Compounds > cysteine

cysteine and phosphoglycolate

cysteine has been researched along with phosphoglycolate in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19901 (20.00)18.7374
1990's2 (40.00)18.2507
2000's2 (40.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Blouquit, Y; Calvin, MC; Prome, D; Prome, JC; Rosa, J; Rosa, R1
Arous, N; Craescu, CT; Garel, MC; Ravel, P; Rosa, J1
Alcántara, GH; de Gómez-Puyou, MT; Gao, XG; Garza-Ramos, G; Gómez-Puyou, A; Maldonado, E; Pérez-Montfort, R; Reyes-Vivas, H1
Cabrera, N; de Gómez-Puyou, MT; Gómez-Puyou, A; Hernández-Alcantara, G; López-Velazquez, G; Pérez-Montfort, R; Reyes-Vivas, H1
Chánez-Cárdenas, ME; González-Mondragón, E; Hernández-Arana, A; Pérez-Montfort, R; Saavedra, E; Zubillaga, RA1

Other Studies

5 other study(ies) available for cysteine and phosphoglycolate

ArticleYear
Isolation, characterization, and structure of a mutant 89 Arg----Cys bisphosphoglycerate mutase. Implication of the active site in the mutation.
    The Journal of biological chemistry, 1989, May-15, Volume: 264, Issue:14

    Topics: Amino Acid Sequence; Animals; Arginine; Binding Sites; Bisphosphoglycerate Mutase; Chromatography, High Pressure Liquid; Cysteine; Drug Stability; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Glyceric Acids; Glycolates; Hot Temperature; Humans; Immunoassay; Kinetics; Molecular Sequence Data; Molecular Weight; Mutation; Nucleic Acid Hybridization; Phosphoglycerate Mutase; Phosphotransferases; Trypsin

1989
Critical role of human bisphosphoglycerate mutase Cys22 in the phosphatase activator-binding site.
    The Journal of biological chemistry, 1997, May-30, Volume: 272, Issue:22

    Topics: Binding Sites; Bisphosphoglycerate Mutase; Circular Dichroism; Cysteine; Escherichia coli; Glycolates; Humans; Phosphoric Monoester Hydrolases; Phosphorylation; Structure-Activity Relationship; Substrate Specificity

1997
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.
    Biochemistry, 1999, Mar-30, Volume: 38, Issue:13

    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
Factors that control the reactivity of the interface cysteine of triosephosphate isomerase from Trypanosoma brucei and Trypanosoma cruzi.
    Biochemistry, 2001, Mar-13, Volume: 40, Issue:10

    Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Cysteine; Dimerization; Enzyme Activation; Enzyme Inhibitors; Glutamic Acid; Glutamine; Glycolates; Hydrogen-Ion Concentration; Leishmania mexicana; Methyl Methanesulfonate; Molecular Sequence Data; Mutagenesis, Site-Directed; Peptide Fragments; Proline; Protein Structure, Tertiary; Triose-Phosphate Isomerase; Trypanosoma brucei brucei; Trypanosoma cruzi

2001
Conserved cysteine 126 in triosephosphate isomerase is required not for enzymatic activity but for proper folding and stability.
    Biochemistry, 2004, Mar-23, Volume: 43, Issue:11

    Topics: Amino Acid Substitution; Binding Sites; Catalysis; Conserved Sequence; Cysteine; Enzyme Activation; Enzyme Stability; Glycolates; Hot Temperature; Kinetics; Models, Chemical; Mutagenesis, Site-Directed; Protein Binding; Protein Denaturation; Protein Folding; Protein Renaturation; Saccharomyces cerevisiae Proteins; Triose-Phosphate Isomerase

2004