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Effect of single amino acid substitutions on the thermal stability of the .alpha. subunit of tryptophan synthase
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Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1016/0003-9861(68)90194-xopenalex-snapshot
Immunochemical comparisons of mutant and wild-type α-subunits of tryptophan synthetase
inferredcites →https://doi.org/10.1016/0005-2795(77)90166-0openalex-snapshot
Stability of phage T4 lysozymes I. Native properties and thermal stability of wild type and two mutant lysozymes
inferredcites →https://doi.org/10.1016/0021-9614(75)90079-8openalex-snapshot
Precision scanning microcalorimeter for the study of liquids
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A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study
inferredcites →https://doi.org/10.1016/0022-2836(74)90353-2openalex-snapshot
Selection for new amino acids at position 211 of the tryptophan synthetase α chain of Escherichia coli
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)45013-8openalex-snapshot
Tryptophan Synthetase α Chain Positions Affected by Mutations near the Ends of the Genetic Map of trpA of Escherichia coli
inferredcites →https://doi.org/10.1016/s0021-9258(19)45611-1openalex-snapshot
Amino Acid Sequences of Fifty Residues from the Amino Termini of the Tryptophan Synthetase α Chains of Several Enterobacteria
inferredcites →https://doi.org/10.1016/s0076-6879(62)05315-xopenalex-snapshot
[107] Enzymes involved in the biosynthesis of tryptophan
inferredcites →https://doi.org/10.1021/bi00574a010openalex-snapshot
Thermodynamics of the denaturation of lysozyme in alcohol-water mixtures
inferredcites →https://doi.org/10.1038/267274a0openalex-snapshot
Effect of a single amino acid substitution on stability of conformation of a protein
inferredcites →https://doi.org/10.1038/277667a0openalex-snapshot
Molecular basis of thermostability in the lysozyme from bacteriophage T4
inferredcites →https://doi.org/10.1073/pnas.57.2.296openalex-snapshot
THE COMPLETE AMINO ACID SEQUENCE OF THE TRYPTOPHAN SYNTHETASE A PROTEIN (α SUBUNIT) AND ITS COLINEAR RELATIONSHIP WITH THE GENETIC MAP OF THE A GENE
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/10.1126/science.125.3250.691openalex-snapshot
Reductive Cleavage of Disulfide Bridges in Ribonuclease
inferredcites →https://doi.org/10.1126/science.181.4096.223openalex-snapshot
Principles that Govern the Folding of Protein Chains
inferredcites →https://doi.org/10.1128/jb.117.2.444-448.1974openalex-snapshot
Structural Interactions Between Amino Acid Residues at Positions 22 and 211 in the Tryptophan Synthetase Alpha Chain of Escherichia coli
inferredcites →https://doi.org/10.3109/10409237509102551openalex-snapshot
The Stability of Globular Protein
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.2139/ssrn.3231858openalex-extracted
Coordinated Network Changes Across the Catalytic Cycle of Alpha Tryptophan Synthase
inferred← citeshttps://doi.org/10.1002/9780470123102.ch3openalex-snapshot
Structural Basis for Catalysis by Tryptophan Synthase
inferred← citeshttps://doi.org/10.1002/9781118935682.ch14openalex-snapshot
Protein Characterization by Thermal Property Measurement
inferred← citeshttps://doi.org/10.1002/jcb.240290306openalex-snapshot
Increasing and decreasing protein stability: Effects of revertant substitutions on the thermal denaturation of phage λ repressor
inferred← citeshttps://doi.org/10.1002/jcb.240290406openalex-snapshot
Dissecting the roles of individual interactions in protein stability: Lessons from a circularized protein
inferred← citeshttps://doi.org/10.1002/pro.5560020408openalex-snapshot
Thermal unfolding of staphylococcal nuclease and several mutant forms thereof studied by differential scanning calorimetry
inferred← citeshttps://doi.org/10.1002/prot.340010406openalex-snapshot
Proteases of enhanced stability: Characteization of a thermostable variant of subtilisin
inferred← citeshttps://doi.org/10.1002/prot.340090203openalex-snapshot
Role of conserved proline residues in stabilizing tryptophan synthase α subunit: Analysis by mutants with alanine or glycine
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Stabilization Energies of Protein Conformation
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How Nature Engineers Protein (Thermo) Stability
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Differential Scanning Calorimetry Applications to Protein Solutions
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The problem of the stability of globular proteins
inferred← citeshttps://doi.org/10.1007/bf01959114openalex-snapshot
Calorimetric studies on monomeric and polymeric actin
inferred← citeshttps://doi.org/10.1007/bf02660210openalex-snapshot
Protein conformations and their stability
inferred← citeshttps://doi.org/10.1016/0003-9861(85)90380-7openalex-snapshot
Structural analyses of various Cu2+, Zn2+-superoxide dismutases by differential scanning calorimetry and Raman spectroscopy
inferred← citeshttps://doi.org/10.1016/0003-9861(91)90280-vopenalex-snapshot
Effect of single amino acid substitutions at positions 49 and 60 on the thermal unfolding of the tryptophan synthase α subunit from Salmonella typhimurium
inferred← citeshttps://doi.org/10.1016/0003-9861(92)90047-zopenalex-snapshot
Thermal stabilities of mutant Escherichia coli tryptophan synthase α subunits
inferred← citeshttps://doi.org/10.1016/0003-9861(92)90479-gopenalex-snapshot
Crystallization and preliminary crystallographic analysis of a thermostable mutant of kanamycin nucleotidyltransferase
inferred← citeshttps://doi.org/10.1016/0022-2836(80)90335-6openalex-snapshot
Role of the environment in the refolding of reduced pancreatic trypsin inhibitor
inferred← citeshttps://doi.org/10.1016/0022-2836(84)90474-1openalex-snapshot
Thermodynamic stability and point mutations of bacteriophage T4 lysozyme
inferred← citeshttps://doi.org/10.1016/0065-227x(84)90004-2openalex-snapshot
Pathways and mechanisms of protein folding
inferred← citeshttps://doi.org/10.1016/0065-227x(85)90028-0openalex-snapshot
Effect of amino acid substitutions on conformational stability of a protein
inferred← citeshttps://doi.org/10.1016/0076-6879(86)31044-9openalex-snapshot
[13]Mutational analysis of protein folding pathways: The P22 tailspike endorhamnosidase
inferred← citeshttps://doi.org/10.1016/0167-4838(82)90406-xopenalex-snapshot
Stability of dehydrogenases III. malate dehydrogenases
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Thermostabilization of Bacillus caldolyticus Glutamine Synthetase by Intrinsic and Extrinsic Factors
inferred← citeshttps://doi.org/10.1016/b978-0-444-42062-6.50017-0openalex-snapshot
10.1016/b978-0-444-42062-6.50017-0
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Influence of specific contacts on the stability and structure of proteins. Theory for the perturbation of a harmonic system
inferred← citeshttps://doi.org/10.1016/s0021-9258(17)32629-7openalex-snapshot
Thermal inactivation of tryptophan synthase. Stabilization by protein-protein interaction and protein-ligand interaction.
inferred← citeshttps://doi.org/10.1016/s0021-9258(18)54334-9openalex-snapshot
Structural and functional consequences of amino acid substitutions in the second conserved loop of Escherichia coli adenylate kinase.
inferred← citeshttps://doi.org/10.1016/s0021-9258(18)90617-4openalex-snapshot
Comparison of active mutants and wild-type aspartate transcarbamoylase of Escherichia coli.
inferred← citeshttps://doi.org/10.1016/s0021-9258(19)69460-3openalex-snapshot
Differential scanning calorimetry of cytoplasmic aspartate transaminase.
inferred← citeshttps://doi.org/10.1016/s0021-9258(19)69732-2openalex-snapshot
A mutant thioredoxin from Escherichia coli tsnC 7007 that is nonfunctional as subunit of phage T7 DNA polymerase.
inferred← citeshttps://doi.org/10.1016/s1043-4526(08)60066-2openalex-snapshot
Protein and Enzyme Stability: Structural, Thermodynamic, and Experimental Aspects
inferred← citeshttps://doi.org/10.1021/acs.chemrev.1c00857openalex-snapshot
Mass Spectrometry Methods for Measuring Protein Stability
inferred← citeshttps://doi.org/10.1021/acs.chemrev.2c00600openalex-snapshot
Ion Mobility Mass Spectrometry (IM-MS) for Structural Biology: Insights Gained by Measuring Mass, Charge, and Collision Cross Section
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Dynamics of a monomeric insulin analog: Testing the molten-globule hypothesis
inferred← citeshttps://doi.org/10.1021/bi00186a040openalex-snapshot
Thermodynamic Properties of the Transition State for the Rate-Limiting Step in the Folding of the .alpha. Subunit of Tryptophan Synthase
inferred← citeshttps://doi.org/10.1021/bi00275a019openalex-snapshot
Effect of a single amino acid substitution on the folding of the .alpha. subunit of tryptophan synthase
inferred← citeshttps://doi.org/10.1021/bi00280a010openalex-snapshot
Conformational stability of mixed disulfide derivatives of .beta.-lactoglobulin B
inferred← citeshttps://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
inferred← citeshttps://doi.org/10.1021/bi00370a032openalex-snapshot
Guanidine hydrochloride-induced equilibrium unfolding of mutant forms of iso-1-cytochrome c with replacement of proline-71
inferred← citeshttps://doi.org/10.1021/bi00370a033openalex-snapshot
Folding/unfolding kinetics of mutant forms of iso-1-cytochrome c with replacement of proline-71
inferred← citeshttps://doi.org/10.1021/bi00382a002openalex-snapshot
Protein engineering of subtilisin BPN': enhanced stabilization through the introduction of two cysteines to form a disulfide bond
inferred← citeshttps://doi.org/10.1038/nbt0190-27openalex-snapshot
The Tryptophan Synthase Multienzyme Complex: Exploring Structure-Function Relationships with X-Ray Crystallography and Mutagenesis
inferred← citeshttps://doi.org/10.1063/1.4947493openalex-snapshot
High-quality Thermodynamic Data on the Stability Changes of Proteins Upon Single-site Mutations
inferred← citeshttps://doi.org/10.1073/pnas.86.2.496openalex-snapshot
Dramatic thermostabilization of yeast iso-1-cytochrome c by an asparagine----isoleucine replacement at position 57.
inferred← citeshttps://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
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PROTEIN THERMOSTABILITY.
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Calorimetric study of tryptophan synthase α‐subunit and two mutant proteins
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Thermal denaturation of human somatotropin, human choriomammotropin and ovine prolactin
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Thermal denaturation of tryptophan synthase α‐subunit
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Folding of thermolysin fragments
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Genetic lesions involved in temperature sensitivity of the src gene products of four Rous sarcoma virus mutants
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Response of Tropical Horticultural Commodities To Insect Disinfestation Treatments.
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