cysteine has been researched along with dithionite in 39 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 13 (33.33) | 18.7374 |
| 1990's | 13 (33.33) | 18.2507 |
| 2000's | 11 (28.21) | 29.6817 |
| 2010's | 2 (5.13) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Thorpe, C; Williams, CH | 1 |
| Bazer, FW; Roberts, RM; Sander, EG; Schlosnagle, DC | 1 |
| Ohnishi, T; Salerno, JC | 1 |
| Kenney, WC; Singer, TP | 1 |
| Hori, S | 1 |
| Salach, JI | 1 |
| Prongay, AJ; Williams, CH | 1 |
| Rothery, RA; Weiner, JH | 1 |
| Ahmed, SA; Claiborne, A | 1 |
| Ballou, DP; Distefano, MD; Massey, V; Miller, SM; Moore, MJ; Walsh, CT; Williams, CH | 1 |
| Ackrell, BA; Cecchini, G; Johnson, MK; Kearney, EB; Morningstar, JE | 1 |
| Frieden, E; Osaki, S; Sirivech, S | 1 |
| Bookjans, G; Shanmugam, KT; Spiller, H | 1 |
| Alvaro, RF; Arison, BH; Bagan, ES; Lu, AY; Vandenheuvel, WJ; Walker, RW; Wislocki, PG; Wolf, FJ | 1 |
| Olson, JS | 1 |
| Hidaka, M; Komagata, K; Kozaki, M; Masaki, H; Niimura, Y; Nishino, T; Ohnishi, K; Suzuki, H; Uchimura, T; Uozumi, T; Yokoyama, K | 1 |
| Fogarasi, M; Hnatowich, DJ; Rusckowski, M; Virzi, F; Winnard, P | 1 |
| Chen, A; Muddukrishna, SN; Qi, P; Rahn, J; Torok-Both, R | 1 |
| Crouse, BR; Dailey, HA; Finnegan, MG; Johnson, MK; Sellers, VM | 1 |
| Armstrong, FA; Bartlett, BM; Breton, JL; Busch, JL; James, R; Thomson, AJ | 1 |
| Mulrooney, SB; Veine, DM; Wang, PF; Williams, CH | 1 |
| Charrier, V; Claiborne, A; Luba, J | 1 |
| Claiborne, A; Mallett, TC; Parsonage, D | 1 |
| Arscott, LD; Gilberger, TW; Müller, S; Wang, PF; Williams, CH | 1 |
| Chan, JM; Christiansen, J; Dean, DR; Seefeldt, LC | 1 |
| Gaillard, J; Guigliarelli, B; Huber, JG; Kümmerle, R; Kyritsis, P; Moulis, JM; Münck, E; Popescu, C | 1 |
| Boxer, SG; Thomas, MR | 1 |
| Adams, MW; Brereton, PS; Calzolai, L; Gorst, CM; La Mar, GN; Sham, S; Webba da Silva, M | 1 |
| Morimoto, K; Nakai, M; Sato, S; Tabata, S | 1 |
| Allen, JW; Barker, PD; Ferguson, SJ | 1 |
| Farrell, SR; Thorpe, C | 1 |
| Hayashibara, M; London, E | 1 |
| Huang, HW; Inoue, M; Kataoka, K; Kitagawa, R; Naruse, D; Sakurai, T | 1 |
| Fujita, Y; Mizoguchi, T; Nomata, J; Tamiaki, H | 1 |
| Bonaventura, J; Montfort, WR; Rodríguez, MM; Schreiter, ER; Weichsel, A | 1 |
| Arrowsmith, CH; Binkowski, A; Brown, G; Edwards, AM; Joachimiak, A; Lukin, JA; Murzin, AG; Proudfoot, M; Sanders, SA; Savchenko, AV; Singer, A; Xu, L; Yakunin, AF; Zhang, R | 1 |
| Bröcker, MJ; Ganskow, S; Heathcote, P; Heinz, DW; Jahn, D; Moser, J; Schubert, WD; Virus, S | 1 |
| Coelho, C; González, PJ; João Romão, M; Moura, I; Moura, JG; Trincão, J | 1 |
| Jian, Y; Li, L; Lin, G; Nelson, RS; Telser, J; Yang, L | 1 |
39 other study(ies) available for cysteine and dithionite
| Article | Year |
|---|---|
Differential reactivity of the two active site cysteine residues generated on reduction of pig heart lipoamide dehydrogenase.
Topics: Anaerobiosis; Animals; Binding Sites; Cysteine; Dihydrolipoamide Dehydrogenase; Dithionite; Hydrogen-Ion Concentration; Iodoacetamide; Myocardium; NAD; Oxidation-Reduction; Protein Binding; Protein Conformation; Spectrophotometry; Spectrophotometry, Ultraviolet; Swine | 1976 |
Requirement of an essential thiol group and ferric iron for the activity of the progesterone-induced porcine uterine purple phosphatase.
Topics: Acid Phosphatase; Animals; Color; Cyanides; Cysteine; Dithionite; Dithiothreitol; Electron Spin Resonance Spectroscopy; Enzyme Activation; Enzyme Induction; Female; Ferric Compounds; Glutathione; Hydrogen-Ion Concentration; Iron; Kinetics; Mercaptoethanol; Progesterone; Sulfhydryl Compounds; Sulfites; Uterus | 1976 |
Tetranuclear and binuclear iron-sulfur clusters in succinate dehydrogenase: a method of iron quantitation by formation of paramagnetic complexes.
Topics: Binding Sites; Cysteine; Dithionite; Electron Spin Resonance Spectroscopy; Flavin-Adenine Dinucleotide; Iron; Iron-Sulfur Proteins; Metalloproteins; Nitric Oxide; Protein Binding; Protein Conformation; Succinate Dehydrogenase; Sulfur | 1976 |
Evidence for a thioether linkage between the flavin and polypeptide chain of Chromatium cytochrome c 552.
Topics: Acetals; Chemical Phenomena; Chemistry; Chromatium; Cysteine; Cytochrome c Group; Dithionite; Flavin-Adenine Dinucleotide; Magnetic Resonance Spectroscopy; Oxidation-Reduction; Spectrophotometry; Zinc | 1977 |
Effects of sulfhydryl agents on the activation of tryptophan-5-monooxygenase from bovine pineal glands.
Topics: 2,2'-Dipyridyl; Animals; Ascorbic Acid; Borohydrides; Cattle; Cysteine; Dithionite; Dithiothreitol; Enzyme Activation; Glutathione; Hydrogen-Ion Concentration; Iron; Kinetics; Mercaptoethanol; Mixed Function Oxygenases; Phenanthrolines; Pineal Gland; Sulfhydryl Reagents; Tryptophan Hydroxylase | 1975 |
Monoamine oxidase from beef liver mitochondria: simplified isolation procedure, properties, and determination of its cysteinyl flavin content.
Topics: Animals; Binding Sites; Cattle; Cysteine; Dithionite; Flavins; Iron; Mitochondria, Liver; Molecular Weight; Monoamine Oxidase; Oxidation-Reduction; Pargyline; Protein Binding; Spectrophotometry | 1979 |
Oxidation-reduction properties of Escherichia coli thioredoxin reductase altered at each active site cysteine residue.
Topics: Amino Acid Sequence; Anaerobiosis; Binding Sites; Cysteine; Dithionite; Escherichia coli; Flavin-Adenine Dinucleotide; Mathematics; Mutagenesis, Site-Directed; NAD; Oxidation-Reduction; Potentiometry; Recombinant Proteins; Spectrophotometry; Thioredoxin-Disulfide Reductase | 1992 |
Alteration of the iron-sulfur cluster composition of Escherichia coli dimethyl sulfoxide reductase by site-directed mutagenesis.
Topics: Amino Acid Sequence; Cell Membrane; Cysteine; Dimethyl Sulfoxide; Dithionite; Electron Spin Resonance Spectroscopy; Escherichia coli; Gene Amplification; Iron-Sulfur Proteins; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidoreductases | 1991 |
The streptococcal flavoprotein NADH oxidase. I. Evidence linking NADH oxidase and NADH peroxidase cysteinyl redox centers.
Topics: Amino Acid Sequence; Binding Sites; Circular Dichroism; Cysteine; Dithionite; Enterococcus faecalis; Flavoproteins; Hydrogen Peroxide; Kinetics; Molecular Sequence Data; Multienzyme Complexes; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Peroxidases; Protein Conformation; Spectrophotometry | 1989 |
Evidence for the participation of Cys558 and Cys559 at the active site of mercuric reductase.
Topics: Binding Sites; Cysteine; Disulfides; Dithionite; Dithiothreitol; Escherichia coli; Kinetics; NADP; Oxidoreductases; Protein Binding; Spectrophotometry | 1989 |
The high potential iron-sulfur center in Escherichia coli fumarate reductase is a three-iron cluster.
Topics: Amino Acid Sequence; Circular Dichroism; Cysteine; Dithionite; Electron Spin Resonance Spectroscopy; Escherichia coli; Iron-Sulfur Proteins; Metalloproteins; Multienzyme Complexes; Succinate Dehydrogenase; Temperature | 1985 |
The release of iron from horse spleen ferritin by reduced flavins.
Topics: Animals; Ascorbic Acid; Cysteine; Dithionite; Ferritins; Flavins; Glutathione; Horses; In Vitro Techniques; Iron; Kinetics; Oxidation-Reduction; Protein Binding; Riboflavin; Spleen; Thermodynamics | 1974 |
Regulation of hydrogenase activity in vegetative cells of Anabaena variabilis.
Topics: Aerobiosis; Cyanobacteria; Cysteine; Dithionite; Enzyme Induction; Hydrogenase; Kinetics; Light; Nitrogenase; Oxidoreductases | 1983 |
Drug residue formation from ronidazole, a 5-nitroimidazole. V. Cysteine adducts formed upon reduction of ronidazole by dithionite or rat liver enzymes in the presence of cysteine.
Topics: Animals; Chemical Phenomena; Chemistry; Cysteine; Dithionite; Magnetic Resonance Spectroscopy; Mass Spectrometry; Microsomes, Liver; Nitroimidazoles; Oxidation-Reduction; Rats; Ronidazole; Sulfites | 1984 |
Stopped-flow, rapid mixing measurements of ligand binding to hemoglobin and red cells.
Topics: Cyanides; Cysteine; Dithionite; Erythrocytes; Hemoglobins; Humans; Hydrogen-Ion Concentration; Kinetics; Ligands; Macromolecular Substances; Oxyhemoglobins; Spectrophotometry | 1981 |
Purification and analysis of a flavoprotein functional as NADH oxidase from Amphibacillus xylanus overexpressed in Escherichia coli.
Topics: Amino Acid Sequence; Bacteria; Catalysis; Cysteine; Dithionite; Flavins; Flavoproteins; Kinetics; Metals; Molecular Sequence Data; Multienzyme Complexes; NAD; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Recombinant Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Thioredoxin-Disulfide Reductase | 1994 |
Investigations of ascorbate for direct labeling of antibodies with technetium-99m.
Topics: Antibodies; Ascorbic Acid; Cysteine; Dithionite; Immunoglobulin G; Immunoglobulins, Intravenous; Sulfhydryl Compounds; Technetium | 1994 |
Direct 99mTc-labeling of antibodies by sodium dithionite reduction, and role of ascorbate as a stabilizer in cysteine challenge.
Topics: Animals; Antibodies, Monoclonal; Ascorbic Acid; Chromatography, High Pressure Liquid; Cysteine; Dithionite; Excipients; Humans; Immunoglobulin G; Isotope Labeling; Mice; Oxidation-Reduction; Sulfhydryl Compounds; Technetium Compounds | 1996 |
Site-directed mutagenesis and spectroscopic characterization of human ferrochelatase: identification of residues coordinating the [2Fe-2S] cluster.
Topics: Amino Acid Sequence; Animals; Cattle; Cloning, Molecular; Cysteine; Dithionite; Electron Spin Resonance Spectroscopy; Escherichia coli; Ferrochelatase; Humans; Iron-Sulfur Proteins; Mice; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Conformation; Recombinant Proteins; Sequence Homology, Amino Acid; Spectrum Analysis, Raman | 1996 |
[3Fe-4S] <--> [4Fe-4S] cluster interconversion in Desulfovibrio africanus ferredoxin III: properties of an Asp14 --> Cys mutant.
Topics: Amino Acid Sequence; Aspartic Acid; Cysteine; Desulfovibrio; Dithionite; Electrochemistry; Electron Spin Resonance Spectroscopy; Electrophoresis, Polyacrylamide Gel; Ferredoxins; Iron; Molecular Sequence Data; Mutagenesis; Restriction Mapping; Spectrophotometry, Ultraviolet; Sulfur | 1997 |
Formation and properties of mixed disulfides between thioredoxin reductase from Escherichia coli and thioredoxin: evidence that cysteine-138 functions to initiate dithiol-disulfide interchange and to accept the reducing equivalent from reduced flavin.
Topics: Cysteine; Disulfides; Dithionite; Dithionitrobenzoic Acid; Dithiothreitol; Escherichia coli; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Mutagenesis, Site-Directed; NADP; Osmolar Concentration; Oxidation-Reduction; Protein Conformation; Protein Engineering; Spectrometry, Fluorescence; Structure-Activity Relationship; Sulfhydryl Compounds; Thioredoxin-Disulfide Reductase; Thioredoxins | 1998 |
Coenzyme A-disulfide reductase from Staphylococcus aureus: evidence for asymmetric behavior on interaction with pyridine nucleotides.
Topics: Catalysis; Coenzyme A; Cysteine; Dithionite; Ferricyanides; Isoenzymes; Mass Spectrometry; NADH, NADPH Oxidoreductases; NADP; Oxidation-Reduction; Recombinant Proteins; Serine; Spectrometry, Fluorescence; Spectrophotometry; Staphylococcus aureus | 1999 |
Equilibrium analyses of the active-site asymmetry in enterococcal NADH oxidase: role of the cysteine-sulfenic acid redox center.
Topics: Bacterial Proteins; Binding Sites; Coenzymes; Cysteine; Dithionite; Electron Transport; Enzyme Stability; Hydrogen-Ion Concentration; Multienzyme Complexes; Mutagenesis, Site-Directed; NAD; NADH, NADPH Oxidoreductases; NADP; Oxidation-Reduction; Recombinant Proteins; Serine; Spectrometry, Fluorescence; Sulfenic Acids | 1999 |
Thioredoxin reductase from Plasmodium falciparum: evidence for interaction between the C-terminal cysteine residues and the active site disulfide-dithiol.
Topics: Alanine; Animals; Binding Sites; Cysteine; Disulfides; Dithionite; Dithionitrobenzoic Acid; Kinetics; Mutagenesis, Site-Directed; NADP; Oxidation-Reduction; Peptide Fragments; Plasmodium falciparum; Thioredoxin-Disulfide Reductase; Titrimetry; Toluene | 1999 |
Spectroscopic evidence for changes in the redox state of the nitrogenase P-cluster during turnover.
Topics: Amino Acid Substitution; Azotobacter vinelandii; Catalysis; Cysteine; Dithionite; Electron Spin Resonance Spectroscopy; Molybdoferredoxin; Mutagenesis, Site-Directed; Nitrogenase; Oxidation-Reduction | 1999 |
Unusual NMR, EPR, and Mössbauer properties of Chromatium vinosum 2[4Fe-4S] ferredoxin.
Topics: Bacterial Proteins; Chromatium; Cysteine; Dithionite; Electron Spin Resonance Spectroscopy; Electron Transport; Ferredoxins; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Spectroscopy, Mossbauer | 1999 |
19F NMR of trifluoroacetyl-labeled cysteine mutants of myoglobin: structural probes of nitric oxide bound to the H93G cavity mutant.
Topics: Animals; Carbon Monoxide; Cysteine; Dithionite; Fluorine; Glycine; Histidine; Ligands; Metmyoglobin; Mutagenesis, Site-Directed; Myoglobin; Nitric Oxide; Nuclear Magnetic Resonance, Biomolecular; Protein Binding; Protons; Sulfhydryl Compounds; Trifluoroacetic Acid; Whales | 2001 |
Solution NMR characterization of the thermodynamics of the disulfide bond orientational isomerism and its effect of cluster electronic properties for the hyperthermostable three-iron cluster ferredoxin from the archaeon Pyrococcus furiosus.
Topics: Amino Acid Sequence; Bridged-Ring Compounds; Cysteine; Disulfides; Dithionite; Electrons; Ferredoxins; Hydrolysis; Iron; Methanol; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Protein Structure, Secondary; Pyrococcus furiosus; Solutions; Stereoisomerism; Temperature; Thermodynamics | 2001 |
A HEAT-repeats containing protein, IaiH, stabilizes the iron-sulfur cluster bound to the cyanobacterial IscA homologue, IscA2.
Topics: Amino Acid Sequence; Amino Acid Substitution; Bacterial Proteins; Cyanobacteria; Cysteine; Dithionite; Edetic Acid; Escherichia coli; Iron-Sulfur Proteins; Molecular Sequence Data; Precipitin Tests; Protein Binding; Recombinant Proteins; Repetitive Sequences, Amino Acid; Spectrophotometry, Ultraviolet; Two-Hybrid System Techniques | 2003 |
A cytochrome b562 variant with a c-type cytochrome CXXCH heme-binding motif as a probe of the Escherichia coli cytochrome c maturation system.
Topics: Amino Acid Motifs; Cysteine; Cytochrome b Group; Cytochromes c; Disulfides; Dithionite; Dithiothreitol; Escherichia coli; Escherichia coli Proteins; Heme; Hemin; Mutation; Plasmids; Protein Binding; Protein Disulfide-Isomerases; Spectrometry, Mass, Electrospray Ionization; Spectrophotometry; Subcellular Fractions | 2003 |
Augmenter of liver regeneration: a flavin-dependent sulfhydryl oxidase with cytochrome c reductase activity.
Topics: Aerobiosis; Alanine; Amino Acid Sequence; Amino Acid Substitution; Anaerobiosis; Animals; Catalysis; Cysteine; Cytochrome Reductases; Dithionite; Electron Transport Complex IV; Flavoproteins; Humans; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Photochemistry; Rats; Structural Homology, Protein | 2005 |
Topography of diphtheria toxin A chain inserted into lipid vesicles.
Topics: 4-Chloro-7-nitrobenzofurazan; Bridged Bicyclo Compounds, Heterocyclic; Cysteine; Dimyristoylphosphatidylcholine; Diphtheria Toxin; Dithionite; Hydrogen-Ion Concentration; Lipid Bilayers; Membrane Fusion; Mutagenesis, Site-Directed; Peptide Fragments; Permeability; Phosphatidylcholines; Phosphatidylglycerols; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Protein Subunits; Protein Transport; Solutions; Spectrometry, Fluorescence; Tryptophan | 2005 |
Point mutations at the type I Cu ligands, Cys457 and Met467, and at the putative proton donor, Asp105, in Myrothecium verrucaria bilirubin oxidase and reactions with dioxygen.
Topics: Alanine; Amino Acid Substitution; Asparagine; Aspartic Acid; Copper; Cysteine; Dithionite; Fungal Proteins; Glutamic Acid; Glutamine; Hypocreales; Ligands; Methionine; Oxidation-Reduction; Oxidoreductases Acting on CH-CH Group Donors; Oxygen; Point Mutation; Protons; Serine | 2005 |
A second nitrogenase-like enzyme for bacteriochlorophyll biosynthesis: reconstitution of chlorophyllide a reductase with purified X-protein (BchX) and YZ-protein (BchY-BchZ) from Rhodobacter capsulatus.
Topics: Adenosine Triphosphate; Bacteriochlorophylls; Cysteine; Dithionite; DNA Primers; Models, Biological; Models, Chemical; Nitrogenase; Oxidoreductases Acting on CH-CH Group Donors; Oxygenases; Peptides; Phenotype; Plasmids; Rhodobacter capsulatus | 2006 |
S-nitrosylation-induced conformational change in blackfin tuna myoglobin.
Topics: Animals; Crystallography, X-Ray; Cysteine; Dithionite; Models, Molecular; Myoglobin; Nitric Oxide; Oxidation-Reduction; Protein Processing, Post-Translational; Protein Structure, Tertiary; Tuna | 2007 |
Biochemical and structural characterization of a novel family of cystathionine beta-synthase domain proteins fused to a Zn ribbon-like domain.
Topics: Amino Acid Motifs; Amino Acid Sequence; Animals; Ascorbic Acid; Calcium; Conserved Sequence; Cystathionine beta-Synthase; Cysteine; Cytochromes c; Dimerization; Dithionite; Escherichia coli; Horses; Iron; Models, Biological; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Myocardium; NAD; Oxidation-Reduction; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Pyrococcus furiosus; Pyrococcus horikoshii; Recombinant Proteins; Rubredoxins; Saccharomyces cerevisiae Proteins; Sequence Homology, Amino Acid; Thermoplasma; Zinc | 2008 |
ATP-driven reduction by dark-operative protochlorophyllide oxidoreductase from Chlorobium tepidum mechanistically resembles nitrogenase catalysis.
Topics: Adenosine Triphosphate; Catalysis; Chlorobium; Cysteine; Dithionite; Electrons; Escherichia coli; Heme; Kinetics; Leucine; Light; Lysine; Nitrogenase; Oxidoreductases; Protochlorophyllide | 2008 |
The crystal structure of Cupriavidus necator nitrate reductase in oxidized and partially reduced states.
Topics: Amino Acid Sequence; Catalytic Domain; Crystallography, X-Ray; Cupriavidus necator; Cysteine; Dithionite; Electron Spin Resonance Spectroscopy; Ionic Liquids; Molecular Sequence Data; Molybdenum; Nitrate Reductase; Periplasm; Protein Conformation | 2011 |
Mechanistic studies of the spore photoproduct lyase via a single cysteine mutation.
Topics: Bacillus subtilis; Catalytic Domain; Cysteine; Dithionite; Electron Transport; Iodoacetamide; Kinetics; Models, Molecular; Mutation; Proteins; Protons; Thymine | 2012 |