s-methyl glutathione has been researched along with dinitrochlorobenzene in 3 studies
*Dinitrochlorobenzene: A skin irritant that may cause dermatitis of both primary and allergic types. Contact sensitization with DNCB has been used as a measure of cellular immunity. DNCB is also used as a reagent for the detection and determination of pyridine compounds. [MeSH]
*Dinitrochlorobenzene: A skin irritant that may cause dermatitis of both primary and allergic types. Contact sensitization with DNCB has been used as a measure of cellular immunity. DNCB is also used as a reagent for the detection and determination of pyridine compounds. [MeSH]
Studies (s-methyl glutathione) | Trials (s-methyl glutathione) | Recent Studies (post-2010) (s-methyl glutathione) | Studies (dinitrochlorobenzene) | Trials (dinitrochlorobenzene) | Recent Studies (post-2010) (dinitrochlorobenzene) |
---|---|---|---|---|---|
41 | 0 | 4 | 2,558 | 68 | 425 |
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 1 (33.33) | 18.7374 |
1990's | 2 (66.67) | 18.2507 |
2000's | 0 (0.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
O'Leary, KA; Tracy, JW | 1 |
Danielson, UH; Mannervik, B; Principato, GB | 1 |
Aceto, A; Allocati, N; Angelucci, S; Bucciarelli, T; Di Ilio, C; Dragani, B; Martini, F; Sacchetta, P | 1 |
3 other study(ies) available for s-methyl glutathione and dinitrochlorobenzene
Article | Year |
---|---|
Schistosoma mansoni: glutathione S-transferase-catalyzed detoxication of dichlorvos.
Topics: Animals; Cytosol; Dichlorvos; Dinitrochlorobenzene; Epoxy Compounds; Female; Glutathione; Glutathione Transferase; Inactivation, Metabolic; Kinetics; Male; Methylation; Nitrobenzenes; Schistosoma mansoni | 1991 |
Relaxed thiol substrate specificity of glutathione transferase effected by a non-substrate glutathione derivative.
Topics: Animals; Dinitrochlorobenzene; Glutathione; Glutathione Transferase; Kinetics; Liver; Mercaptoethanol; Rats; Substrate Specificity | 1988 |
Analysis by limited proteolysis of domain organization and GSH-site arrangement of bacterial glutathione transferase B1-1.
Topics: Amino Acid Sequence; Binding Sites; Biological Evolution; Chymotrypsin; Circular Dichroism; Dinitrochlorobenzene; Electrophoresis, Polyacrylamide Gel; Glutathione; Glutathione Transferase; Molecular Sequence Data; Peptide Fragments; Protein Structure, Secondary; Proteus mirabilis; Sequence Homology, Amino Acid; Structure-Activity Relationship; Trypsin | 1995 |