Compounds > methyl methanethiosulfonate
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methyl methanethiosulfonate and nadp

methyl methanethiosulfonate has been researched along with nadp in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19902 (40.00)18.7374
1990's1 (20.00)18.2507
2000's2 (40.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Claiborne, A; Miller, H1
Chung, H; Fried, J; Jarabak, J1
Paglia, DE; Valentine, WN1
Andricopulo, AD; Arscott, LD; Becker, K; Davioud-Charvet, E; Giegel, D; Kenyon, GL; McLeish, MJ; Müller, S; Schirmer, RH; Veine, DM; Williams, CH1
González-Segura, L; Mújica-Jiménez, C; Muñoz-Clares, RA; Velasco-García, R; Zaldívar-Machorro, VJ1

Other Studies

5 other study(ies) available for methyl methanethiosulfonate and nadp

ArticleYear
Peroxide modification of monoalkylated glutathione reductase. Stabilization of an active-site cysteine-sulfenic acid.
    The Journal of biological chemistry, 1991, Oct-15, Volume: 266, Issue:29

    Topics: Alkylation; Binding Sites; Chromatography, Gel; Dithiothreitol; Electrophoresis, Polyacrylamide Gel; Glutathione Reductase; Hydrogen Peroxide; Iodoacetamide; Methyl Methanesulfonate; NADP; Oxidation-Reduction; Phenylmercuric Acetate; Saccharomyces cerevisiae

1991
Irreversible inhibition of the human placental NADP-linked 15-hydroxyprostaglandin dehydrogenase/9-ketoprostaglandin reductase by glutathione thiosulfonate.
    Prostaglandins, 1987, Volume: 33, Issue:3

    Topics: Binding Sites; Enzyme Inhibitors; Glutathione; Glutathione Disulfide; Humans; Hydroxyprostaglandin Dehydrogenases; Methyl Methanesulfonate; NADP; Oxidation-Reduction; Placenta; Prostaglandins A; Time Factors

1987
Effect of chemical modification of sulfhydryl groups of human erythrocyte enzymes.
    American journal of hematology, 1981, Volume: 11, Issue:2

    Topics: Catalysis; Erythrocytes; Glucosephosphate Dehydrogenase; Hot Temperature; Hydrogen-Ion Concentration; L-Lactate Dehydrogenase; Methyl Methanesulfonate; NADP; Phosphopyruvate Hydratase; Sulfhydryl Compounds

1981
Mechanism-based inactivation of thioredoxin reductase from Plasmodium falciparum by Mannich bases. Implication for cytotoxicity.
    Biochemistry, 2003, Nov-18, Volume: 42, Issue:45

    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
Disulfiram irreversibly aggregates betaine aldehyde dehydrogenase--a potential target for antimicrobial agents against Pseudomonas aeruginosa.
    Biochemical and biophysical research communications, 2006, Mar-10, Volume: 341, Issue:2

    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