Page last updated: 2024-08-23

sulfur and xanthine

sulfur has been researched along with xanthine in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Eger, BT; Hille, R; Matsumoto, K; Nishino, T; Okamoto, K; Pai, EF	1
Hille, R; Igarashi, K; Leimkühler, S; Nishino, T; Stockert, AL	1

Other Studies

2 other study(ies) available for sulfur and xanthine

Article	Year
The crystal structure of xanthine oxidoreductase during catalysis: implications for reaction mechanism and enzyme inhibition. Proceedings of the National Academy of Sciences of the United States of America, 2004, May-25, Volume: 101, Issue:21 Topics: Animals; Catalysis; Crystallography, X-Ray; Enzyme Inhibitors; Hydroxides; Hydroxylation; Ligands; Milk; Models, Chemical; Models, Molecular; Molybdenum; Oxidoreductases; Oxygen; Structure-Activity Relationship; Sulfur; Xanthine; Xanthine Dehydrogenase	2004
The role of active site glutamate residues in catalysis of Rhodobacter capsulatus xanthine dehydrogenase. The Journal of biological chemistry, 2004, Sep-24, Volume: 279, Issue:39 Topics: Binding Sites; Catalysis; Crystallography, X-Ray; Dimerization; Dithionite; Dose-Response Relationship, Drug; Glutamic Acid; Hydrogen-Ion Concentration; Kinetics; Models, Chemical; Mutation; NAD; Oxygen; Protein Binding; Protein Structure, Tertiary; Rhodobacter capsulatus; Spectrophotometry; Substrate Specificity; Sulfur; Time Factors; Ultraviolet Rays; Uric Acid; Xanthine; Xanthine Dehydrogenase	2004

Article

Year

The crystal structure of xanthine oxidoreductase during catalysis: implications for reaction mechanism and enzyme inhibition.

Proceedings of the National Academy of Sciences of the United States of America, 2004, May-25, Volume: 101, Issue:21

Topics: Animals; Catalysis; Crystallography, X-Ray; Enzyme Inhibitors; Hydroxides; Hydroxylation; Ligands; Milk; Models, Chemical; Models, Molecular; Molybdenum; Oxidoreductases; Oxygen; Structure-Activity Relationship; Sulfur; Xanthine; Xanthine Dehydrogenase

2004

The role of active site glutamate residues in catalysis of Rhodobacter capsulatus xanthine dehydrogenase.

The Journal of biological chemistry, 2004, Sep-24, Volume: 279, Issue:39

Topics: Binding Sites; Catalysis; Crystallography, X-Ray; Dimerization; Dithionite; Dose-Response Relationship, Drug; Glutamic Acid; Hydrogen-Ion Concentration; Kinetics; Models, Chemical; Mutation; NAD; Oxygen; Protein Binding; Protein Structure, Tertiary; Rhodobacter capsulatus; Spectrophotometry; Substrate Specificity; Sulfur; Time Factors; Ultraviolet Rays; Uric Acid; Xanthine; Xanthine Dehydrogenase

2004