cysteine has been researched along with phenylglyoxal in 11 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 5 (45.45) | 18.7374 |
| 1990's | 6 (54.55) | 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 |
|---|---|
| Cheon, HG; Hanna, PE | 1 |
| Davis, JP; Van Etten, RL; Zhang, ZY | 1 |
| Caine, JM; McLeish, MJ | 1 |
| Austin, AJ; Cottingham, IR; Slabas, AR | 1 |
| Kumar, S; Lennane, J; Ratner, S | 1 |
| Eun, HM; Miles, EW | 1 |
| Appaji Rao, N; Manohar, R | 1 |
| Mäntsälä, P; Myöhänen, T | 1 |
| Michelangeli, F | 1 |
| Andersson, C; Bergman, T; Ekström, L; Morgenstern, R; Raza, H; Weinander, R | 1 |
| Romaniouk, A; Vijay, IK | 1 |
11 other study(ies) available for cysteine and phenylglyoxal
| Article | Year |
|---|---|
Effect of group-selective modification reagents on arylamine N-acetyltransferase activities.
Topics: Animals; Arginine; Arylamine N-Acetyltransferase; Binding Sites; Cricetinae; Cysteine; Diethyl Pyrocarbonate; Enzyme Activation; Ethylmaleimide; Histidine; Hydroxylamine; Hydroxylamines; Liver; Male; Mesocricetus; Phenylglyoxal | 1992 |
Covalent modification and active site-directed inactivation of a low molecular weight phosphotyrosyl protein phosphatase.
Topics: Animals; Arginine; Arsenicals; Binding Sites; Binding, Competitive; Cattle; Cyclohexanones; Cysteine; Epoxy Compounds; Glutathione; Histidine; Hydrogen-Ion Concentration; Iodoacetamide; Iodoacetates; Iodoacetic Acid; Kinetics; Molecular Weight; Phenylglyoxal; Protein Tyrosine Phosphatases | 1992 |
Chemical modification of PABA synthase.
Topics: Arginine; Cysteine; Diethyl Pyrocarbonate; Escherichia coli; Folic Acid; Histidine; Iodoacetamide; Phenylglyoxal; Sulfhydryl Reagents; Tetranitromethane; Transaminases; Tyrosine | 1991 |
Inhibition and covalent modification of rape seed (Brassica napus) enoyl ACP reductase by phenylglyoxal.
Topics: Aldehydes; Arginine; Binding Sites; Brassica; Cysteine; Enoyl-(Acyl-Carrier-Protein) Reductase (NADH); Enzyme Activation; Kinetics; Oxidoreductases; Phenylglyoxal; Structure-Activity Relationship; Substrate Specificity | 1989 |
Argininosuccinate synthetase: essential role of cysteine and arginine residues in relation to structure and mechanism of ATP activation.
Topics: Adenosine Triphosphate; Animals; Arginine; Argininosuccinate Synthase; Binding Sites; Cattle; Cysteine; Dithionitrobenzoic Acid; Enzyme Activation; Kinetics; Ligases; Liver; Phenylglyoxal; Protein Binding | 1985 |
Reaction of phenylglyoxal and (p-hydroxyphenyl) glyoxal with arginines and cysteines in the alpha subunit of tryptophan synthase.
Topics: Arginine; Binding Sites; Cysteine; Escherichia coli; Phenylglyoxal; Protein Conformation; Sulfhydryl Compounds; Tryptophan Synthase | 1984 |
Identification of active-site residues of sheep liver serine hydroxymethyltransferase.
Topics: Animals; Arginine; Binding Sites; Cysteine; Diethyl Pyrocarbonate; Ethylmaleimide; Glycine Hydroxymethyltransferase; Histidine; Kinetics; Liver; Phenylglyoxal; Sheep; Spectrophotometry; Transferases | 1984 |
Evidence for the importance of cysteine and arginine residues in Pseudomonas fluorescens UK-1 pantoate dehydrogenase.
Topics: Alcohol Oxidoreductases; Arginine; Chloromercuribenzoates; Cysteine; Dithionitrobenzoic Acid; Hydroxybutyrates; Iodoacetates; NAD; Phenylglyoxal; Pseudomonas fluorescens | 1980 |
The effects of amino acid-reactive reagents on the functioning of the inositol 1,4,5-trisphosphate-sensitive calcium channel from rat cerebellum.
Topics: 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Adenosine Triphosphate; Animals; Arginine; Binding Sites; Biological Transport, Active; Calcimycin; Calcium; Calcium Channels; Cerebellum; Cysteine; Inositol 1,4,5-Trisphosphate; Lysine; Microsomes; Phenylglyoxal; Rats; Ruthenium Red; Signal Transduction; Silver Nitrate; Vanadates | 1993 |
Structural and functional aspects of rat microsomal glutathione transferase. The roles of cysteine 49, arginine 107, lysine 67, histidine, and tyrosine residues.
Topics: Amino Acid Sequence; Animals; Arginine; Cysteine; Enzyme Inhibitors; Glutathione Transferase; Histidine; Indicators and Reagents; Lysine; Male; Microsomes, Liver; Molecular Sequence Data; Mutagenesis, Site-Directed; Phenylglyoxal; Rats; Rats, Sprague-Dawley; Structure-Activity Relationship; Trinitrobenzenesulfonic Acid; Tyrosine | 1997 |
Structure-function relationships in glucosidase I: amino acids involved in binding the substrate to the enzyme.
Topics: alpha-Glucosidases; Amino Acid Sequence; Animals; Arginine; Binding Sites; Bromosuccinimide; Cattle; Cysteine; Enzyme Inhibitors; Female; Glycoproteins; Glycoside Hydrolase Inhibitors; Mammary Glands, Animal; Phenylglyoxal; Protein Binding; Rats; Rats, Sprague-Dawley; Structure-Activity Relationship; Tryptophan | 1997 |