glyoxal has been researched along with cysteine in 13 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 2 (15.38) | 18.7374 |
1990's | 1 (7.69) | 18.2507 |
2000's | 3 (23.08) | 29.6817 |
2010's | 5 (38.46) | 24.3611 |
2020's | 2 (15.38) | 2.80 |
Authors | Studies |
---|---|
Heinrikson, RL; Weng, L; Westley, J | 1 |
Lange, LG; Riordan, JF; Vallee, BL | 1 |
Bazaes, S; Cardemil, E; Goldie, H; Jabalquinto, AM; Silva, R | 1 |
Djurdjevic-Pahl, A; Hewage, C; Lowther, J; Malthouse, JP | 1 |
Davies, MJ; Zeng, J | 1 |
Henle, T; Mende, S; Schwarzenbolz, U | 1 |
Guo, W; Liu, J; Liu, Y; Lv, X; Wang, P; Zhao, Y | 1 |
Bui, LC; Dairou, J; Lamouri, A; Leger, T; Mihoub, M; Richarme, G | 1 |
Abdallah, J; Dairou, J; Gontero, B; Mihoub, M; Richarme, G | 1 |
Dairou, J; Richarme, G | 1 |
Abdallah, J; Mihoub, M; Richarme, G | 1 |
Dong, L; Du, M; Guo, Y; Luo, XL; Ma, YJ; Wang, XY; Xu, XB; Yu, P | 1 |
Hayat, K; Ho, CT; Liu, M; Xu, H; Yu, J; Zhang, X; Zhou, T | 1 |
13 other study(ies) available for glyoxal and cysteine
Article | Year |
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Active site cysteinyl and arginyl residues of rhodanese. A novel formation of disulfide bonds in the active site promoted by phenylglyoxal.
Topics: Aldehydes; Amino Acid Sequence; Animals; Arginine; Binding Sites; Cattle; Cysteine; Disulfides; Glyoxal; Kinetics; Sulfurtransferases; Thiosulfate Sulfurtransferase | 1978 |
Functional arginyl residues as NADH binding sites of alcohol dehydrogenases.
Topics: Alcohol Oxidoreductases; Alkylation; Animals; Arginine; Binding Sites; Butanones; Carbon Radioisotopes; Chromatography, Gel; Circular Dichroism; Cysteine; Drug Stability; Glycols; Glyoxal; Horses; Humans; Kinetics; Liver; Mercuribenzoates; NAD; Oxidation-Reduction; Protein Binding; Saccharomyces cerevisiae; Species Specificity; Spectrophotometry; Structure-Activity Relationship | 1974 |
Reactivity of cysteinyl, arginyl, and lysyl residues of Escherichia coli phosphoenolpyruvate carboxykinase against group-specific chemical reagents.
Topics: Arginine; Binding Sites; Cysteine; Diacetyl; Escherichia coli; Glyoxal; Kinetics; Lysine; Phosphoenolpyruvate Carboxykinase (GTP); Pyrenes; Pyridoxal Phosphate; Sulfhydryl Reagents | 1993 |
A 13C-NMR study of the inhibition of papain by a dipeptide-glyoxal inhibitor.
Topics: Alanine; Catalysis; Cysteine; Dipeptides; Glyoxal; Magnetic Resonance Spectroscopy; Models, Chemical; Papain; Phenylalanine; Sulfhydryl Compounds | 2002 |
Evidence for the formation of adducts and S-(carboxymethyl)cysteine on reaction of alpha-dicarbonyl compounds with thiol groups on amino acids, peptides, and proteins.
Topics: Amino Acids; Carbocysteine; Chromatography, High Pressure Liquid; Cysteine; Glucose; Glycation End Products, Advanced; Glyoxal; Peptides; Proteins; Serum Albumin, Bovine; Spectrometry, Fluorescence; Spectrometry, Mass, Electrospray Ionization; Sulfhydryl Compounds | 2005 |
Model studies on protein glycation: influence of cysteine on the reactivity of arginine and lysine residues toward glyoxal.
Topics: Arginine; Chromatography, High Pressure Liquid; Cysteine; Glycosylation; Glyoxal; Kinetics; Lysine; Mass Spectrometry; Models, Molecular | 2008 |
A naphthalimide-based glyoxal hydrazone for selective fluorescence turn-on sensing of Cys and Hcy.
Topics: Cysteine; Fluorescent Dyes; Glyoxal; Homocysteine; Hydrazones; Isomerism; Molecular Structure; Naphthalimides; Tetrahymena | 2012 |
Parkinsonism-associated protein DJ-1/Park7 is a major protein deglycase that repairs methylglyoxal- and glyoxal-glycated cysteine, arginine, and lysine residues.
Topics: Acetylcysteine; Albumins; Apoptosis; Arginine; Aspartate Aminotransferases; Catalysis; Cell Survival; Cysteine; Escherichia coli; Fructose-Bisphosphate Aldolase; Glucose; Glycolates; Glyoxal; Humans; Intracellular Signaling Peptides and Proteins; Lactates; Lysine; Mass Spectrometry; Oncogene Proteins; Oxidative Stress; Parkinsonian Disorders; Protein Deglycase DJ-1; Pyruvaldehyde | 2015 |
The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal.
Topics: Arginine; Cysteine; Escherichia coli Proteins; Glucose; Glyceraldehyde-3-Phosphate Dehydrogenases; Glyoxal; Lysine; Molecular Chaperones; Pyruvaldehyde; Schiff Bases | 2015 |
Parkinsonism-associated protein DJ-1 is a bona fide deglycase.
Topics: Acetylcysteine; Artifacts; Culture Media; Cysteine; Escherichia coli; Glucose; Glycation End Products, Advanced; Glycosylation; Glyoxal; Humans; Intracellular Signaling Peptides and Proteins; Mutation; Oncogene Proteins; Parkinsonian Disorders; Protein Deglycase DJ-1; Pyruvaldehyde | 2017 |
Protein Repair from Glycation by Glyoxals by the DJ-1 Family Maillard Deglycases.
Topics: Acrylamide; Animals; Arginine; Bacteria; Bacterial Proteins; Cysteine; Glycation End Products, Advanced; Glycosylation; Glyoxal; Humans; Lysine; Maillard Reaction; Protein Deglycase DJ-1; Protein Processing, Post-Translational | 2017 |
Reinvestigation of 2-acetylthiazole formation pathways in the Maillard reaction.
Topics: Chromatography, High Pressure Liquid; Cysteine; Glucose; Glyoxal; Maillard Reaction; Odorants; Pyruvaldehyde; Tandem Mass Spectrometry; Thiazoles | 2021 |
Formation Priority of Pyrazines and 2-Acetylthiazole Dependent on the Added Cysteine and Fragments of Deoxyosones during the Thermal Process of the Glycine-Ribose Amadori Compound.
Topics: Cysteamine; Cysteine; Glycine; Glyoxal; Magnesium Oxide; Maillard Reaction; Pyrazines; Pyruvaldehyde; Ribose; Thiazoles | 2022 |