cysteine sulfinic acid has been researched along with histidine in 4 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 3 (75.00) | 29.6817 |
2010's | 1 (25.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Bulaj, G; Burrows, CJ; Goldenberg, DP; Van Horn, JD | 1 |
Banik, JJ; Chai, SC; Jerkins, AA; Maroney, MJ; Pinkham, JL; Shalev, I; Uden, PC | 1 |
Hao, Q; Simmons, CR; Stipanuk, MH | 1 |
Her, AS; Huo, Y; Liu, P; Raso, F; Song, H; Zhen, Z | 1 |
4 other study(ies) available for cysteine sulfinic acid and histidine
Article | Year |
---|---|
The Cys-Xaa-His metal-binding motif: [N] versus [S] coordination and nickel-mediated formation of cysteinyl sulfinic acid.
Topics: Alkylation; Amino Acid Motifs; Chromatography, High Pressure Liquid; Copper; Cysteine; Glycine; Histidine; Humans; Hydrogen-Ion Concentration; Lysine; Metalloproteins; Metals; Molecular Structure; Neurotransmitter Agents; Nickel; Oxidation-Reduction; Peptides | 2003 |
Heterologous expression, purification, and characterization of recombinant rat cysteine dioxygenase.
Topics: Animals; Catalysis; Chromatography, High Pressure Liquid; Cysteine; Cysteine Dioxygenase; Dioxygenases; DNA, Complementary; Escherichia coli; Histidine; Homocysteine; Hydrogen-Ion Concentration; Iron; Kinetics; Models, Chemical; Open Reading Frames; Oxygen; Protein Structure, Tertiary; Rats; Recombinant Proteins; Spectrometry, Mass, Electrospray Ionization; Temperature; Time Factors | 2005 |
Preparation, crystallization and X-ray diffraction analysis to 1.5 A resolution of rat cysteine dioxygenase, a mononuclear iron enzyme responsible for cysteine thiol oxidation.
Topics: Animals; Binding Sites; Catalysis; Cloning, Molecular; Crystallization; Cysteine; Cysteine Dioxygenase; Dioxygenases; DNA, Complementary; Factor Xa; Histidine; Iron; Liver; Oxidation-Reduction; Oxygen; Rats; Recombinant Fusion Proteins; Recombinant Proteins; Solubility; Sulfhydryl Compounds; Temperature; X-Ray Diffraction | 2005 |
Cysteine oxidation reactions catalyzed by a mononuclear non-heme iron enzyme (OvoA) in ovothiol biosynthesis.
Topics: Betaine; Catalysis; Cysteine; Cysteine Dioxygenase; Heme; Histidine; Humans; Methylhistidines; Models, Biological; Molecular Structure; Mycobacterium smegmatis; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction | 2014 |