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Mutagenic analysis of the interior packing of an .alpha./.beta. barrel protein. Effects on the stabilities and rates of interconversion of the native and partially folded forms of the .alpha. subunit of tryptophan synthase
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
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Structural principles of α/β barrel proteins: The packing of the interior of the sheet
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[2] New M13 vectors for cloning
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[26] Effect of point mutations of the folding of globular proteins
inferredcites →https://doi.org/10.1016/0167-4838(87)90328-1openalex-snapshot
Proline isomerization and the slow folding reactions of the α subunit of tryptophan synthase from Escherichia coli
inferredcites →https://doi.org/10.1016/s0021-9258(18)61017-8openalex-snapshot
Site-specific mutagenesis of the alpha subunit of tryptophan synthase from Salmonella typhimurium. Changing arginine 179 to leucine alters the reciprocal transmission of substrate-induced conformational changes between the alpha and beta 2 subunits.
inferredcites →https://doi.org/10.1016/s0021-9258(18)89858-1openalex-snapshot
Effect of amino acid residues on conformational stability in eight mutant proteins variously substituted at a unique position of the tryptophan synthase alpha-subunit.
inferredcites →https://doi.org/10.1016/s0021-9258(19)42032-2openalex-snapshot
Crystalline α2β2 Complexes of Tryptophan Synthetase of Escherichia coli
inferredcites →https://doi.org/10.1016/s0021-9258(19)77913-7openalex-snapshot
Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium.
inferredcites →https://doi.org/10.1016/s0065-3233(08)60286-7openalex-snapshot
λ Repressor: A Model System for Understanding Protein–DNA Interactions and Protein Stability
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[24] Nanosecond fluorescence spectroscopy of macromolecules
inferredcites →https://doi.org/10.1017/s0016672300016517openalex-snapshot
The association of tryptophan synthetase subunits fromEscherichia coliandSalmonella typhimuriumin homologous and heterologous combinations
inferredcites →https://doi.org/10.1021/bi00123a002openalex-snapshot
Amino acid replacements can selectively affect the interaction energy of autonomous folding units in the .alpha. subunit of tryptophan synthase
inferredcites →https://doi.org/10.1021/bi00129a010openalex-snapshot
Stable substructures of eightfold .beta..alpha.-barrel proteins: fragment complementation of phosphoribosylanthranilate isomerase
inferredcites →https://doi.org/10.1021/bi00238a023openalex-snapshot
Solvent denaturation and stabilization of globular proteins
inferredcites →https://doi.org/10.1021/bi00275a019openalex-snapshot
Effect of a single amino acid substitution on the folding of the .alpha. subunit of tryptophan synthase
inferredcites →https://doi.org/10.1021/bi00280a010openalex-snapshot
Conformational stability of mixed disulfide derivatives of .beta.-lactoglobulin B
inferredcites →https://doi.org/10.1021/bi00335a024openalex-snapshot
Characterization of an early intermediate in the folding of the .alpha. subunit of tryptophan synthase by hydrogen exchange measurement
inferredcites →https://doi.org/10.1021/bi00358a035openalex-snapshot
Effects of the phenylalanine-22 .fwdarw. leucine, glutamic acid-49 .fwdarw. methionine, glycine-234 .fwdarw. aspartic acid and glycine-234 .fwdarw. lysine mutations on the folding and stability of the .alpha. subunit of tryptophan synthase from Escherichia coli
inferredcites →https://doi.org/10.1021/bi00369a002openalex-snapshot
Synergism in folding of a double mutant of the .alpha. subunit of tryptophan synthase
inferredcites →https://doi.org/10.1021/bi00402a050openalex-snapshot
Folding of homologous proteins: Conservation of the folding mechanism of the .alpha. subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrides
inferredcites →https://doi.org/10.1021/bi00431a018openalex-snapshot
Effects of multiple replacements at a single position on the folding and stability of dihydrofolate reductase from Escherichia coli
inferredcites →https://doi.org/10.1021/bi00458a027openalex-snapshot
Multiple replacements at position 211 in the .alpha. subunit of tryptophan synthase as a probe of the folding unit association reaction
inferredcites →https://doi.org/10.1021/bi00460a027openalex-snapshot
Role of diffusion in the folding of the .alpha. subunit of tryptophan synthase from Escherichia coli
inferredcites →https://doi.org/10.1021/bi00507a021openalex-snapshot
Urea-induced unfolding of the .alpha. subunit of tryptophan synthase: evidence for a multistate process
inferredcites →https://doi.org/10.1021/bi00540a002openalex-snapshot
Guanidine hydrochloride-induced unfolding of the .alpha. subunit of tryptophan synthase and of the two .alpha. proteolytic fragments: evidence for stepwise unfolding of the two .alpha. domains
inferredcites →https://doi.org/10.1038/227680a0openalex-snapshot
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
inferredcites →https://doi.org/10.1038/340122a0openalex-snapshot
Mapping the transition state and pathway of protein folding by protein engineering
inferredcites →https://doi.org/10.1038/nbt0389-282openalex-snapshot
Efficient Degradation of Trichloroethylene by a Recombinant Escherichia Coli
inferredcites →https://doi.org/10.1073/pnas.78.4.2169openalex-snapshot
Procedure for production of hybrid genes and proteins and its use in assessing significance of amino acid differences in homologous tryptophan synthetase alpha polypeptides.
inferredcites →https://doi.org/10.1073/pnas.82.2.488openalex-snapshot
Rapid and efficient site-specific mutagenesis without phenotypic selection.
inferredcites →https://doi.org/10.1073/pnas.85.10.3338openalex-snapshot
Structural principles of parallel beta-barrels in proteins.
inferredcites →https://doi.org/10.1073/pnas.89.7.2629openalex-snapshot
Simulations of the folding pathway of triose phosphate isomerase-type alpha/beta barrel proteins.
inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a132423openalex-snapshot
Comparison of Denaturation by Guanidine Hydrochloride of the Wild Type Tryptophan Synthase α-Subunit of Escherichia coli and Two Mutant Proteins (Glu 49—Met or Gln)
inferredcites →https://doi.org/10.1111/j.1432-1033.1975.tb21030.xopenalex-snapshot
The Tryptophan Synthase from Escherichia coli
inferredcites →https://doi.org/10.1111/j.1749-6632.1964.tb14213.xopenalex-snapshot
DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*
inferredcites →https://doi.org/10.1126/science.1736361openalex-snapshot
Ordered Self-Assembly of Polypeptide Fragments to form Nativelike Dimeric trp Repressor
inferredcites →https://doi.org/10.1126/science.2643160openalex-snapshot
Correct Folding of Circularly Permuted Variants of a βα Barrel Enzyme in Vivo
inferredcites →https://doi.org/10.1126/science.2787053openalex-snapshot
Influence of Interior Packing and Hydrophobicity on the Stability of a Protein
inferredcites →https://doi.org/10.1146/annurev.bi.54.070185.003121openalex-snapshot
EFFECTS OF SITE-SPECIFIC AMINO ACID MODIFICATION ON PROTEIN INTERACTIONS AND BIOLOGICAL FUNCTION
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
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Mutational analysis of the BPTI folding pathway: II. Effects of aromatic → leucine substitutions on folding kinetics and thermodynamics
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Thermodynamic and Structural Compensation in “Size-switch” Core Repacking Variants of Bacteriophage T4 Lysozyme
inferred← citeshttps://doi.org/10.1016/0959-440x(93)90089-4openalex-snapshot
Protein engineering strategies in examining protein folding intermediates
inferred← citeshttps://doi.org/10.1016/bs.apcsb.2021.01.007openalex-snapshot
The concept of protein folding/unfolding and its impacts on human health
inferred← citeshttps://doi.org/10.1016/j.jmb.2007.06.018openalex-snapshot
Topology and Sequence in the Folding of a TIM Barrel Protein: Global Analysis Highlights Partitioning between Transient Off-pathway and Stable On-pathway Folding Intermediates in the Complex Folding Mechanism of a (βα)8 Barrel of Unknown Function from B. subtilis
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Structural Analysis of Kinetic Folding Intermediates for a TIM Barrel Protein, Indole-3-glycerol Phosphate Synthase, by Hydrogen Exchange Mass Spectrometry and Gō Model Simulation
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Intracellular Domain Contacts Contribute to Ecadherin Constitutive Dimerization in the Plasma Membrane
inferred← citeshttps://doi.org/10.1016/s0022-2836(02)00465-5openalex-snapshot
Thermodynamic Consequences of Burial of Polar and Non-polar Amino Acid Residues in the Protein Interior
inferred← citeshttps://doi.org/10.1016/s0022-2836(02)00737-4openalex-snapshot
A Cis-Prolyl Peptide Bond Isomerization Dominates the Folding of the Alpha Subunit of Trp Synthase, a TIM Barrel Protein
inferred← citeshttps://doi.org/10.1016/s0065-3233(00)53001-0openalex-snapshot
Autonomous protein folding units
inferred← citeshttps://doi.org/10.1016/s0065-3233(00)53004-6openalex-snapshot
Barriers in protein folding reactions
inferred← citeshttps://doi.org/10.1016/s0065-3233(00)53007-1openalex-snapshot
Folding and association of oligomeric and multimeric proteins
inferred← citeshttps://doi.org/10.1016/s0959-440x(94)90062-0openalex-snapshot
The thermodynamic effects of protein mutations
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Chapter 5 Protein folding
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An analysis of packing in the protein folding problem
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Detection of an Intermediate in the Folding of the (.beta..alpha.)8-Barrel N-(5'-Phosphoribosyl)anthranilate Isomerase from Escherichia coli
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Thermodynamic Properties of the Transition State for the Rate-Limiting Step in the Folding of the .alpha. Subunit of Tryptophan Synthase
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Urea-induced unfolding of the .alpha. subunit of tryptophan synthase: One-dimensional proton NMR evidence for residual structure near histidine-92 at high denaturant concentration
inferred← citeshttps://doi.org/10.1021/jp7117295openalex-snapshot
Crystallographic B-Factors Highlight Energetic Frustration in Aldolase Folding
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Kinetics of protein folding: The dynamics of globally connected rough energy landscapes with biases
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Tryptophan-containing α-Subunits of the Escherichia coli Tryptophan Synthase
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Unfolding Properties of Tryptophan-containing α-Subunits of the Escherichia coli Tryptophan Synthase
inferred← citeshttps://doi.org/10.1074/jbc.271.25.14754openalex-snapshot
On the Role of Helix 0 of the Tryptophan Synthetase α Chain of
inferred← citeshttps://doi.org/10.1107/s0907444900017388openalex-snapshot
Design, X-ray crystallography, molecular modelling and thermal stability studies of mutant enzymes at site 172 of 3-isopropylmalate dehydrogenase fromThermus thermophilus
inferred← citeshttps://doi.org/10.1110/ps.8.6.1200openalex-snapshot
Identifying the structural boundaries of independent folding domains in the a subunit of tryptophan synthase, a β/α barrel protein
inferred← citeshttps://doi.org/10.1110/ps.8.8.1623openalex-snapshot
The progressive development of structure and stability during the equilibrium folding of the α subunit of tryptophan synthase from Escherichia coli
inferred← citeshttps://doi.org/10.1529/biophysj.105.059147openalex-snapshot
Equilibrium and Kinetic Folding Pathways of a TIM Barrel with a Funneled Energy Landscape
inferred← citeshttps://doi.org/10.1529/biophysj.107.108068openalex-snapshot
Folding and Unfolding of γTIM Monomers and Dimers
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PON-tstab: Protein Variant Stability Predictor. Importance of Training Data Quality
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