Page last updated: 2024-08-17

aspartic acid and nicorandil

aspartic acid has been researched along with nicorandil in 2 studies

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
Baert, B; Beetens, J; Bodé, S; De Spiegeleer, B; Deconinck, E; Lambert, J; Slegers, G; Slodicka, M; Stoppie, P; Van Gele, M; Vander Heyden, Y	1
Hibino, H; Ishii, M; Kurachi, Y; Yamada, M	1

Other Studies

2 other study(ies) available for aspartic acid and nicorandil

Article	Year
Transdermal penetration behaviour of drugs: CART-clustering, QSPR and selection of model compounds. Bioorganic & medicinal chemistry, 2007, Nov-15, Volume: 15, Issue:22 Topics: Anti-Inflammatory Agents; Cell Membrane Permeability; Cluster Analysis; Drug Evaluation, Preclinical; Humans; Models, Biological; Predictive Value of Tests; Quantitative Structure-Activity Relationship; Regression Analysis; Skin; Skin Absorption	2007
Mutation in nucleotide-binding domains of sulfonylurea receptor 2 evokes Na-ATP-dependent activation of ATP-sensitive K+ channels: implication for dimerization of nucleotide-binding domains to induce channel opening. Molecular pharmacology, 2004, Volume: 66, Issue:4 Topics: Adenosine Triphosphate; Amino Acid Substitution; Animals; Asparagine; Aspartic Acid; ATP-Binding Cassette Transporters; Binding Sites; Dimerization; Glutamic Acid; Glutamine; Humans; Membrane Proteins; Mice; Mutation; Nicorandil; Nucleotides; Potassium Channels; Potassium Channels, Inwardly Rectifying; Protein Structure, Tertiary; Receptors, Drug; Sodium; Sulfonylurea Receptors	2004

Article

Year

Transdermal penetration behaviour of drugs: CART-clustering, QSPR and selection of model compounds.

Bioorganic & medicinal chemistry, 2007, Nov-15, Volume: 15, Issue:22

Topics: Anti-Inflammatory Agents; Cell Membrane Permeability; Cluster Analysis; Drug Evaluation, Preclinical; Humans; Models, Biological; Predictive Value of Tests; Quantitative Structure-Activity Relationship; Regression Analysis; Skin; Skin Absorption

2007

Mutation in nucleotide-binding domains of sulfonylurea receptor 2 evokes Na-ATP-dependent activation of ATP-sensitive K+ channels: implication for dimerization of nucleotide-binding domains to induce channel opening.

Molecular pharmacology, 2004, Volume: 66, Issue:4

Topics: Adenosine Triphosphate; Amino Acid Substitution; Animals; Asparagine; Aspartic Acid; ATP-Binding Cassette Transporters; Binding Sites; Dimerization; Glutamic Acid; Glutamine; Humans; Membrane Proteins; Mice; Mutation; Nicorandil; Nucleotides; Potassium Channels; Potassium Channels, Inwardly Rectifying; Protein Structure, Tertiary; Receptors, Drug; Sodium; Sulfonylurea Receptors

2004