proline and octanoic acid

proline has been researched along with octanoic acid in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	1 (50.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Filippi, C; Keriel, C; Leverve, X; Nogueira, V; Ronot, X; Sibille, B	1
Liaw, YC; Lin, SC; Lo, YC; Shaw, JF	1

Other Studies

2 other study(ies) available for proline and octanoic acid

Article	Year
2,4 Dinitrophenol-uncoupling effect on delta psi in living hepatocytes depends on reducing-equivalent supply. Cytometry, 1998, Jun-01, Volume: 32, Issue:2 Topics: 2,4-Dinitrophenol; Animals; Caprylates; Cells, Cultured; Flow Cytometry; Fluorescent Dyes; Intracellular Membranes; Kinetics; Liver; Male; Membrane Potentials; Methacrylates; Mitochondria, Liver; Proline; Rats; Rats, Wistar; Rhodamine 123; Rhodamines; Thiazoles; Uncoupling Agents	1998
Substrate specificities of Escherichia coli thioesterase I/protease I/lysophospholipase L1 are governed by its switch loop movement. Biochemistry, 2005, Feb-15, Volume: 44, Issue:6 Topics: Binding Sites; Caprylates; Catalysis; Coenzyme A; Crystallography, X-Ray; Escherichia coli Proteins; Hydrophobic and Hydrophilic Interactions; Leucine; Lysophospholipase; Models, Molecular; Multienzyme Complexes; Palmitoyl-CoA Hydrolase; Periplasmic Proteins; Proline; Protein Binding; Protein Structure, Secondary; Recombinant Proteins; Substrate Specificity; Thermodynamics	2005

Article

Year

2,4 Dinitrophenol-uncoupling effect on delta psi in living hepatocytes depends on reducing-equivalent supply.

Cytometry, 1998, Jun-01, Volume: 32, Issue:2

Topics: 2,4-Dinitrophenol; Animals; Caprylates; Cells, Cultured; Flow Cytometry; Fluorescent Dyes; Intracellular Membranes; Kinetics; Liver; Male; Membrane Potentials; Methacrylates; Mitochondria, Liver; Proline; Rats; Rats, Wistar; Rhodamine 123; Rhodamines; Thiazoles; Uncoupling Agents

1998

Substrate specificities of Escherichia coli thioesterase I/protease I/lysophospholipase L1 are governed by its switch loop movement.

Biochemistry, 2005, Feb-15, Volume: 44, Issue:6

Topics: Binding Sites; Caprylates; Catalysis; Coenzyme A; Crystallography, X-Ray; Escherichia coli Proteins; Hydrophobic and Hydrophilic Interactions; Leucine; Lysophospholipase; Models, Molecular; Multienzyme Complexes; Palmitoyl-CoA Hydrolase; Periplasmic Proteins; Proline; Protein Binding; Protein Structure, Secondary; Recombinant Proteins; Substrate Specificity; Thermodynamics

2005