Compounds > arsenic acid

arsenic acid and tungstate

arsenic acid has been researched along with tungstate in 6 studies

Research

Studies (6)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's3 (50.00)18.2507
2000's2 (33.33)29.6817
2010's1 (16.67)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Crans, DC; Holz, RC; Que, L; Simone, CM1
Averill, BA; Merkx, M1
Keng, YF; Wu, L; Zhang, ZY1
Reiter, NJ; Rusnak, F; White, DJ1
Fisher, AJ; Lansdon, EB; Segel, IH1
Maret, W; Singh, KB1

Other Studies

6 other study(ies) available for arsenic acid and tungstate

ArticleYear
Interaction of porcine uterine fluid purple acid phosphatase with vanadate and vanadyl cation.
    Biochemistry, 1992, Dec-01, Volume: 31, Issue:47

    Topics: Acid Phosphatase; Animals; Anions; Arsenates; Binding Sites; Cations; Edetic Acid; Electron Spin Resonance Spectroscopy; Female; Iron; Isoenzymes; Kinetics; Metalloproteins; Molybdenum; Oxidation-Reduction; Phosphates; Rhenium; Swine; Tartrate-Resistant Acid Phosphatase; Tungsten; Tungsten Compounds; Vanadates; Vanadium

1992
The activity of oxidized bovine spleen purple acid phosphatase is due to an Fe(III)Zn(II) 'impurity'.
    Biochemistry, 1998, Aug-11, Volume: 37, Issue:32

    Topics: Acid Phosphatase; Animals; Apoenzymes; Arsenates; Binding, Competitive; Catalysis; Cattle; Edetic Acid; Electron Spin Resonance Spectroscopy; Enzyme Activation; Ferric Compounds; Glycoproteins; Kinetics; Molybdenum; Oxidation-Reduction; Phosphates; Spleen; Tungsten Compounds; Zinc

1998
Probing the function of the conserved tryptophan in the flexible loop of the Yersinia protein-tyrosine phosphatase.
    European journal of biochemistry, 1999, Volume: 259, Issue:3

    Topics: Arsenates; Bacterial Proteins; Binding Sites; Enzyme Inhibitors; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Molecular Conformation; Mutagenesis, Site-Directed; Protein Binding; Protein Tyrosine Phosphatases; Tryptophan; Tungsten Compounds; Yersinia

1999
Inhibition of bacteriophage lambda protein phosphatase by organic and oxoanion inhibitors.
    Biochemistry, 2002, Jan-22, Volume: 41, Issue:3

    Topics: Anions; Arsenates; Bacteriophage lambda; Binding, Competitive; Electron Spin Resonance Spectroscopy; Enzyme Inhibitors; Hydroxamic Acids; Kinetics; Magnetic Resonance Spectroscopy; Magnetics; Manganese; Molybdenum; Phosphonoacetic Acid; Protein Conformation; Protein Tyrosine Phosphatases; Receptor-Like Protein Tyrosine Phosphatases, Class 2; Tungsten Compounds; Vanadates

2002
Human 3'-phosphoadenosine 5'-phosphosulfate synthetase (isoform 1, brain): kinetic properties of the adenosine triphosphate sulfurylase and adenosine 5'-phosphosulfate kinase domains.
    Biochemistry, 2004, Apr-13, Volume: 43, Issue:14

    Topics: Adenosine Phosphosulfate; Adenosine Triphosphate; Arsenates; Binding, Competitive; Brain; Chromium; Humans; Inorganic Pyrophosphatase; Isoenzymes; Kinetics; Molecular Weight; Molybdenum; Multienzyme Complexes; Phosphotransferases (Alcohol Group Acceptor); Protein Structure, Tertiary; Recombinant Proteins; Selenic Acid; Selenium Compounds; Substrate Specificity; Sulfate Adenylyltransferase; Tungsten Compounds

2004
The interactions of metal cations and oxyanions with protein tyrosine phosphatase 1B.
    Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine, 2017, Volume: 30, Issue:4

    Topics: Arsenates; Cadmium; Cations, Divalent; Copper; Enzyme Assays; Enzyme Inhibitors; Glutathione; Humans; Hydrogen-Ion Concentration; Kinetics; Molybdenum; Nitrates; Protein Binding; Protein Tyrosine Phosphatase, Non-Receptor Type 1; Recombinant Proteins; Solutions; Tungsten Compounds; Vanadates; Zinc

2017