s-hydroxymethylglutathione has been researched along with s-nitrosoglutathione in 2 studies
Studies (s-hydroxymethylglutathione) | Trials (s-hydroxymethylglutathione) | Recent Studies (post-2010) (s-hydroxymethylglutathione) | Studies (s-nitrosoglutathione) | Trials (s-nitrosoglutathione) | Recent Studies (post-2010) (s-nitrosoglutathione) |
---|---|---|---|---|---|
20 | 0 | 2 | 1,193 | 19 | 394 |
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 2 (100.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Davis, WI; Robinson, H; Sanghani, PC; Zhai, L | 1 |
Alander, J; Brandt, M; Grafström, RC; Höög, JO; Lengqvist, J; Morgenstern, R; Staab, CA | 1 |
2 other study(ies) available for s-hydroxymethylglutathione and s-nitrosoglutathione
Article | Year |
---|---|
Structure-function relationships in human glutathione-dependent formaldehyde dehydrogenase. Role of Glu-67 and Arg-368 in the catalytic mechanism.
Topics: Adenosine Diphosphate Ribose; Aldehyde Oxidoreductases; Amino Acid Substitution; Arginine; Catalysis; Glutamic Acid; Glutathione; Humans; Hydrogen-Ion Concentration; Kinetics; Lauric Acids; Leucine; Models, Molecular; Protein Conformation; S-Nitrosoglutathione; Structure-Activity Relationship; Time Factors; Zinc | 2006 |
Reduction of S-nitrosoglutathione by alcohol dehydrogenase 3 is facilitated by substrate alcohols via direct cofactor recycling and leads to GSH-controlled formation of glutathione transferase inhibitors.
Topics: Alcohol Dehydrogenase; Alcohols; Cell Line, Tumor; Enzyme Inhibitors; Glutathione; Glutathione Disulfide; Glutathione Transferase; Humans; Kinetics; Nitrosation; Oxidation-Reduction; S-Nitrosoglutathione; Sulfinic Acids | 2008 |