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s-(2,4-dinitrophenyl)glutathione and dithionitrobenzoic acid

s-(2,4-dinitrophenyl)glutathione has been researched along with dithionitrobenzoic acid in 3 studies

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's2 (66.67)18.2507
2000's0 (0.00)29.6817
2010's1 (33.33)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Akerboom, TP; Bartosz, G; Sies, H1
Mantle, TJ; Phillips, MF1
Canals, A; Coll, M; Costa, M; Mantle, TJ; McManus, G1

Other Studies

3 other study(ies) available for s-(2,4-dinitrophenyl)glutathione and dithionitrobenzoic acid

ArticleYear
Low- and high-Km transport of dinitrophenyl glutathione in inside out vesicles from human erythrocytes.
    Biochimica et biophysica acta, 1992, Jan-10, Volume: 1103, Issue:1

    Topics: Biological Transport; Chloromercuribenzoates; Dithionitrobenzoic Acid; Erythrocyte Membrane; Ethylmaleimide; Fluorides; Glutathione; Glutathione Disulfide; Hot Temperature; Humans; Kinetics; Substrate Specificity; Vanadates

1992
Inactivation of mouse liver glutathione S-transferase YfYf (Pi class) by ethacrynic acid and 5,5'-dithiobis-(2-nitrobenzoic acid).
    The Biochemical journal, 1993, Aug-15, Volume: 294 ( Pt 1)

    Topics: Amino Acid Sequence; Animals; Dithionitrobenzoic Acid; Ethacrynic Acid; Glutathione; Glutathione Transferase; Hydrogen-Ion Concentration; Isoenzymes; Kinetics; Liver; Mice; Molecular Sequence Data; Peptide Fragments; Peptide Mapping; Sulfhydryl Compounds

1993
Site-directed mutagenesis of mouse glutathione transferase P1-1 unlocks masked cooperativity, introduces a novel mechanism for 'ping pong' kinetic behaviour, and provides further structural evidence for participation of a water molecule in proton abstract
    The FEBS journal, 2011, Volume: 278, Issue:2

    Topics: Amino Acid Substitution; Animals; Biocatalysis; Catalytic Domain; Crystallography, X-Ray; Cysteine; Dinitrochlorobenzene; Dithionitrobenzoic Acid; Glutathione; Glutathione S-Transferase pi; Hydrogen-Ion Concentration; Kinetics; Mice; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; Protein Binding; Protein Conformation; Protons; Recombinant Proteins; Water

2011