cysteine and antimony potassium tartrate

cysteine has been researched along with antimony potassium tartrate in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	1 (50.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Khayyal, MT; Saleh, S	1
Bhattacharjee, H; Rosen, BP; Ruan, X	1

Other Studies

2 other study(ies) available for cysteine and antimony potassium tartrate

Article	Year
Effect of cysteine on the hepatic toxicity and antischistosomal activity of antimonyl potassium tartrate. Bulletin of the World Health Organization, 1976, Volume: 53, Issue:4 Topics: Animals; Antimony; Antimony Potassium Tartrate; Chemical and Drug Induced Liver Injury; Cysteine; Liver; Male; Mice; Rabbits; Schistosomiasis	1976
Cys-113 and Cys-422 form a high affinity metalloid binding site in the ArsA ATPase. The Journal of biological chemistry, 2006, Apr-14, Volume: 281, Issue:15 Topics: Adenosine Triphosphatases; Adenosine Triphosphate; Antimony Potassium Tartrate; Arsenites; Binding Sites; Catalysis; Catalytic Domain; Codon; Cysteine; Dose-Response Relationship, Drug; Escherichia coli; Escherichia coli Proteins; Hydrolysis; Ion Pumps; Magnesium; Models, Chemical; Models, Molecular; Multienzyme Complexes; Mutagenesis, Site-Directed; Mutation; Nucleotides; Oligonucleotides; Plasmids; Protein Binding; Protein Conformation; Sodium Compounds; Time Factors; Trypsin	2006

Article

Year

Effect of cysteine on the hepatic toxicity and antischistosomal activity of antimonyl potassium tartrate.

Bulletin of the World Health Organization, 1976, Volume: 53, Issue:4

Topics: Animals; Antimony; Antimony Potassium Tartrate; Chemical and Drug Induced Liver Injury; Cysteine; Liver; Male; Mice; Rabbits; Schistosomiasis

1976

Cys-113 and Cys-422 form a high affinity metalloid binding site in the ArsA ATPase.

The Journal of biological chemistry, 2006, Apr-14, Volume: 281, Issue:15

Topics: Adenosine Triphosphatases; Adenosine Triphosphate; Antimony Potassium Tartrate; Arsenites; Binding Sites; Catalysis; Catalytic Domain; Codon; Cysteine; Dose-Response Relationship, Drug; Escherichia coli; Escherichia coli Proteins; Hydrolysis; Ion Pumps; Magnesium; Models, Chemical; Models, Molecular; Multienzyme Complexes; Mutagenesis, Site-Directed; Mutation; Nucleotides; Oligonucleotides; Plasmids; Protein Binding; Protein Conformation; Sodium Compounds; Time Factors; Trypsin

2006