Page last updated: 2024-08-20

e-z cinnamic acid and Methylenedioxycinnamic acid

e-z cinnamic acid has been researched along with Methylenedioxycinnamic acid 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	0 (0.00)	29.6817
2010's	2 (100.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Abdelkadir, MJ; Artsen, CM; Blad, CC; Brussee, J; Ijzerman, AP; Klopman, C; Lane, JR; van Veldhoven, JP; Wolfram, DR	1
Blondel, A; Colas, C; Corringer, PJ; Delarue-Cochin, S; Joseph, D; Malliavin, T; Marteaux, J; Prevost, MS; Van Renterghem, C	1

Other Studies

2 other study(ies) available for e-z cinnamic acid and Methylenedioxycinnamic acid

Article	Year
Structure-activity relationships of trans-substituted-propenoic acid derivatives on the nicotinic acid receptor HCA2 (GPR109A). Bioorganic & medicinal chemistry letters, 2011, May-01, Volume: 21, Issue:9 Topics: Acrylates; Humans; Models, Molecular; Molecular Structure; Protein Binding; Receptors, G-Protein-Coupled; Receptors, Nicotinic; Structure-Activity Relationship	2011
Identification of cinnamic acid derivatives as novel antagonists of the prokaryotic proton-gated ion channel GLIC. Journal of medicinal chemistry, 2013, Jun-13, Volume: 56, Issue:11 Topics: Animals; Bacterial Proteins; Binding Sites; Caffeic Acids; Cinnamates; Computer Simulation; Cyanobacteria; Databases, Factual; Female; Hydrogen-Ion Concentration; Ligand-Gated Ion Channels; Models, Molecular; Oocytes; Patch-Clamp Techniques; Protein Multimerization; Protons; Stereoisomerism; Xenopus	2013

Article

Year

Structure-activity relationships of trans-substituted-propenoic acid derivatives on the nicotinic acid receptor HCA2 (GPR109A).

Bioorganic & medicinal chemistry letters, 2011, May-01, Volume: 21, Issue:9

Topics: Acrylates; Humans; Models, Molecular; Molecular Structure; Protein Binding; Receptors, G-Protein-Coupled; Receptors, Nicotinic; Structure-Activity Relationship

2011

Identification of cinnamic acid derivatives as novel antagonists of the prokaryotic proton-gated ion channel GLIC.

Journal of medicinal chemistry, 2013, Jun-13, Volume: 56, Issue:11

Topics: Animals; Bacterial Proteins; Binding Sites; Caffeic Acids; Cinnamates; Computer Simulation; Cyanobacteria; Databases, Factual; Female; Hydrogen-Ion Concentration; Ligand-Gated Ion Channels; Models, Molecular; Oocytes; Patch-Clamp Techniques; Protein Multimerization; Protons; Stereoisomerism; Xenopus

2013