glutamic acid and sch 28080

glutamic acid has been researched along with sch 28080 in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's3 (60.00)18.2507
2000's1 (20.00)29.6817
2010's1 (20.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
De Pont, JJ; Klaassen, CH; Swarts, HP1
De Pont, JJ; Hermsen, HP; Koenderink, JB; Swarts, HG1
de Pont, JJ; Hermsen, HP; Koenderink, JB; Swarts, HG; Willems, PH1
De Pont, JJ; Hermsen, HP; Koenderink, JB; Swarts, HG; Wassink, L; Willems, PH1
Dürr, KL; Friedrich, T; Seuffert, I1

Other Studies

5 other study(ies) available for glutamic acid and sch 28080

ArticleYear
Involvement of glutamic acid 820 in K+ and SCH 28080 binding to gastric H+,K(+)-ATPase.
    Annals of the New York Academy of Sciences, 1997, Nov-03, Volume: 834

    Topics: Amino Acid Substitution; Animals; Cell Line; Cell Membrane; Enzyme Inhibitors; Gastric Mucosa; Glutamic Acid; H(+)-K(+)-Exchanging ATPase; Imidazoles; Kinetics; Mutagenesis, Site-Directed; Ouabain; Point Mutation; Potassium; Recombinant Proteins; Spodoptera; Swine; Transfection

1997
The negative charge of glutamic acid-820 in the gastric H+,K+-ATPase alpha-subunit is essential for K+ activation of the enzyme activity.
    The Biochemical journal, 1998, Apr-15, Volume: 331 ( Pt 2)

    Topics: Adenosine Triphosphate; Amino Acid Sequence; Animals; Baculoviridae; Electrochemistry; Enzyme Activation; Enzyme Inhibitors; Gene Expression; Glutamic Acid; H(+)-K(+)-Exchanging ATPase; Imidazoles; Molecular Sequence Data; Mutagenesis, Site-Directed; Phosphorylation; Potassium; Proton Pump Inhibitors; Recombinant Proteins; Spodoptera; Stomach; Structure-Activity Relationship

1998
Conformation-dependent inhibition of gastric H+,K+-ATPase by SCH 28080 demonstrated by mutagenesis of glutamic acid 820.
    Molecular pharmacology, 1999, Volume: 55, Issue:3

    Topics: Adenosine Triphosphate; Animals; Catalysis; Cells, Cultured; Enzyme Inhibitors; Glutamic Acid; H(+)-K(+)-Exchanging ATPase; Imidazoles; Mutagenesis; Phosphates; Phosphorylation; Potassium; Protein Conformation; Proton Pump Inhibitors; Rats; Recombinant Proteins; Stomach; Time Factors; Vanadates

1999
Mimicking of K+ activation by double mutation of glutamate 795 and glutamate 820 of gastric H+,K+-ATPase.
    Biochemistry, 2001, May-29, Volume: 40, Issue:21

    Topics: Adenosine Triphosphatases; Amino Acid Substitution; Animals; Baculoviridae; Enzyme Activation; Enzyme Inhibitors; Glutamic Acid; H(+)-K(+)-Exchanging ATPase; Hydroxylamine; Imidazoles; Mutagenesis, Site-Directed; Phosphorylation; Potassium; Proton Pump Inhibitors; Rats; Spodoptera; Stomach

2001
Deceleration of the E1P-E2P transition and ion transport by mutation of potentially salt bridge-forming residues Lys-791 and Glu-820 in gastric H+/K+-ATPase.
    The Journal of biological chemistry, 2010, Dec-10, Volume: 285, Issue:50

    Topics: Amino Acid Sequence; Animals; Cell Membrane; Electrophysiology; Gastric Mucosa; Glutamic Acid; H(+)-K(+)-Exchanging ATPase; Imidazoles; Lysine; Molecular Sequence Data; Mutation; Oocytes; Protein Conformation; Rats; Rhodamines; Salts; Sequence Homology, Amino Acid; Spectrophotometry, Atomic; Xenopus

2010