On the public citation graph
Effects of multiple replacements at a single position on the folding and stability of dihydrofolate reductase from Escherichia coli
0 signed · 104 inferred · view as graph
Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.
Is this your work? Sign in with ORCID and put your name on the
claims that are yours.
Reference health. See whether every reference in this work resolves to a
known work and none has been retracted — and get a dated CiteStamped
badge you can embed.
What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1006/abio.1976.9999openalex-snapshot
A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding
inferredcites →https://doi.org/10.1016/0003-2697(67)90179-0openalex-snapshot
Effect of substrate decomposition on the spectrophotometric assay of dihydrofolate reductase
inferredcites →https://doi.org/10.1016/0022-2836(78)90245-0openalex-snapshot
Structure of the lysozyme from bacteriophage T4: An electron density map at 2.4 Å resolution
inferredcites →https://doi.org/10.1016/0079-6107(72)90005-3openalex-snapshot
Protein volume in solution
inferredcites →https://doi.org/10.1016/0079-6107(84)90007-5openalex-snapshot
Hydrogen bonding in globular proteins
inferredcites →https://doi.org/10.1016/s0021-9258(17)37725-6openalex-snapshot
Dihydrofolate reductase from trimethoprim-resistant Escherichia coli MB 3746 and MB 3747. Purification, amino acid composition, and some kinetic properties.
inferredcites →https://doi.org/10.1016/s0021-9258(18)33497-5openalex-snapshot
Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. I. General features and binding of methotrexate.
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)77913-7openalex-snapshot
Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium.
inferredcites →https://doi.org/10.1021/bi00280a010openalex-snapshot
Conformational stability of mixed disulfide derivatives of .beta.-lactoglobulin B
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/bi00367a015openalex-snapshot
Folding of dihydrofolate reductase 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/bi00384a004openalex-snapshot
Effect of single amino acid replacements on the folding and stability of dihydrofolate reductase from Escherichia coli
inferredcites →https://doi.org/10.1021/bi00393a048openalex-snapshot
Site-directed mutants of staphylococcal nuclease. Detection and localization by proton NMR spectroscopy of conformational changes accompanying substitutions for glutamic acid-43
inferredcites →https://doi.org/10.1021/bi00396a001openalex-snapshot
Genetic and structural analysis of the protein stability problem
inferredcites →https://doi.org/10.1021/bi00411a033openalex-snapshot
Identification of residues involved in a conformational change accompanying substitutions for glutamate-43 in staphylococcal nuclease
inferredcites →https://doi.org/10.1021/bi00507a034openalex-snapshot
Kinetics of substrate, coenzyme, and inhibitor binding to Escherichia coli dihydrofolate reductase
inferredcites →https://doi.org/10.1021/bi00635a010openalex-snapshot
Escherichia coli dihydrofolate reductase: isolation and characterization of two isozymes
inferredcites →https://doi.org/10.1021/bi00695a006openalex-snapshot
Purification and properties of Escherichia coli dihydrofolate reductase
inferredcites →https://doi.org/10.1021/bi00705a015openalex-snapshot
Growth hormone conformation and conformational equilibriums
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/10.1038/254304a0openalex-snapshot
Structural invariants in protein folding
inferredcites →https://doi.org/10.1038/320192a0openalex-snapshot
Multiple conformations of a protein demonstrated by magnetization transfer NMR spectroscopy
inferredcites →https://doi.org/10.1038/330041a0openalex-snapshot
Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme
inferredcites →https://doi.org/10.1038/334406a0openalex-snapshot
Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3
inferredcites →https://doi.org/10.1042/bj1550331openalex-snapshot
The mechanism of folding of globular proteins. Equilibria and kinetics of conformational transitions of penicillinase from Staphylococcus aureus involving a state of intermediate conformation
inferredcites →https://doi.org/10.1073/pnas.79.21.6409openalex-snapshot
Oligonucleotide-directed mutagenesis as a general and powerful method for studies of protein function.
inferredcites →https://doi.org/10.1073/pnas.84.13.4441openalex-snapshot
Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit.
inferredcites →https://doi.org/10.1111/j.1432-1033.1988.tb13844.xopenalex-snapshot
Role of tyrosine‐80 in the stability of kanamycin nucleotidyltransferase analyzed by site‐directed mutagenesis
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/10.1146/annurev.bb.17.060188.002405openalex-snapshot
Genetic Studies of Protein Stability and Mechanisms of Folding
inferredcites →https://doi.org/10.1146/annurev.bi.51.070182.002331openalex-snapshot
Specific Intermediates in the Folding Reactions of Small Proteins and the Mechanism of Protein Folding
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/(sici)1097-461x(1999)75:6<1027::aid-qua7>3.0.co;2-8openalex-snapshot
Uncovering the innate thermodynamic quantities in protein unfolding
inferred← citeshttps://doi.org/10.1002/9783527620999.ch20bopenalex-snapshot
In vitroProtein Refolding
inferred← citeshttps://doi.org/10.1002/ange.19911030404openalex-snapshot
Ribonuclease T1: Struktur, Funktion und Stabilität
inferred← citeshttps://doi.org/10.1002/anie.199103433openalex-snapshot
Ribonuclease T1: Structure, Function, and Stability
inferred← citeshttps://doi.org/10.1002/pro.5560050910openalex-snapshot
Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands
inferred← citeshttps://doi.org/10.1002/prot.340060308openalex-snapshot
A hydrophobic cluster forms early in the folding of dihydrofolate reductase
inferred← citeshttps://doi.org/10.1006/abbi.2000.1982openalex-snapshot
Functional Implications of the β-Helical Protein Fold: Differences in Chemical and Thermal Stabilities of Erwinia chrysanthemi EC16 Pectate Lyases B, C, and E
inferred← citeshttps://doi.org/10.1006/abio.2001.5301openalex-snapshot
Subtle Differences in Dissociation Rates of Interactions between Destabilized Human Carbonic Anhydrase II Mutants and Immobilized Benzenesulfonamide Inhibitors Probed by a Surface Plasmon Resonance Biosensor
inferred← citeshttps://doi.org/10.1007/978-1-4612-2406-8_14openalex-snapshot
Structure and Biologic Characteristics of Prion Protein (Scrapie Amyloid): Implications for the Safety of Naturally Derived Biologics
inferred← citeshttps://doi.org/10.1007/978-1-4757-9637-7_8openalex-snapshot
Characterization of a Transient intermediate in the Folding of Dihydrofolate Reductase
inferred← citeshttps://doi.org/10.1007/s00792-017-0928-0openalex-snapshot
Halophilic mechanism of the enzymatic function of a moderately halophilic dihydrofolate reductase from Haloarcula japonica strain TR-1
inferred← citeshttps://doi.org/10.1016/0076-6879(91)02008-wopenalex-snapshot
[6] Protein engineering in analysis of protein folding pathways and stability
inferred← citeshttps://doi.org/10.1016/0076-6879(91)02009-xopenalex-snapshot
[7] Mutatational analysis of protein folding mechanisms
inferred← citeshttps://doi.org/10.1016/0167-4838(95)00041-ropenalex-snapshot
Conformation and stability of recombinant HIV-1 capsid protein p24 (rp24)
inferred← citeshttps://doi.org/10.1016/0167-7799(91)90190-sopenalex-snapshot
Repacking protein interiors
inferred← citeshttps://doi.org/10.1016/0169-409x(90)90028-qopenalex-snapshot
Structure-stability relationships in proteins: a guide to approaches to stabilizing enzymes
inferred← citeshttps://doi.org/10.1016/0959-440x(92)90175-7openalex-snapshot
Mutational analysis of protein stability
inferred← citeshttps://doi.org/10.1016/0960-9822(92)90210-2openalex-snapshot
Mutational analysis of protein stability
inferred← citeshttps://doi.org/10.1016/0968-0004(90)90124-topenalex-snapshot
Conformational stability of globular proteins
inferred← citeshttps://doi.org/10.1016/b978-1-85166-512-9.50016-9openalex-snapshot
CONFORMATIONAL STABILITY OF GLOBULAR PROTEINS
inferred← citeshttps://doi.org/10.1016/j.bbrc.2009.12.134openalex-snapshot
Probing the roles of conserved arginine-44 of Escherichia coli dihydrofolate reductase in its function and stability by systematic sequence perturbation analysis
inferred← citeshttps://doi.org/10.1016/j.cels.2026.101681openalex-snapshot
Quantifying protein unfolding kinetics with a high-throughput microfluidic platform
inferred← citeshttps://doi.org/10.1016/j.chembiol.2011.11.009openalex-snapshot
ATP-Independent Control of Autotransporter Virulence Protein Transport via the Folding Properties of the Secreted Protein
inferred← citeshttps://doi.org/10.1016/j.jmb.2005.01.033openalex-snapshot
Probing the Interactions between the Folding Elements Early in the Folding of Escherichia coli Dihydrofolate Reductase by Systematic Sequence Perturbation Analysis
inferred← citeshttps://doi.org/10.1016/j.jmb.2005.08.054openalex-snapshot
Fine Structure Analysis of a Protein Folding Transition State; Distinguishing Between Hydrophobic Stabilization and Specific Packing
inferred← citeshttps://doi.org/10.1016/j.jmb.2008.01.005openalex-snapshot
The Fellowship of the RING: The RING–B-Box Linker Region Interacts with the RING in TRIM21/Ro52, Contains a Native Autoantigenic Epitope in Sjögren Syndrome, and is an Integral and Conserved Region in TRIM Proteins
inferred← citeshttps://doi.org/10.1016/j.jmb.2010.08.049openalex-snapshot
Investigation of an Anomalously Accelerating Substitution in the Folding of a Prototypical Two-State Protein
inferred← citeshttps://doi.org/10.1016/s0022-2836(02)01444-4openalex-snapshot
The Coordination of the Isomerization of a Conserved Non-prolyl cis Peptide Bond with the Rate-limiting Steps in the Folding of Dihydrofolate Reductase
inferred← citeshttps://doi.org/10.1016/s0065-3233(08)60335-6openalex-snapshot
Engineering the Stability and Function of Gene V Protein
inferred← citeshttps://doi.org/10.1016/s0065-3233(08)60546-xopenalex-snapshot
Molten Globule and Protein Folding
inferred← citeshttps://doi.org/10.1016/s0076-6879(04)80012-0openalex-snapshot
Circular Dichroism of Protein-Folding Intermediates
inferred← citeshttps://doi.org/10.1016/s0076-6879(98)95043-1openalex-snapshot
[12] Application of planck-benzinger relationships to biology
inferred← citeshttps://doi.org/10.1016/s0079-6603(08)00403-0openalex-snapshot
Use of Protein Engineering Techniques to Elucidate Protein Folding Pathways
inferred← citeshttps://doi.org/10.1016/s0167-4838(00)00019-4openalex-snapshot
Effect of ligand binding on the flexibility of dihydrofolate reductase as revealed by compressibility
inferred← citeshttps://doi.org/10.1016/s0167-4838(98)00283-0openalex-snapshot
Characterization of a molten globule state of bovine carbonic anhydrase III: loss of asymmetrical environment of the aromatic residues has a profound effect on both the near- and far-UV CD spectrum
inferred← citeshttps://doi.org/10.1016/s1874-5989(99)80007-6openalex-snapshot
Chapter 5 Protein folding
inferred← citeshttps://doi.org/10.1017/s0033583500002845openalex-snapshot
An analysis of packing in the protein folding problem
inferred← citeshttps://doi.org/10.1017/s0033583500004674openalex-snapshot
Mutational studies of protein structures and their stabilities
inferred← citeshttps://doi.org/10.1021/bi00003a036openalex-snapshot
Contribution of Individual Tryptophan Residues to the Fluorescence Spectrum of Native and Denatured Forms of Human Carbonic Anhydrase II
inferred← citeshttps://doi.org/10.1021/bi00027a010openalex-snapshot
Mapping the Folding Intermediate of Human Carbonic Anhydrase II. Probing Substructure by Chemical Reactivity and Spin and Fluorescence Labeling of Engineered Cysteine Residues
inferred← citeshttps://doi.org/10.1021/bi00072a011openalex-snapshot
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
inferred← citeshttps://doi.org/10.1021/bi00082a015openalex-snapshot
In vitro protein engineering using synthetic tRNAAla with different anticodons
inferred← citeshttps://doi.org/10.1021/bi00093a013openalex-snapshot
Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala .fwdarw. Ser and Val .fwdarw. Thr substitutions in T4 lysozyme
inferred← citeshttps://doi.org/10.1021/bi00132a025openalex-snapshot
Structural and energetic consequences of disruptive mutations in a protein core
inferred← citeshttps://doi.org/10.1021/bi00140a001openalex-snapshot
Intramolecular catalysis of a proline isomerization reaction in the folding of dihydrofolate reductase
inferred← citeshttps://doi.org/10.1021/bi00184a019openalex-snapshot
19F NMR Spectroscopy of [6-19F]Tryptophan-Labeled Escherichia coli Dihydrofolate Reductase: Equilibrium Folding and Ligand Binding Studies
inferred← citeshttps://doi.org/10.1021/bi00216a038openalex-snapshot
Correlation between mutational destabilization of phage T4 lysozyme and increased unfolding rates
inferred← citeshttps://doi.org/10.1021/bi00245a005openalex-snapshot
Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy
inferred← citeshttps://doi.org/10.1021/bi00245a020openalex-snapshot
Effects of point mutations in a hinge region on the stability, folding, and enzymic activity of Escherichia coli dihydrofolate reductase
inferred← citeshttps://doi.org/10.1021/bi00255a005openalex-snapshot
Development of Nonpolar Surfaces in the Folding of Escherichia coli Dihydrofolate Reductase Detected by 1-Anilinonaphthalene-8-sulfonate Binding
inferred← citeshttps://doi.org/10.1021/bi00462a019openalex-snapshot
pH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1
inferred← citeshttps://doi.org/10.1021/bi00470a021openalex-snapshot
Denaturant-dependent folding of bovine pancreatic trypsin inhibitor mutants with two intact disulfide bonds
inferred← citeshttps://doi.org/10.1021/la0002738openalex-snapshot
Adsorption of Human Carbonic Anhydrase II Variants to Silica Nanoparticles Occur Stepwise: Binding Is Followed by Successive Conformational Changes to a Molten-Globule-like State
inferred← citeshttps://doi.org/10.1038/340122a0openalex-snapshot
Mapping the transition state and pathway of protein folding by protein engineering
inferred← citeshttps://doi.org/10.1046/j.1432-1327.1999.00812.xopenalex-snapshot
Stability and physicochemical properties of the bovine brain phosphatidylethanolamine‐binding protein
inferred← citeshttps://doi.org/10.1073/pnas.1610272113openalex-snapshot
Quantitative determination of ribosome nascent chain stability
inferred← citeshttps://doi.org/10.1073/pnas.87.12.4413openalex-snapshot
Refolding of Escherichia coli dihydrofolate reductase: sequential formation of substrate binding sites.
inferred← citeshttps://doi.org/10.1073/pnas.88.5.1706openalex-snapshot
Energetics of repacking a protein interior.
inferred← citeshttps://doi.org/10.1073/pnas.93.18.9425openalex-snapshot
A thermodynamic coupling mechanism for GroEL-mediated unfolding.
inferred← citeshttps://doi.org/10.1074/jbc.m001843200openalex-snapshot
The Neuropeptide Processing Enzyme EC 3.4.24.15 Is Modulated by Protein Kinase A Phosphorylation
inferred← citeshttps://doi.org/10.1093/oxfordjournals.molbev.a040676openalex-snapshot
Temporal and topological clustering of diverged residues among enterobacterial dihydrofolate reductases.
inferred← citeshttps://doi.org/10.1093/protein/gzj017openalex-snapshot
The relationship between chain connectivity and domain stability in the equilibrium and kinetic folding mechanisms of dihydrofolate reductase from E.coli
inferred← citeshttps://doi.org/10.1101/677617openalex-snapshot
Intramolecular Communication and Allosteric Sites in Enzymes Unraveled by Time-Dependent Linear Response Theory
inferred← citeshttps://doi.org/10.1110/ps.051870506openalex-snapshot
On the precision of experimentally determined protein folding rates and ϕ‐values
inferred← citeshttps://doi.org/10.1110/ps.062230106openalex-snapshot
Methods for the accurate estimation of confidence intervals on protein folding φ‐values
inferred← citeshttps://doi.org/10.1126/science.1359644openalex-snapshot
Prevention of Protein Denaturation Under Heat Stress by the Chaperonin Hsp60
inferred← citeshttps://doi.org/10.2139/ssrn.5113797openalex-snapshot
Quantifying Protein Unfolding Kinetics with a High-Throughput Microfluidic Platform
Editorial review for independent work. ICSAC — the Institute for Complexity
Science and Advanced Computing — runs a structured editorial panel for researchers
publishing outside journals, and publishes on CiteStamp rails. Submission is free
and goes through ORCID: icsacinstitute.org/submit.