Page last updated: 2024-09-02

sch 28080 and oligomycins

sch 28080 has been researched along with oligomycins in 2 studies

Compound Research Comparison

Studies (sch 28080)	Trials (sch 28080)	Recent Studies (post-2010) (sch 28080)	Studies (oligomycins)	Trials (oligomycins)	Recent Studies (post-2010) (oligomycins)
217	0	20	3,033	0	265

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
De Pont, JJ; Koenderink, JB; Swarts, HG; Willems, PH	2

Other Studies

2 other study(ies) available for sch 28080 and oligomycins

Article	Year
The non-gastric H,K-ATPase is oligomycin-sensitive and can function as an H+,NH4(+)-ATPase. The Journal of biological chemistry, 2005, Sep-30, Volume: 280, Issue:39 Topics: Adenosine Triphosphatases; Ammonia; Animals; Baculoviridae; Binding Sites; Blotting, Western; Cation Transport Proteins; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Enzyme Inhibitors; H(+)-K(+)-Exchanging ATPase; Imidazoles; Kinetics; Mutagenesis, Site-Directed; Oligomycins; Ouabain; Phosphorylation; Potassium; Protein Binding; Protein Conformation; Protein Subunits; Rats; Recombinant Proteins; Sequence Deletion; Sodium; Spodoptera; Vanadates	2005
The human non-gastric H,K-ATPase has a different cation specificity than the rat enzyme. Biochimica et biophysica acta, 2007, Volume: 1768, Issue:3 Topics: Adenosine Triphosphatases; Amino Acid Sequence; Ammonia; Animals; Baculoviridae; Catalytic Domain; Cations; Cell Line; Enzyme Inhibitors; Escherichia coli; H(+)-K(+)-Exchanging ATPase; Humans; Imidazoles; Inhibitory Concentration 50; Kinetics; Magnesium; Oligomycins; Ouabain; Phosphorylation; Potassium; Protein Structure, Tertiary; Protein Subunits; Rats; Recombinant Proteins; Sodium; Species Specificity; Spodoptera	2007

Article

Year

The non-gastric H,K-ATPase is oligomycin-sensitive and can function as an H+,NH4(+)-ATPase.

The Journal of biological chemistry, 2005, Sep-30, Volume: 280, Issue:39

Topics: Adenosine Triphosphatases; Ammonia; Animals; Baculoviridae; Binding Sites; Blotting, Western; Cation Transport Proteins; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Enzyme Inhibitors; H(+)-K(+)-Exchanging ATPase; Imidazoles; Kinetics; Mutagenesis, Site-Directed; Oligomycins; Ouabain; Phosphorylation; Potassium; Protein Binding; Protein Conformation; Protein Subunits; Rats; Recombinant Proteins; Sequence Deletion; Sodium; Spodoptera; Vanadates

2005

The human non-gastric H,K-ATPase has a different cation specificity than the rat enzyme.

Biochimica et biophysica acta, 2007, Volume: 1768, Issue:3

Topics: Adenosine Triphosphatases; Amino Acid Sequence; Ammonia; Animals; Baculoviridae; Catalytic Domain; Cations; Cell Line; Enzyme Inhibitors; Escherichia coli; H(+)-K(+)-Exchanging ATPase; Humans; Imidazoles; Inhibitory Concentration 50; Kinetics; Magnesium; Oligomycins; Ouabain; Phosphorylation; Potassium; Protein Structure, Tertiary; Protein Subunits; Rats; Recombinant Proteins; Sodium; Species Specificity; Spodoptera

2007