methyl methanethiosulfonate has been researched along with dithionitrobenzoic acid in 21 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 8 (38.10) | 18.7374 |
| 1990's | 7 (33.33) | 18.2507 |
| 2000's | 6 (28.57) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Atkinson, T; Gore, MG; Scawen, MD; Spencer, P | 1 |
| Beinert, H; Emptage, MH; Kennedy, MC; Spoto, G | 1 |
| Van Etten, RL; Waheed, A | 1 |
| Alvear, M; Cardemil, E; Jabalquinto, AM | 1 |
| Daly, TJ; Matthews, KS; Olson, JS | 1 |
| Smith, S; Witkowski, A | 1 |
| De Bruyne, CK; Kersters-Hilderson, H; Lippens, M; Van Doorslaer, E | 1 |
| Franson, RC; Kyger, EM | 1 |
| Gavilanes, F; Peterson, D; Schirch, L | 1 |
| Blättler, WA; Collinson, AR; Singh, R | 1 |
| Hou, LX; Vollmer, S | 1 |
| Patel, MA; Salleh, HM; Woodard, RW | 1 |
| Ha, JH; Loh, SN | 1 |
| Cabrera, N; de Gómez-Puyou, M; Garza-Ramos, G; Gómez-Puyou, A; Maldonado, E; Moreno, A; Perez-Montfort, R; Soriano-García, M | 1 |
| Alcántara, GH; de Gómez-Puyou, MT; Gao, XG; Garza-Ramos, G; Gómez-Puyou, A; Maldonado, E; Pérez-Montfort, R; Reyes-Vivas, H | 1 |
| Alam, SL; Butler, MC; Feng, Z; Loh, SN | 1 |
| Andricopulo, AD; Arscott, LD; Becker, K; Davioud-Charvet, E; Giegel, D; Kenyon, GL; McLeish, MJ; Müller, S; Schirmer, RH; Veine, DM; Williams, CH | 1 |
| Britto, PJ; Knipling, L; McPhie, P; Wolff, J | 1 |
| González-Segura, L; Mújica-Jiménez, C; Muñoz-Clares, RA; Velasco-García, R; Zaldívar-Machorro, VJ | 1 |
| Hynson, RM; Mathews, FS; Schuman Jorns, M | 1 |
| Carvajal, K; De la Mora-De la Mora, I; Enriquez-Flores, S; Gutierrez-Castrellon, P; Hernandez-Alcantara, G; Lopez-Velazquez, G; Reyes-Vivas, H; Rodriguez-Romero, A | 1 |
21 other study(ies) available for methyl methanethiosulfonate and dithionitrobenzoic acid
| Article | Year |
|---|---|
The identification of a structurally important cysteine residue in the glycerol dehydrogenase from Bacillus stearothermophilus.
Topics: Chemical Phenomena; Chemistry; Chromatography, High Pressure Liquid; Cobalt; Cysteine; Diethyl Pyrocarbonate; Dithionitrobenzoic Acid; Geobacillus stearothermophilus; Histidine; Iodoacetates; Iodoacetic Acid; Kinetics; Macromolecular Substances; Methyl Methanesulfonate; Molecular Weight; Peptide Fragments; Sugar Alcohol Dehydrogenases; Tritium; Trypsin; Zinc | 1991 |
The active site sulfhydryl of aconitase is not required for catalytic activity.
Topics: Acetophenones; Aconitate Hydratase; Binding Sites; Dithionitrobenzoic Acid; Electron Spin Resonance Spectroscopy; Ethylmaleimide; Kinetics; Methyl Methanesulfonate; Sulfhydryl Reagents | 1988 |
Sulfhydryl groups of rabbit liver arylsulfatase A.
Topics: Animals; Cerebroside-Sulfatase; Chromatography, Gel; Dithionitrobenzoic Acid; Fluorescent Dyes; Hydrogen-Ion Concentration; Hydroxymercuribenzoates; Liver; Methyl Methanesulfonate; Naphthalenesulfonates; Phenylmercury Compounds; Rabbits; Spectrometry, Fluorescence; Sulfatases; Sulfhydryl Compounds; Time Factors | 1985 |
Inactivation of chicken liver mevalonate 5-diphosphate decarboxylase by sulfhydryl-directed reagents: evidence of a functional dithiol.
Topics: Adenosine Triphosphate; Animals; Arsenicals; Carboxy-Lyases; Chickens; Dithionitrobenzoic Acid; Dithiothreitol; Enzyme Activation; Hydrogen-Ion Concentration; Kinetics; Liver; Methyl Methanesulfonate; Mevalonic Acid; Sulfhydryl Reagents; Toluene | 1989 |
Formation of mixed disulfide adducts at cysteine-281 of the lactose repressor protein affects operator and inducer binding parameters.
Topics: Cysteine; Cystine; Dansyl Compounds; Disulfides; Dithionitrobenzoic Acid; Escherichia coli; Isopropyl Thiogalactoside; Kinetics; Methyl Methanesulfonate; Nitrobenzoates; Operator Regions, Genetic; Protein Binding; Repressor Proteins; Transcription Factors | 1986 |
Inhibition of the functional interaction between fatty acid synthetase and thioesterase II by modification of a single cysteine thiol on the thioesterase.
Topics: Animals; Binding Sites; Chemical Phenomena; Chemistry; Cysteine; Dithionitrobenzoic Acid; Fatty Acid Synthases; Female; Hydrolysis; Kinetics; Methyl Methanesulfonate; Protein Binding; Rats; Sulfhydryl Compounds; Thiolester Hydrolases | 1985 |
The pH dependence and group modification of beta-D-xylosidase from Bacillus pumilus: evidence for sulfhydryl and histidyl groups.
Topics: Allosteric Site; Bacillus; Catalysis; Chemical Phenomena; Chemistry; Diethyl Pyrocarbonate; Dithionitrobenzoic Acid; Glycoside Hydrolases; Histidine; Hydrogen-Ion Concentration; Kinetics; Methyl Methanesulfonate; Protein Binding; Sulfhydryl Compounds; Xylosidases | 1984 |
Nonspecific inhibition of enzymes by p-bromophenacyl bromide. Inhibition of human platelet phospholipase C and modification of sulfhydryl groups.
Topics: Acetophenones; Blood Platelets; Cysteine; Cytosol; Dithionitrobenzoic Acid; Humans; Kinetics; Methyl Methanesulfonate; Phospholipases; Sulfhydryl Compounds; Type C Phospholipases | 1984 |
Methyl methanethiosulfonate as an active site probe of serine hydroxymethyltransferase.
Topics: Amino Acid Sequence; Animals; Binding Sites; Cytosol; Dithionitrobenzoic Acid; Glycine Hydroxymethyltransferase; Kinetics; Liver; Methyl Methanesulfonate; Peptide Fragments; Rabbits; Spectrophotometry; Transferases; Trypsin | 1982 |
Assay for thiols based on reactivation of papain.
Topics: Animals; Binding Sites; Cysteine; Disulfides; Dithionitrobenzoic Acid; Edetic Acid; Fabaceae; Fructose-Bisphosphate Aldolase; Indicators and Reagents; Kinetics; Methyl Methanesulfonate; Muscle, Skeletal; Oxidation-Reduction; Papain; Plants, Medicinal; Proteins; Rabbits; Sensitivity and Specificity; Serum Albumin, Bovine; Spectrophotometry; Sulfhydryl Compounds; Urease | 1995 |
The activity of S-thiomethyl modified creatine kinase is due to the regeneration of free thiol at the active site.
Topics: Animals; Binding Sites; Creatine Kinase; Dithionitrobenzoic Acid; Enzyme Activation; Methyl Methanesulfonate; Muscles; Rabbits; Sulfhydryl Compounds | 1994 |
Essential cysteines in 3-deoxy-D-manno-octulosonic acid 8-phosphate synthase from Escherichia coli: analysis by chemical modification and site-directed mutagenesis.
Topics: Aldehyde-Lyases; Base Sequence; Binding Sites; Cysteine; Dithionitrobenzoic Acid; Enzyme Inhibitors; Escherichia coli; Methyl Methanesulfonate; Molecular Sequence Data; Pentosephosphates; Phosphoenolpyruvate; Recombinant Proteins; Structure-Activity Relationship; Sulfhydryl Reagents | 1996 |
Changes in side chain packing during apomyoglobin folding characterized by pulsed thiol-disulfide exchange.
Topics: Amino Acids, Sulfur; Apoproteins; Cysteine; Cystine; Disulfides; Dithionitrobenzoic Acid; Flow Injection Analysis; Kinetics; Methyl Methanesulfonate; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; Myoglobin; Protein Denaturation; Protein Engineering; Protein Folding; Spectrometry, Fluorescence; Sulfhydryl Compounds; Sulfhydryl Reagents | 1998 |
Differences in the intersubunit contacts in triosephosphate isomerase from two closely related pathogenic trypanosomes.
Topics: Amino Acid Sequence; Animals; Binding Sites; Crystallography, X-Ray; Dimerization; Dithionitrobenzoic Acid; Humans; Methyl Methanesulfonate; Models, Molecular; Molecular Sequence Data; Protein Conformation; Protein Structure, Secondary; Recombinant Proteins; Sequence Alignment; Sulfhydryl Reagents; Triose-Phosphate Isomerase; Trypanosoma brucei brucei; Trypanosoma cruzi | 1998 |
Derivatization of the interface cysteine of triosephosphate isomerase from Trypanosoma brucei and Trypanosoma cruzi as probe of the interrelationship between the catalytic sites and the dimer interface.
Topics: Animals; Catalysis; Cysteine; Dimerization; Dithionitrobenzoic Acid; Enzyme Activation; Enzyme Inhibitors; Glyceraldehyde 3-Phosphate; Glycolates; Methyl Methanesulfonate; Mutagenesis, Site-Directed; Serine; Substrate Specificity; Sulfhydryl Reagents; Triose-Phosphate Isomerase; Trypanosoma brucei brucei; Trypanosoma cruzi | 1999 |
On the nature of conformational openings: native and unfolded-state hydrogen and thiol-disulfide exchange studies of ferric aquomyoglobin.
Topics: Amides; Animals; Circular Dichroism; Cysteine; Disulfides; Dithionitrobenzoic Acid; Guanidine; Hydrogen; Kinetics; Methyl Methanesulfonate; Models, Molecular; Mutation; Myoglobin; Protein Conformation; Protein Folding; Sulfhydryl Compounds; Thermodynamics; Whales | 2001 |
Mechanism-based inactivation of thioredoxin reductase from Plasmodium falciparum by Mannich bases. Implication for cytotoxicity.
Topics: Alkylating Agents; Animals; Dithionitrobenzoic Acid; Dose-Response Relationship, Drug; Enzyme Inhibitors; Glutathione; Glutathione Reductase; Humans; Hydrogen-Ion Concentration; Kinetics; Mannich Bases; Methyl Methanesulfonate; Models, Chemical; NADP; Oxidation-Reduction; Plasmodium falciparum; Propiophenones; Thioredoxin-Disulfide Reductase | 2003 |
Thiol-disulphide interchange in tubulin: kinetics and the effect on polymerization.
Topics: 2,2'-Dipyridyl; Adenosine Triphosphate; Amino Acid Sequence; Biopolymers; Cysteine; Disulfides; Dithionitrobenzoic Acid; Guanosine Diphosphate; Guanosine Triphosphate; Kinetics; Methyl Methanesulfonate; Molecular Structure; Nitrobenzoates; Protein Denaturation; Sulfhydryl Compounds; Tubulin | 2005 |
Disulfiram irreversibly aggregates betaine aldehyde dehydrogenase--a potential target for antimicrobial agents against Pseudomonas aeruginosa.
Topics: Alanine; Anti-Infective Agents; Betaine-Aldehyde Dehydrogenase; Binding Sites; Catalysis; Chromatography; Cysteine; Disulfiram; Dithionitrobenzoic Acid; Enzyme Inhibitors; Glutathione; Kinetics; Methyl Methanesulfonate; Models, Chemical; Mutagenesis, Site-Directed; Mutation; NADP; Protein Conformation; Protein Structure, Quaternary; Proteins; Pseudomonas aeruginosa; Sulfhydryl Compounds; Temperature; Time Factors | 2006 |
Identification of a stable flavin-thiolate adduct in heterotetrameric sarcosine oxidase.
Topics: Dithionitrobenzoic Acid; Flavin Mononucleotide; Methyl Methanesulfonate; Models, Molecular; Protein Structure, Quaternary; Pseudomonas; Sarcosine Oxidase; Sulfhydryl Compounds; Sulfides; Sulfites | 2006 |
Species-specific inhibition of Giardia lamblia triosephosphate isomerase by localized perturbation of the homodimer.
Topics: Animals; Cysteine; Dimerization; Dithionitrobenzoic Acid; Enzyme Stability; Giardia lamblia; Hot Temperature; Methyl Methanesulfonate; Models, Molecular; Protein Structure, Secondary; Protozoan Proteins; Triose-Phosphate Isomerase | 2008 |