cysteine has been researched along with diamide in 68 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 6 (8.82) | 18.7374 |
| 1990's | 22 (32.35) | 18.2507 |
| 2000's | 22 (32.35) | 29.6817 |
| 2010's | 15 (22.06) | 24.3611 |
| 2020's | 3 (4.41) | 2.80 |
| Authors | Studies |
|---|---|
| Olefsky, JM | 2 |
| Quinn, D; Warr, JR | 1 |
| Howley, PM; Klausner, RD; McBride, AA | 1 |
| Cotgreave, IA; Moldéus, P; Schuppe, I | 1 |
| Hecker, M; Macarthur, H; Sessa, WC; Siegle, I; Vane, JR | 1 |
| Guehmann, S; Kalkbrenner, F; Moelling, K; Vorbrueggen, G | 1 |
| Hiraishi, H; Ivey, KJ; Mutoh, H; Ota, S; Sugimoto, T; Terano, A | 1 |
| Abate, C; Curran, T; Patel, L; Rauscher, FJ | 1 |
| Beidler, D; Collison, MW; Grimm, LM; Thomas, JA | 1 |
| Lahti, R; Suonpää, M | 1 |
| Silbernagl, S; Völkl, H | 1 |
| Bennett, N; Ildefonse, M; Serre, V | 1 |
| Henderson, BR; Hirling, H; Kühn, LC | 1 |
| Arnone, MI; Di Lauro, R; Zannini, M | 1 |
| Ochi, T | 1 |
| Kachar, B; Kalinec, F | 1 |
| Hirai, H; Hirano, N; Kurokawa, M; Mitani, K; Ogawa, S; Tanaka, K; Tanaka, T; Yazaki, Y | 1 |
| Harris, C; Hiranruengchok, R | 1 |
| Björkbacka, H; Forsman, C; Johansson, IM; Skärfstad, E | 1 |
| Jones, N; Kuge, S; Nomoto, A | 1 |
| Akamatsu, Y; Hirota, K; Kagoshima, H; Ohno, T; Shigesada, K; Yodoi, J | 1 |
| Di Simplicio, P; Giannerini, F; Giustarini, D; Lusini, L; Rossi, R | 1 |
| Fahey, RC; Sherrill, C | 1 |
| Brunner-Neuenschwander, B; Levings, CS; Rhoads, DM; Siedow, JN | 1 |
| Amiconi, G; Barra, D; Bellelli, A; Boumis, G; Canofeni, S; Di Simplicio, P; Lusini, L; Pascarella, S; Rossi, R | 1 |
| Lee, SH; Park, JS; Park, SJ; Wang, M | 1 |
| Coleman, ST; Epping, EA; Moye-Rowley, WS; Steggerda, SM | 1 |
| Campoccia, G; Di Simplicio, P; Fanetti, G; Giannerini, F; Giustarini, D; Lusini, L; Rossi, R | 1 |
| Delaunay, A; Isnard, AD; Toledano, MB | 1 |
| Colombo, R; Dalle-Donne, I; Di Simplicio, P; Giannerini, F; Giustarini, D; Lusini, L; Milzani, A; Rossi, R | 1 |
| Kelley, MR; Parsons, SH | 1 |
| Gordienko, DV; Greenwood, IA; Large, WA; Leblanc, N | 1 |
| Clarke, SJ; Halestrap, AP; McStay, GP | 1 |
| Humphries, KM; Juliano, C; Taylor, SS | 1 |
| Ergün, Y; Ogülener, N | 1 |
| Colombo, R; Dalle-Donne, I; Giustarini, D; Milzani, A; Rossi, R | 1 |
| Budde, AD; Jones, BL | 1 |
| Caplan, JF; Filipenko, NR; Fitzpatrick, SL; Waisman, DM | 1 |
| Kil, IS; Park, JW | 1 |
| Giangregorio, N; Indiveri, C; Palmieri, F; Tonazzi, A | 1 |
| Ng, VS; Siedow, JN; Umbach, AL | 1 |
| Gupta, N; Pop, SM; Ragsdale, SW; Raza, AS | 1 |
| Doneanu, CE; Niture, SK; Pattabiraman, N; Srivenugopal, KS; Velu, CS | 1 |
| Becher, D; Hecker, M; Helmann, JD; Hochgräfe, F; Mostertz, J; Pöther, DC | 1 |
| Antelmann, H; Becher, D; Hecker, M; Huyen, NT; Leelakriangsak, M; Töwe, S; van Duy, N; Zuber, P | 1 |
| Hashemy, SI; Holmgren, A | 1 |
| Hondorp, ER; Matthews, RG | 1 |
| Grant, N; Ito, K; Kakizaki, Y; Onda, Y; Robinson, S; Watling, J | 1 |
| Dalle-Donne, I; Giustarini, D; Milzani, A; Rossi, R | 1 |
| Coppo, L; Di Giuseppe, D; Di Simplicio, P; Frosali, S; Heo, J; Margaritis, A; Priora, R; Summa, D | 1 |
| Hatano, N; Kambe, T; Miyamoto, Y; Naito, Y; Nozaki, N; Song, T; Takata, T; Tokumitsu, H; Watanabe, Y | 1 |
| Albrecht, D; Antelmann, H; Becher, D; Chi, BK; Gronau, K; Hecker, M | 1 |
| Aleanzi, MC; Bosco, MB; Iglesias, AÁ | 1 |
| Iyamu, EW; Perdew, HA; Woods, GM | 1 |
| Anastasiou, D; Asara, JM; Auld, DS; Bellinger, G; Boxer, MB; Cantley, LC; Jiang, JK; Locasale, JW; Poulogiannis, G; Sasaki, AT; Shen, M; Thomas, CJ; Vander Heiden, MG | 1 |
| Albrecht, D; Antelmann, H; Becher, D; Gronau, K; Hinrichs, W; Khanh Chi, B; Palm, GJ; Read, RJ; Waack, P | 1 |
| Adámik, M; Brázdová, M; Fojta, M; Navrátilová, L; Tichý, V | 1 |
| Aharonowitz, Y; Antelmann, H; Borovok, I; Gierok, P; Hamilton, CJ; Harms, M; Hecker, M; Hochgräfe, F; Lalk, M; Mostertz, J; Pöther, DC | 1 |
| Takata, T; Tsuchiya, Y; Watanabe, Y | 1 |
| Gonzalez, DH; Güttlein, LN; Viola, IL | 1 |
| Aldrich, JT; Camp, DG; Chu, RK; Clauss, TR; Gaffrey, MJ; Guo, J; Hatchell, KE; Purvine, S; Qian, WJ; Smith, RD; Su, D; Thrall, BD; Wu, S | 1 |
| Avenoza, A; Aydillo, C; Busto, JH; Compañón, I; Corzana, F; Peregrina, JM; Zurbano, MM | 1 |
| Bordin, L; Bosello-Travain, V; Falda, M; Maiorino, M; Roveri, A; Toppo, S; Ursini, F; Zaccarin, M | 1 |
| Ebihara, Y; Kawakami, Y; Yamauchi, K | 1 |
| Hashimoto, K; Kataoka, N; Kihara, D; Masaki, S; Suzuki, K; Tsuzuki, C | 1 |
| Aliverti, A; de Rosa, M; Nonnis, S | 1 |
| Boonyakanog, A; Charoenlap, N; Chattrakarn, S; Mongkolsuk, S; Vattanaviboon, P | 1 |
68 other study(ies) available for cysteine and diamide
| Article | Year |
|---|---|
Comparison of the effects of insulin and insulin-like agents on different aspects of adipocyte metabolism.
Topics: Adipose Tissue; Animals; Azo Compounds; Biological Transport, Active; Cysteine; Cytochalasin B; Deoxyglucose; Diamide; Glucose; Glycolysis; Insulin; Kinetics; Male; Rats; Spermine | 1979 |
Low molecular weight sulphydryl compounds and the expression of a cell division mutant of Chlamydomonas reinhardi.
Topics: Azo Compounds; Cell Division; Cell Nucleus; Chlamydomonas; Cysteine; Cystine; Diamide; Ethanol; Mercaptoethanol; Mutation | 1977 |
Interaction between insulin receptors and glucose transport: effect of prostaglandin E2.
Topics: Adipose Tissue; Animals; Biological Transport; Cysteine; Deoxy Sugars; Deoxyglucose; Diamide; Insulin; Kinetics; Male; Oleic Acids; Prostaglandins E; Prostaglandins F; Rats; Receptor, Insulin; Spermine | 1977 |
Conserved cysteine residue in the DNA-binding domain of the bovine papillomavirus type 1 E2 protein confers redox regulation of the DNA-binding activity in vitro.
Topics: Amino Acid Sequence; Animals; Base Sequence; Binding Sites; Bovine papillomavirus 1; Cysteine; Diamide; Disulfides; DNA-Binding Proteins; Ethylmaleimide; Molecular Sequence Data; Oligonucleotide Probes; Oncogene Proteins, Viral; Open Reading Frames; Plasmids; Protein Biosynthesis; Rabbits; Reticulocytes; Sequence Homology, Nucleic Acid; Sulfhydryl Reagents; Transcription, Genetic | 1992 |
Protein-specific S-thiolation in human endothelial cells during oxidative stress.
Topics: Cysteine; Diamide; Endothelium, Vascular; Female; Glutathione; Glutathione Disulfide; Humans; Hydrogen Peroxide; Intracellular Fluid; Oxidants; Oxidation-Reduction; Peroxides; Pregnancy; Proteins; Sensitivity and Specificity; Sulfhydryl Compounds; Sulfur Radioisotopes; tert-Butylhydroperoxide; Umbilical Veins | 1992 |
Role of intracellular thiols in release of EDRF from cultured endothelial cells.
Topics: Adenosine Diphosphate; Animals; Aorta; Arginine; Biological Assay; Cattle; Cells, Cultured; Cysteine; Diamide; Endothelium, Vascular; Ethylmaleimide; Glutathione; Ionomycin; Kinetics; Nitric Oxide; Nitroarginine; omega-N-Methylarginine; Sulfhydryl Compounds; Sulfhydryl Reagents | 1992 |
Reduction of a conserved Cys is essential for Myb DNA-binding.
Topics: Alkylation; Base Sequence; Cysteine; Diamide; DNA; Electrophoresis, Polyacrylamide Gel; Gene Expression; Humans; Molecular Sequence Data; Mutation; Oxidation-Reduction; Proto-Oncogene Proteins; Proto-Oncogene Proteins c-myb | 1992 |
Reduced glutathione protects cultured gastric mucosal cells from suckling rats against acid.
Topics: Acids; Animals; Animals, Newborn; Catalase; Cells, Cultured; Cysteine; Diamide; Dimethyl Sulfoxide; Dinitrochlorobenzene; Female; Gastric Mucosa; Glutathione; Hydrogen-Ion Concentration; Kinetics; Male; Maleates; Oxidation-Reduction; Peroxides; Rats; Rats, Inbred Strains; Stomach Ulcer; Superoxide Dismutase; tert-Butylhydroperoxide | 1991 |
Redox regulation of fos and jun DNA-binding activity in vitro.
Topics: Amino Acid Sequence; Animals; Cell-Free System; Cysteine; Diamide; DNA Mutational Analysis; DNA-Binding Proteins; Humans; In Vitro Techniques; Molecular Sequence Data; Oxidation-Reduction; Proto-Oncogene Proteins; Proto-Oncogene Proteins c-fos; Proto-Oncogene Proteins c-jun; Rats; Recombinant Proteins; Signal Transduction; Structure-Activity Relationship; Sulfhydryl Reagents; Transcription Factors | 1990 |
A comparison of protein S-thiolation (protein mixed-disulfide formation) in heart cells treated with t-butyl hydroperoxide or diamide.
Topics: Animals; Azo Compounds; Cells, Cultured; Cysteine; Diamide; Disulfides; Glutathione; In Vitro Techniques; Muscle Proteins; Myocardial Contraction; Oxidation-Reduction; Peroxides; Rats; tert-Butylhydroperoxide | 1986 |
Role of glutathione in the regulation of inorganic pyrophosphatase activity in Streptococcus faecalis.
Topics: Cysteine; Diamide; Enterococcus faecalis; Glutathione; Inorganic Pyrophosphatase; Oxidation-Reduction; Pyrophosphatases | 1982 |
Reexamination of the interplay between dibasic amino acids and I-cystine/L-cysteine during tubular reabsorption.
Topics: Absorption; Amino Acids; Animals; Arginine; Cysteine; Cystine; Diamide; Dithioerythritol; Kidney Tubules, Proximal; Perfusion; Rats | 1982 |
Effects of cysteine modification on the activity of the cGMP-gated channel from retinal rods.
Topics: Animals; Blotting, Western; Calcium; Calcium Channels; Cattle; Cyclic GMP; Cyclic Nucleotide-Gated Cation Channels; Cysteine; Diamide; Dithiothreitol; Ethylmaleimide; Glutathione; Glutathione Disulfide; Ion Channel Gating; Ion Channels; Lipid Bilayers; Mersalyl; Nitric Oxide; Rod Cell Outer Segment; Sodium; Sulfhydryl Reagents | 1995 |
Mutational analysis of the [4Fe-4S]-cluster converting iron regulatory factor from its RNA-binding form to cytoplasmic aconitase.
Topics: Aconitate Hydratase; Animals; Cysteine; Cytoplasm; Diamide; Enzyme Activation; Ethylmaleimide; Humans; Iron; Iron-Regulatory Proteins; L Cells; Mercaptoethanol; Mice; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Binding; Protein Conformation; RNA; RNA-Binding Proteins; Substrate Specificity; Transfection | 1994 |
The DNA binding activity and the dimerization ability of the thyroid transcription factor I are redox regulated.
Topics: Alkylation; Animals; Base Sequence; Binding Sites; Consensus Sequence; Cysteine; Cystine; Diamide; Dithiothreitol; DNA; DNA-Binding Proteins; Glutathione; HeLa Cells; Homeodomain Proteins; Humans; Molecular Sequence Data; Oxidation-Reduction; Promoter Regions, Genetic; Protein Conformation; Rats; Recombinant Fusion Proteins; Sequence Alignment; Sequence Homology, Nucleic Acid; Thyroid Neoplasms; Tumor Cells, Cultured | 1995 |
Mechanism for the changes in levels of glutathione upon exposure of cultured mammalian cells to tertiary-butylhydroperoxide and diamide.
Topics: Animals; Cells, Cultured; Cricetinae; Cricetulus; Cysteine; Diamide; Extracellular Space; Fibroblasts; Glutathione; Glutathione Disulfide; Hydrogen-Ion Concentration; Male; Oxidants; Oxidation-Reduction; Peroxides; Phenanthrolines; Protein Biosynthesis; Reactive Oxygen Species; Solubility; Sulfur Radioisotopes; tert-Butylhydroperoxide | 1993 |
Inhibition of outer hair cell electromotility by sulfhydryl specific reagents.
Topics: 4-Chloromercuribenzenesulfonate; Animals; Cell Movement; Cysteine; Cystine; Diamide; Electric Stimulation; Ethacrynic Acid; Ethylmaleimide; Guinea Pigs; Hair Cells, Auditory, Outer; Membrane Proteins; Mersalyl; Nerve Tissue Proteins; Protein Conformation; Sulfhydryl Reagents | 1993 |
A conserved cysteine residue in the runt homology domain of AML1 is required for the DNA binding ability and the transforming activity on fibroblasts.
Topics: 3T3 Cells; Animals; Cell Line; Cell Transformation, Neoplastic; Conserved Sequence; Core Binding Factor Alpha 2 Subunit; Cysteine; Diamide; DNA-Binding Proteins; Ethylmaleimide; Fibroblasts; Mice; Mutagenesis, Site-Directed; Neoplasm Proteins; Oxidation-Reduction; Protein Binding; Proto-Oncogene Proteins; Serine; Transcription Factor AP-2; Transcription Factors; Transcriptional Activation | 1996 |
Formation of protein-glutathione mixed disulfides in the developing rat conceptus following diamide treatment in vitro.
Topics: Animals; Cysteine; Diamide; Dithiothreitol; Dose-Response Relationship, Drug; Embryo, Mammalian; Embryonic and Fetal Development; Ethylmaleimide; Female; Glutathione; Organ Culture Techniques; Pregnancy; Protein Disulfide Reductase (Glutathione); Rats; Rats, Sprague-Dawley; Sulfhydryl Reagents; Tissue Distribution | 1995 |
The sulfhydryl groups of Cys 269 and Cys 272 are critical for the oligomeric state of chloroplast carbonic anhydrase from Pisum sativum.
Topics: Carbon Dioxide; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Chloroplasts; Circular Dichroism; Cross-Linking Reagents; Cysteine; Diamide; Dithionitrobenzoic Acid; Escherichia coli; Ethoxzolamide; Gene Expression; Kinetics; Molecular Weight; Mutagenesis, Site-Directed; Phosphines; Pisum sativum; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrometry, Fluorescence | 1997 |
Regulation of yAP-1 nuclear localization in response to oxidative stress.
Topics: Amino Acid Sequence; Base Sequence; Cell Nucleus; Conserved Sequence; Cysteine; Cytoplasm; Diamide; DNA Primers; DNA-Binding Proteins; Drug Resistance, Microbial; Fungal Proteins; Hydrogen Peroxide; Maleates; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidative Stress; Polymerase Chain Reaction; Recombinant Fusion Proteins; Recombinant Proteins; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sequence Deletion; Sequence Homology, Amino Acid; Sequence Tagged Sites; Transcription Factors | 1997 |
Redox regulation of the DNA binding activity in transcription factor PEBP2. The roles of two conserved cysteine residues.
Topics: Amino Acid Sequence; Animals; Conserved Sequence; Cysteine; Diamide; Dimerization; DNA; DNA-Binding Proteins; Evolution, Molecular; Kinetics; Macromolecular Substances; Mammals; Mice; Mutagenesis, Site-Directed; Oxidation-Reduction; Recombinant Proteins; Sequence Tagged Sites; Transcription Factor AP-2; Transcription Factors | 1997 |
The role of cysteine in the regulation of blood glutathione-protein mixed disulfides in rats treated with diamide.
Topics: Animals; Chromatography, High Pressure Liquid; Cysteine; Diamide; Disulfides; Erythrocytes; Glutathione; Glutathione Disulfide; In Vitro Techniques; Injections, Intraperitoneal; Kinetics; Liver; Male; Rats; Rats, Wistar; Sulfhydryl Reagents | 1998 |
Import and metabolism of glutathione by Streptococcus mutans.
Topics: Biological Transport, Active; Chromatography, High Pressure Liquid; Culture Media; Cysteine; Diamide; Glucose; Glutamine; Glutathione; Glutathione Disulfide; Kinetics; Streptococcus mutans; Sulfides | 1998 |
Cross-linking and disulfide bond formation of introduced cysteine residues suggest a modified model for the tertiary structure of URF13 in the pore-forming oligomers.
Topics: Amino Acid Sequence; Cross-Linking Reagents; Cysteine; Diamide; Dicyclohexylcarbodiimide; Disulfides; Maleimides; Mitochondrial Proteins; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Plant Proteins; Protein Structure, Tertiary; Sulfhydryl Compounds; Threonine; Zea mays | 1998 |
Fast-reacting thiols in rat hemoglobins can intercept damaging species in erythrocytes more efficiently than glutathione.
Topics: Animals; Cysteine; Diamide; Disulfides; Dithionitrobenzoic Acid; Erythrocytes; Glutathione; Hemoglobins; Male; Models, Molecular; Oxidants; Oxidative Stress; Protein Conformation; Rats; Rats, Sprague-Dawley; Structure-Activity Relationship; Sulfhydryl Compounds; Sulfhydryl Reagents | 1998 |
Zinc finger of replication protein A, a non-DNA binding element, regulates its DNA binding activity through redox.
Topics: Amino Acid Sequence; Chelating Agents; Cysteine; Diamide; Dithiothreitol; DNA Helicases; DNA-Binding Proteins; DNA, Single-Stranded; Humans; Models, Molecular; Molecular Sequence Data; Mutation; Oxidation-Reduction; Phenanthrolines; Proteins; Sulfhydryl Reagents; Thioredoxins; Trans-Activators; Zinc Fingers | 1999 |
Yap1p activates gene transcription in an oxidant-specific fashion.
Topics: Alanine; Binding Sites; Cysteine; Diamide; DNA-Binding Proteins; Fungal Proteins; Gene Expression Regulation, Fungal; Genes, Reporter; Hydrogen Peroxide; Membrane Proteins; Mutagenesis; Oxidants; Promoter Regions, Genetic; Repetitive Sequences, Nucleic Acid; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thioredoxins; Transcription Factors; Transcription, Genetic | 1999 |
Minor thiols cysteine and cysteinylglycine regulate the competition between glutathione and protein SH groups in human platelets subjected to oxidative stress.
Topics: Antioxidants; Blood Platelets; Chromatography, High Pressure Liquid; Cysteine; Diamide; Dipeptides; Disulfides; Dithionitrobenzoic Acid; Erythrocytes; Glutathione; Humans; Oxidative Stress; Spectrophotometry; src Homology Domains; Sulfhydryl Compounds; tert-Butylhydroperoxide; Time Factors | 2000 |
H2O2 sensing through oxidation of the Yap1 transcription factor.
Topics: Adaptation, Physiological; Blotting, Western; Cysteine; Diamide; DNA-Binding Proteins; Fluorescent Antibody Technique; Fungal Proteins; Homeostasis; Hydrogen Peroxide; Models, Biological; Oxidation-Reduction; Reverse Transcriptase Polymerase Chain Reaction; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thioredoxins; Transcription Factors; Two-Hybrid System Techniques | 2000 |
Different metabolizing ability of thiol reactants in human and rat blood: biochemical and pharmacological implications.
Topics: Adult; Animals; Chromatography, High Pressure Liquid; Cysteine; Diamide; Dithionitrobenzoic Acid; Dose-Response Relationship, Drug; Erythrocytes; Glutathione; Glutathione Reductase; Hemoglobins; Humans; Hydrogen Peroxide; Male; Middle Aged; Nitric Oxide; Nitric Oxide Donors; Nitroso Compounds; Rats; Rats, Wistar; S-Nitrosothiols; Sulfhydryl Compounds; Sulfhydryl Reagents; Time Factors | 2001 |
Redox regulation of the DNA repair function of the human AP endonuclease Ape1/ref-1.
Topics: Apurinic Acid; Carbon-Oxygen Lyases; Cysteine; Diamide; Dithiothreitol; DNA Damage; DNA Repair; DNA-(Apurinic or Apyrimidinic Site) Lyase; Humans; Hydrogen Peroxide; Kinetics; Models, Biological; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Oxidants; Oxidation-Reduction; Protein Processing, Post-Translational; Recombinant Fusion Proteins; Structure-Activity Relationship; Transcription Factors | 2001 |
Modulation of ICl(Ca) in vascular smooth muscle cells by oxidizing and cysteine-reactive reagents.
Topics: 4-Chloromercuribenzenesulfonate; Animals; Calcium; Chloride Channels; Cysteine; Diamide; Dithiothreitol; Hydrogen Peroxide; In Vitro Techniques; Membrane Potentials; Muscle, Smooth, Vascular; Oxidants; Oxidation-Reduction; Patch-Clamp Techniques; Portal Vein; Rabbits; Sulfhydryl Reagents | 2002 |
Role of critical thiol groups on the matrix surface of the adenine nucleotide translocase in the mechanism of the mitochondrial permeability transition pore.
Topics: Adenosine Diphosphate; Animals; Arsenicals; Chromatography, Affinity; Cross-Linking Reagents; Cyclophilins; Cysteine; Diamide; Dimerization; Eosine Yellowish-(YS); Glutathione Transferase; Intracellular Membranes; Male; Mitochondria; Mitochondrial ADP, ATP Translocases; Oxidative Stress; Peptidyl-Prolyl Isomerase F; Permeability; Phenanthrolines; Rats; Rats, Wistar; Sulfhydryl Compounds; Sulfhydryl Reagents | 2002 |
Regulation of cAMP-dependent protein kinase activity by glutathionylation.
Topics: Alanine; Amino Acid Sequence; Binding Sites; Biotinylation; Conserved Sequence; Cyclic AMP-Dependent Protein Kinases; Cysteine; Diamide; Glutathione; Isoenzymes; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Processing, Post-Translational; Protein Subunits; Recombinant Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Sulfhydryl Compounds | 2002 |
A putative role for S-nitrosoglutathione as the source of nitric oxide in photorelaxation of the mouse gastric fundus.
Topics: Acetylcysteine; Animals; Cysteine; Diamide; Enzyme Inhibitors; Ethacrynic Acid; Female; Gastric Fundus; Glutathione; In Vitro Techniques; Isoproterenol; Male; Mice; Muscle Relaxation; Muscle, Smooth; Nitric Oxide; S-Nitrosoglutathione; S-Nitrosothiols; Ultraviolet Rays | 2002 |
Actin S-glutathionylation: evidence against a thiol-disulphide exchange mechanism.
Topics: Actins; Animals; Chromatography, High Pressure Liquid; Cysteine; Diamide; Dithionitrobenzoic Acid; Glutathione; Glutathione Disulfide; Muscle, Skeletal; Rabbits; Sulfhydryl Compounds | 2003 |
Effect of reducing and oxidizing agents and pH on malt endoproteolytic activities and brewing mashes.
Topics: Cysteine; Diamide; Dithiothreitol; Edible Grain; Endopeptidases; Food Handling; Hordeum; Hot Temperature; Hydrogen Peroxide; Hydrogen-Ion Concentration; Hydrolysis; Mercaptoethanol; Oxidants; Protease Inhibitors; Reducing Agents | 2003 |
Regulation of annexin A2 by reversible glutathionylation.
Topics: Actins; Animals; Annexin A2; Biotinylation; Cattle; Cysteine; Diamide; Dithiothreitol; Glutaredoxins; Glutathione; Homeostasis; Hydrogen Peroxide; Liposomes; Mass Spectrometry; Oxidants; Oxidation-Reduction; Oxidative Stress; Oxidoreductases; Phospholipids; Proteins; Structure-Activity Relationship; Tumor Necrosis Factor-alpha | 2004 |
Regulation of mitochondrial NADP+-dependent isocitrate dehydrogenase activity by glutathionylation.
Topics: 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine; Animals; Brain; Cell Line; Cysteine; Diamide; Disulfides; DNA Fragmentation; Dopamine Agents; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Genetic Vectors; Glutathione; Humans; Hydrogen Peroxide; Immunoblotting; Immunoprecipitation; Isocitrate Dehydrogenase; Mass Spectrometry; Mice; Mice, Inbred ICR; Mitochondria; Mutagenesis, Site-Directed; NADP; Oxidants; Oxidation-Reduction; Oxidative Stress; Oxygen; Rabbits; Sulfhydryl Compounds; Time Factors | 2005 |
Identification by site-directed mutagenesis and chemical modification of three vicinal cysteine residues in rat mitochondrial carnitine/acylcarnitine transporter.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Arsenicals; Carnitine; Carnitine Acyltransferases; Cattle; Cysteine; Diamide; Enzyme Inhibitors; In Vitro Techniques; Kinetics; Liposomes; Mitochondria; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Phenanthrolines; Rats; Recombinant Proteins; Sequence Homology, Amino Acid | 2005 |
Regulation of plant alternative oxidase activity: a tale of two cysteines.
Topics: Amino Acid Sequence; Amino Acid Substitution; Arabidopsis; Arabidopsis Proteins; Cysteine; Diamide; Disulfides; Glyoxylates; Mitochondrial Proteins; Mutagenesis, Site-Directed; Oxidoreductases; Plant Proteins; Pyruvic Acid | 2006 |
Transcriptional activation of dehalorespiration. Identification of redox-active cysteines regulating dimerization and DNA binding.
Topics: Amino Acid Sequence; Bacterial Proteins; Cysteine; Desulfitobacterium; Diamide; Dimerization; Disulfides; Dithiothreitol; DNA-Binding Proteins; Gene Expression Regulation, Bacterial; Iron-Sulfur Proteins; Molecular Sequence Data; Multigene Family; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxygen; Peptides; Polychlorinated Biphenyls; Protein Structure, Quaternary; Protein Subunits; Sulfhydryl Reagents; Transcription Factors; Transcriptional Activation | 2006 |
Human p53 is inhibited by glutathionylation of cysteines present in the proximal DNA-binding domain during oxidative stress.
Topics: Acetylcysteine; Amino Acid Sequence; Binding Sites; Buthionine Sulfoximine; Camptothecin; Cell Line, Tumor; Cross-Linking Reagents; Cysteine; Diamide; DNA Damage; DNA-Binding Proteins; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Glutaral; Glutathione; Glutathione Disulfide; Humans; Hydrogen Peroxide; Models, Molecular; Oxidative Stress; Phosphorylation; Recombinant Proteins; Tandem Mass Spectrometry; tert-Butylhydroperoxide; Tumor Suppressor Protein p53 | 2007 |
S-cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress.
Topics: Bacillus subtilis; Bacterial Proteins; Cysteine; Diamide; Electrophoresis, Gel, Two-Dimensional; Glutathione; Oxidative Stress; Protein Processing, Post-Translational | 2007 |
Regulation of quinone detoxification by the thiol stress sensing DUF24/MarR-like repressor, YodB in Bacillus subtilis.
Topics: Bacillus subtilis; Bacterial Proteins; Catechols; Cysteine; Diamide; DNA Footprinting; DNA-Binding Proteins; Gene Expression Regulation, Bacterial; Hydrogen Peroxide; Hydroquinones; Mass Spectrometry; Models, Molecular; NADH, NADPH Oxidoreductases; Nitroreductases; Oligonucleotide Array Sequence Analysis; Oxidative Stress; Promoter Regions, Genetic; Proteomics; Quinones; Repressor Proteins; Sulfhydryl Compounds; Transcription, Genetic; Up-Regulation | 2008 |
Regulation of the catalytic activity and structure of human thioredoxin 1 via oxidation and S-nitrosylation of cysteine residues.
Topics: Catalysis; Cysteine; Diamide; Humans; Hydrogen Peroxide; Models, Molecular; Nitric Oxide Donors; Oxidants; Oxidation-Reduction; Proline; Protein Structure, Tertiary; S-Nitrosoglutathione; Sulfhydryl Reagents; Thioredoxins; Time Factors | 2008 |
Oxidation of cysteine 645 of cobalamin-independent methionine synthase causes a methionine limitation in Escherichia coli.
Topics: Alanine; Cysteine; Diamide; Escherichia coli; Methionine; Methyltransferases; Mutation; Oxidation-Reduction; Structure-Activity Relationship | 2009 |
Two cys or not two cys? That is the question; alternative oxidase in the thermogenic plant sacred Lotus.
Topics: Amino Acid Sequence; Cysteine; Diamide; Disulfides; Glyoxylates; Immunoblotting; Isoenzymes; Mitochondria; Mitochondrial Proteins; Molecular Sequence Data; Nelumbo; Oxidoreductases; Oxygen; Phylogeny; Plant Proteins; Protein Multimerization; Pyruvic Acid; Succinates; Temperature | 2009 |
Oxidative stress induces a reversible flux of cysteine from tissues to blood in vivo in the rat.
Topics: Animals; Antioxidants; Cysteine; Diamide; Disulfides; Glutathione; Male; Methionine; Organ Specificity; Oxidative Stress; Rats; Rats, Sprague-Dawley; Sulfhydryl Compounds; Sulfhydryl Reagents | 2009 |
The control of S-thiolation by cysteine via gamma-glutamyltranspeptidase and thiol exchanges in erythrocytes and plasma of diamide-treated rats.
Topics: Animals; Cysteine; Diamide; Enzyme Inhibitors; Erythrocytes; gamma-Glutamyltransferase; Glutathione; Isoxazoles; Kidney; Liver; Male; Oxidation-Reduction; Rats; Rats, Sprague-Dawley; Sulfhydryl Compounds; Sulfhydryl Reagents; Time Factors | 2010 |
Inactivation of Ca2+/calmodulin-dependent protein kinase I by S-glutathionylation of the active-site cysteine residue.
Topics: Binding Sites; Calcium; Calcium-Calmodulin-Dependent Protein Kinase Type 1; Calmodulin; Cysteine; Diamide; Glutathione; Ions; Mass Spectrometry; Protein Kinases; Signal Transduction | 2010 |
The redox-sensing regulator YodB senses quinones and diamide via a thiol-disulfide switch in Bacillus subtilis.
Topics: Amino Acid Sequence; Bacillus subtilis; Bacterial Proteins; Blotting, Western; Cysteine; Diamide; Disulfides; Models, Molecular; Molecular Sequence Annotation; Molecular Sequence Data; Mutation; Oxidation-Reduction; Quinones; Repressor Proteins; Reproducibility of Results; Sequence Alignment; Sulfhydryl Compounds | 2010 |
Plastidic phosphoglycerate kinase from Phaeodactylum tricornutum: on the critical role of cysteine residues for the enzyme function.
Topics: Amino Acid Sequence; Cloning, Molecular; Cysteine; Diamide; Diatoms; Disulfides; Dithiothreitol; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Enzyme Assays; Enzyme Inhibitors; Escherichia coli; Glutathione; Hydrogen Peroxide; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Nitroprusside; Oxidation-Reduction; Phosphoglycerate Kinase; Plasmids; Plastids; Recombinant Proteins; Sequence Alignment; Sulfenic Acids; Thioredoxins | 2012 |
Oxidant-mediated modification of the cellular thiols is sufficient for arginase activation in cultured cells.
Topics: Animals; Arginase; Buthionine Sulfoximine; Cattle; Cell Line, Tumor; Cell Survival; Cysteine; Diamide; Enzyme Activation; Glutathione; Glutathione Synthase; Humans; Kinetics; Ornithine; Oxidants; Oxidation-Reduction; Oxidative Stress | 2012 |
Inhibition of pyruvate kinase M2 by reactive oxygen species contributes to cellular antioxidant responses.
Topics: Acetylcysteine; Amino Acid Substitution; Animals; Antioxidants; Cell Line; Cell Line, Tumor; Cell Survival; Cysteine; Diamide; Enzyme Activators; Glucose; Glutathione; Humans; Mice; Mice, Nude; Mutant Proteins; Neoplasm Transplantation; Neoplasms, Experimental; Oxidation-Reduction; Oxidative Stress; Pentose Phosphate Pathway; Protein Subunits; Pyruvate Kinase; Reactive Oxygen Species; Transplantation, Heterologous | 2011 |
Structural insights into the redox-switch mechanism of the MarR/DUF24-type regulator HypR.
Topics: Bacillus subtilis; Bacterial Proteins; Base Sequence; Cysteine; Diamide; DNA-Binding Proteins; Gene Expression Regulation, Bacterial; Models, Molecular; Molecular Sequence Data; Nitroreductases; Operator Regions, Genetic; Oxidation-Reduction; Oxidoreductases; Sodium Hypochlorite; Stress, Physiological; Trans-Activators; Transcriptional Activation | 2012 |
Redox state of p63 and p73 core domains regulates sequence-specific DNA binding.
Topics: Base Sequence; Cysteine; Diamide; Dithiothreitol; DNA; DNA-Binding Proteins; Edetic Acid; Electrophoresis, Agar Gel; Electrophoretic Mobility Shift Assay; Humans; Nuclear Proteins; Oxidation-Reduction; Protein Interaction Mapping; Protein Structure, Tertiary; Tumor Protein p73; Tumor Suppressor Protein p53; Tumor Suppressor Proteins; Zinc | 2013 |
Distribution and infection-related functions of bacillithiol in Staphylococcus aureus.
Topics: Animals; Anti-Bacterial Agents; Antioxidants; Bacterial Load; Cell Line; Chromatography, High Pressure Liquid; Cysteine; Diamide; Drug Resistance, Bacterial; Epithelial Cells; Fosfomycin; Gene Expression; Glucosamine; Humans; Hydrogen Peroxide; Hypochlorous Acid; Macrophages; Mice; Oxidants; Staphylococcus aureus; Virulence Factors | 2013 |
90-kDa ribosomal S6 kinase 1 is inhibited by S-glutathionylation of its active-site cysteine residue during oxidative stress.
Topics: Animals; Brain; Catalytic Domain; Cysteine; Diamide; Epidermal Growth Factor; Glutathione; HEK293 Cells; Humans; Kinetics; Mice; Nitric Oxide Synthase Type I; Oxidative Stress; Phosphorylation; Protein Processing, Post-Translational; Ribosomal Protein S6 Kinases, 90-kDa | 2013 |
Redox modulation of plant developmental regulators from the class I TCP transcription factor family.
Topics: Arabidopsis; Arabidopsis Proteins; Cysteine; Diamide; Disulfides; DNA, Plant; Escherichia coli; Gene Expression Regulation, Plant; Glutathione; Hydrogen Peroxide; Models, Molecular; Mutation; Oxidation-Reduction; Oxidative Stress; Protein Multimerization; Protein Structure, Tertiary; Saccharomyces cerevisiae; Thioredoxin-Disulfide Reductase; Transcription Factors | 2013 |
Proteomic identification and quantification of S-glutathionylation in mouse macrophages using resin-assisted enrichment and isobaric labeling.
Topics: Animals; Cell Line; Cysteine; Diamide; Glutathione; Hydrogen Peroxide; Macrophages; Mass Spectrometry; Mice; Oxidation-Reduction; Oxidative Stress; Protein Processing, Post-Translational; Proteome; Proteomics; Staining and Labeling | 2014 |
S-Michael additions to chiral dehydroalanines as an entry to glycosylated cysteines and a sulfa-Tn antigen mimic.
Topics: Alanine; Antigens, Tumor-Associated, Carbohydrate; Carbohydrates; Cysteine; Diamide; Glycosylation; Models, Molecular; Molecular Conformation | 2014 |
Quantitative label-free redox proteomics of reversible cysteine oxidation in red blood cell membranes.
Topics: Cysteine; Cytoskeleton; Diamide; Disulfides; Erythrocyte Membrane; Hemoglobins; Humans; Membrane Proteins; Oxidation-Reduction; Oxidative Stress; Peroxiredoxins; Protein Binding; Protein Processing, Post-Translational; Proteomics | 2014 |
Redox status of serum apolipoprotein E and its impact on HDL cholesterol levels.
Topics: Apolipoprotein A-II; Apolipoprotein E2; Apolipoprotein E3; Apolipoprotein E4; Apolipoproteins E; Cholesterol, HDL; Cysteine; Diamide; Dimerization; Dithiothreitol; Electrophoretic Mobility Shift Assay; HEK293 Cells; Humans; Indicators and Reagents; Molecular Weight; Oxidation-Reduction; Photochemical Processes; Polyethylene Glycols; Solubility; Sulfhydryl Reagents; Ultraviolet Rays | 2017 |
The cysteine residue at 424th of pyruvate kinase M2 is crucial for tetramerization and responsiveness to oxidative stress.
Topics: Amino Acid Sequence; Carrier Proteins; Cysteine; Diamide; HeLa Cells; Humans; Membrane Proteins; Mutant Proteins; Mutation; Oxidation-Reduction; Oxidative Stress; Protein Multimerization; Structure-Activity Relationship; Thyroid Hormone-Binding Proteins; Thyroid Hormones | 2020 |
Covalent inhibition of P. falciparum ferredoxin-NADP
Topics: Antineoplastic Agents, Alkylating; Biocatalysis; Carmustine; Catalytic Domain; Cysteine; Diamide; Enzyme Inhibitors; Ferredoxin-NADP Reductase; Kinetics; Malaria, Falciparum; Molecular Structure; NADP; Organomercury Compounds; Plasmodium falciparum; Protein Binding; Protein Domains; Protozoan Proteins; Substrate Specificity | 2021 |
Contribution of Stenotrophomonas maltophilia MfsC transporter to protection against diamide and the regulation of its expression by the diamide responsive repressor DitR.
Topics: Bacterial Proteins; Cysteine; Diamide; Gene Expression Regulation, Bacterial; Membrane Transport Proteins; Promoter Regions, Genetic; Stenotrophomonas maltophilia | 2022 |