Page last updated: 2024-08-22

dithiothreitol and mesna

dithiothreitol has been researched along with mesna in 6 studies

Research

Studies (6)

TimeframeStudies, this research(%)All Research%
pre-19903 (50.00)18.7374
1990's1 (16.67)18.2507
2000's1 (16.67)29.6817
2010's1 (16.67)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Gobert, JG; Risack, LE; Vandevelde, ME1
Ankel-Fuchs, D; Thauer, RK1
Fahey, RC; Gonick, G; Newton, GL; Ward, JF; Zheng, S1
Brenner, MC; Scott, RA; Zhang, H1
Evans, TC; Martin, DD; Xu, MQ1
Liu, XQ; Volkmann, G1

Other Studies

6 other study(ies) available for dithiothreitol and mesna

ArticleYear
Effect of thiol derivatives on mixed mucus and blood clots in vitro.
    Resuscitation, 1978, Volume: 6, Issue:1

    Topics: Acetylcysteine; Blood Coagulation; Dithiothreitol; Expectorants; Humans; In Vitro Techniques; Mercaptoethanol; Mesna; Mucus; Respiratory System; Saline Solution, Hypertonic

1978
Methane formation from methyl-coenzyme M in a system containing methyl-coenzyme M reductase, component B and reduced cobalamin.
    European journal of biochemistry, 1986, Apr-01, Volume: 156, Issue:1

    Topics: Catalysis; Dithiothreitol; Euryarchaeota; Mercaptoethanol; Mesna; Methane; Oxidoreductases; Vitamin B 12

1986
Radioprotection of DNA by thiols: relationship between the net charge on a thiol and its ability to protect DNA.
    Radiation research, 1988, Volume: 114, Issue:1

    Topics: Anions; Cations; Cysteamine; Dithiothreitol; DNA; DNA Damage; Glutathione; Mercaptoethanol; Mercaptoethylamines; Mesna; Radiation-Protective Agents; Sulfhydryl Compounds; Thiomalates

1988
Nature of the low activity of S-methyl-coenzyme M reductase as determined by active site titrations.
    The Journal of biological chemistry, 1993, Sep-05, Volume: 268, Issue:25

    Topics: Alkanesulfonates; Binding Sites; Binding, Competitive; Chromatography, High Pressure Liquid; Disulfides; Dithiothreitol; Electron Spin Resonance Spectroscopy; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Euryarchaeota; Mesna; Oxidation-Reduction; Oxidoreductases; Phosphothreonine

1993
Characterization of a naturally occurring trans-splicing intein from Synechocystis sp. PCC6803.
    Biochemistry, 2001, Feb-06, Volume: 40, Issue:5

    Topics: Amino Acid Sequence; Cyanobacteria; Dithiothreitol; DNA Polymerase III; Esterification; Hydrogen-Ion Concentration; Hydrolysis; Hydroxylamine; Kinetics; Mesna; Molecular Sequence Data; Peptide Fragments; Protein Binding; Protein Splicing; Sensitivity and Specificity; Sulfhydryl Compounds; Temperature; Trans-Splicing

2001
Intein lacking conserved C-terminal motif G retains controllable N-cleavage activity.
    The FEBS journal, 2011, Volume: 278, Issue:18

    Topics: Bacterial Proteins; Catalysis; Dithiothreitol; DNA Gyrase; Enzyme Precursors; Enzyme Stability; Hydroxylamine; Inteins; Kinetics; Mesna; Mutant Proteins; Oligopeptides; Peptide Fragments; Protein Engineering; Protein Interaction Domains and Motifs; Protein Splicing; Recombinant Fusion Proteins; Reducing Agents; Synechocystis; Zinc

2011