Page last updated: 2024-09-02

sch 28080 and glutamic acid

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

Compound Research Comparison

Studies
(sch 28080)
Trials
(sch 28080)
Recent Studies (post-2010)
(sch 28080)
Studies
(glutamic acid)
Trials
(glutamic acid)
Recent Studies (post-2010) (glutamic acid)
21702041,75745212,876

Protein Interaction Comparison

ProteinTaxonomysch 28080 (IC50)glutamic acid (IC50)
Chain A, GLUTAMATE RECEPTOR SUBUNIT 2Rattus norvegicus (Norway rat)0.821
Chain A, Glutamate Receptor Subunit 2Rattus norvegicus (Norway rat)0.821
Chain B, Glutamate Receptor Subunit 2Rattus norvegicus (Norway rat)0.821
Metabotropic glutamate receptor 8Homo sapiens (human)0.0057
Glutamate receptor ionotropic, NMDA 2DHomo sapiens (human)0.07
Glutamate receptor ionotropic, NMDA 3BHomo sapiens (human)0.07
Glutamate receptor 1Rattus norvegicus (Norway rat)0.5885
Glutamate receptor 2Rattus norvegicus (Norway rat)0.5885
Glutamate receptor 3Rattus norvegicus (Norway rat)0.5885
Glutamate receptor 4Rattus norvegicus (Norway rat)0.5885
Glutamate receptor ionotropic, kainate 1Rattus norvegicus (Norway rat)0.38
Glutamate receptor ionotropic, NMDA 1 Rattus norvegicus (Norway rat)0.1533
Glutamate receptor ionotropic, kainate 2Rattus norvegicus (Norway rat)0.38
Glutamate receptor 1Homo sapiens (human)0.613
Glutamate receptor 2Homo sapiens (human)0.613
Glutamate receptor 3Homo sapiens (human)0.613
Glutamate receptor ionotropic, kainate 3Rattus norvegicus (Norway rat)0.38
Excitatory amino acid transporter 1Homo sapiens (human)207
Glutamate receptor 4Homo sapiens (human)0.613
Glutamate receptor ionotropic, NMDA 2A Rattus norvegicus (Norway rat)0.1533
Glutamate receptor ionotropic, NMDA 2BRattus norvegicus (Norway rat)0.1533
Glutamate receptor ionotropic, NMDA 2CRattus norvegicus (Norway rat)0.1533
Glutamate receptor ionotropic, kainate 4Rattus norvegicus (Norway rat)0.38
Glutamate receptor ionotropic, NMDA 1Homo sapiens (human)0.07
Glutamate receptor ionotropic, NMDA 2AHomo sapiens (human)0.07
Glutamate receptor ionotropic, NMDA 2BHomo sapiens (human)0.07
Glutamate receptor ionotropic, NMDA 2CHomo sapiens (human)0.07
Glutamate receptor ionotropic, NMDA 2DRattus norvegicus (Norway rat)0.1533
Glutamate receptor ionotropic, kainate 5Rattus norvegicus (Norway rat)0.38
Glutamate receptor ionotropic, NMDA 3AHomo sapiens (human)0.07
Glutamate receptor ionotropic, NMDA 3BRattus norvegicus (Norway rat)0.1533
Glutamate receptor ionotropic, NMDA 3ARattus norvegicus (Norway rat)0.1533

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 sch 28080 and glutamic acid

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