredcites →https://doi.org/10.1111/j.1432-1033.1976.tb10351.xopenalex-snapshot
Steady‐State Kinetic Studies of the Synthesis of Indoleglycerol Phosphate Catalyzed by the α Subunit of Tryptophan Synthase from Escherichia coli
inferredcites →https://doi.org/10.1371/journal.pcbi.1000994openalex-snapshot
The Role of Oligomerization and Cooperative Regulation in Protein Function: The Case of Tryptophan Synthase
inferredcites →https://doi.org/10.1371/journal.pone.0048707openalex-snapshot
The Auto-Inhibitory Role of the EPAC Hinge Helix as Mapped by NMR
inferredcites →https://doi.org/10.1371/journal.pone.0074347openalex-snapshot
Allosteric Coupling between the Intracellular Coupling Helix 4 and Regulatory Sites of the First Nucleotide-binding Domain of CFTR
inferredcites →https://doi.org/10.2174/138920312799277992openalex-snapshot
Disordered Proteins and Network Disorder in Network Descriptions of Protein Structure, Dynamics and Function: Hypotheses and a Comprehensive Review

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Coordinated Network Changes Across the Catalytic Cycle of Alpha Tryptophan Synthase
inferred← citeshttps://doi.org/10.1002/1873-3468.14610openalex-snapshot
An NMR portrait of functional and dysfunctional allosteric cooperativity in cAMP ‐dependent protein kinase A
inferred← citeshttps://doi.org/10.1002/bies.202000092openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/chem.201801068openalex-snapshot
Epoxide Hydrolase Conformational Heterogeneity for the Resolution of Bulky Pharmacologically Relevant Epoxide Substrates
inferred← citeshttps://doi.org/10.1002/pro.2598openalex-snapshot
Severing of a hydrogen bond disrupts amino acid networks in the catalytically active state of the alpha subunit of tryptophan synthase
inferred← citeshttps://doi.org/10.1002/pro.2613openalex-snapshot
Network of long‐range concerted chemical shift displacements upon ligand binding to human angiogenin
inferred← citeshttps://doi.org/10.1002/pro.3379openalex-snapshot
Engineered control of enzyme structural dynamics and function
inferred← citeshttps://doi.org/10.1002/pro.4011openalex-snapshot
Distinct conformational dynamics and allosteric networks in alpha tryptophan synthase during active catalysis
inferred← citeshttps://doi.org/10.1002/pro.4236openalex-snapshot
Discovery of antimicrobial agent targeting tryptophan synthase
inferred← citeshttps://doi.org/10.1007/978-1-4939-7386-6_18openalex-snapshot
Implementation of the NMR CHEmical Shift Covariance Analysis (CHESCA): A Chemical Biologist’s Approach to Allostery
inferred← citeshttps://doi.org/10.1007/978-981-13-8719-7_15openalex-snapshot
Engineering Allostery into Proteins
inferred← citeshttps://doi.org/10.1007/s10858-020-00320-2openalex-snapshot
Backbone assignments and conformational dynamics in the S. typhimurium tryptophan synthase α-subunit from solution-state NMR
inferred← citeshttps://doi.org/10.1007/s10930-021-10012-xopenalex-snapshot
A Minireview on Temperature Dependent Protein Conformational Sampling
inferred← citeshttps://doi.org/10.1016/j.bbrep.2026.102586openalex-snapshot
Solution-state nuclear magnetic resonance studies of the Salmonella typhimurium tryptophan synthase complex
inferred← citeshttps://doi.org/10.1016/j.csbj.2016.06.002openalex-snapshot
Biophysical and computational methods to analyze amino acid interaction networks in proteins
inferred← citeshttps://doi.org/10.1016/j.fbio.2023.102934openalex-snapshot
Study on a galactose decomposition strain of Lactiplantibacillus plantarum MWLp-4 from human milk: Safety evaluating and key genes analysis of potential probiotic function
inferred← citeshttps://doi.org/10.1016/j.jmb.2017.06.009openalex-snapshot
Leveraging Reciprocity to Identify and Characterize Unknown Allosteric Sites in Protein Tyrosine Phosphatases
inferred← citeshttps://doi.org/10.1016/j.sbi.2023.102657openalex-snapshot
Allostery, engineering and inhibition of tryptophan synthase
inferred← citeshttps://doi.org/10.1016/j.str.2015.11.016openalex-snapshot
Uncoupling Catalytic and Binding Functions in the Cyclic AMP-Dependent Protein Kinase A
inferred← citeshttps://doi.org/10.1016/j.str.2019.05.013openalex-snapshot
Coordinated Network Changes across the Catalytic Cycle of Alpha Tryptophan Synthase
inferred← citeshttps://doi.org/10.1016/j.ymeth.2018.05.018openalex-snapshot
NMR methods to dissect the molecular mechanisms of disease-related mutations (DRMs): Understanding how DRMs remodel functional free energy landscapes
inferred← citeshttps://doi.org/10.1016/j.ymeth.2018.06.010openalex-snapshot
Assigning methyl resonances for protein solution-state NMR studies
inferred← citeshttps://doi.org/10.1016/j.ymeth.2022.12.002openalex-snapshot
Analysis of coordinated NMR chemical shifts to map allosteric regulatory networks in proteins
inferred← citeshttps://doi.org/10.1021/acs.biochem.9b00721openalex-snapshot
Energy and Enzyme Activity Landscapes of Yeast Chorismate Mutase at Cellular Concentrations of Allosteric Effectors
inferred← citeshttps://doi.org/10.1021/acs.jpcb.5c04831openalex-snapshot
Multiscale Modeling of Enzymatic Efficiency in Multienzyme Complex: Effect of Interenzyme Distance, Crowding Effect and Side Reactions
inferred← citeshttps://doi.org/10.1021/acscatal.7b02954openalex-snapshot
Role of Conformational Dynamics in the Evolution of Retro-Aldolase Activity
inferred← citeshttps://doi.org/10.1038/s41467-020-17618-2openalex-snapshot
Mapping allosteric communications within individual proteins
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A Tool Set to Map Allosteric Networks through the NMR Chemical Shift Covariance Analysis
inferred← citeshttps://doi.org/10.1039/c8cc02426jopenalex-snapshot
Role of conformational dynamics in the evolution of novel enzyme function
inferred← citeshttps://doi.org/10.1073/pnas.1811168116openalex-snapshot
Identifying coupled clusters of allostery participants through chemical shift perturbations
inferred← citeshttps://doi.org/10.1093/bioinformatics/btaa781openalex-snapshot
CHESPA/CHESCA-SPARKY: automated NMR data analysis plugins for SPARKY to map protein allostery
inferred← citeshttps://doi.org/10.1096/fasebj.2018.32.1_supplement.527.6openalex-snapshot
The evolution of dynamic amino acid interaction networks around the catalytic cycle of α tryptophan synthase
inferred← citeshttps://doi.org/10.1109/bibm.2015.7359854openalex-snapshot
Visualizing the topology and re-analyzing the causes of small-world property of amino acid network
inferred← citeshttps://doi.org/10.1111/febs.13659openalex-snapshot
Protein thermal denaturation is modulated by central residues in the protein structure network
inferred← citeshttps://doi.org/10.3389/fmolb.2018.00092openalex-snapshot
Millisecond Timescale Motions Connect Amino Acid Interaction Networks in Alpha Tryptophan Synthase
inferred← citeshttps://doi.org/10.3389/fmolb.2021.679915openalex-snapshot
Substitution of a Surface-Exposed Residue Involved in an Allosteric Network Enhances Tryptophan Synthase Function in Cells
inferred← citeshttps://doi.org/10.3390/biology4020282openalex-snapshot
NPPD: A Protein-Protein Docking Scoring Function Based on Dyadic Differences in Networks of Hydrophobic and Hydrophilic Amino Acid Residues
inferred← citeshttps://doi.org/10.3390/catal6060082openalex-snapshot
Investigation of Structural Dynamics of Enzymes and Protonation States of Substrates Using Computational Tools
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Site-Mutation of Hydrophobic Core Residues Synchronically Poise Super Interleukin 2 for Signaling: Identifying Distant Structural Effects through Affordable Computations
inferred← citeshttps://doi.org/10.3390/ijms19051427openalex-snapshot
Amino-Acid Network Clique Analysis of Protein Mutation Non-Additive Effects: A Case Study of Lysozyme
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Investigation de la durabilité des structures protéiques et bio-inspiration pour les systèmes urbains
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