Compounds > 2-(4-amylcinnamoyl)amino-4-chlorobenzoic-acid

2-(4-amylcinnamoyl)amino-4-chlorobenzoic-acid and 4-amylcinnamoylanthranilic-acid

2-(4-amylcinnamoyl)amino-4-chlorobenzoic-acid has been researched along with 4-amylcinnamoylanthranilic-acid* in 2 studies

Other Studies

2 other study(ies) available for 2-(4-amylcinnamoyl)amino-4-chlorobenzoic-acid and 4-amylcinnamoylanthranilic-acid

Article	Year
Cytosolic Phospholipase A Infection and immunity, 2017, Volume: 85, Issue:11 Pulmonary infection by Topics: Animals; Arachidonic Acid; Bacteremia; Cell Line, Tumor; Chemotactic Factors; Chlorobenzoates; Cinnamates; Cyclohexanones; Enzyme Inhibitors; Epithelial Cells; Group IV Phospholipases A2; Host-Pathogen Interactions; Humans; Lung; Mice; Mice, Inbred BALB C; Mice, Knockout; Neutrophil Infiltration; Neutrophils; ortho-Aminobenzoates; Pneumococcal Infections; Pneumonia, Bacterial; Streptococcus pneumoniae; Survival Analysis; Transendothelial and Transepithelial Migration	2017
Arachidonyltrifluoromethy ketone, a phospholipase A(2) antagonist, induces dispersal of both Golgi stack- and trans Golgi network-resident proteins throughout the cytoplasm. Biochemical and biophysical research communications, 2001, Feb-23, Volume: 281, Issue:2 Arachidonyltrifluoromethy ketone (AACOCF(3)), a phospholipase A(2) antagonist, reversibly induced dispersal of Golgi stack- and trans Golgi network (TGN)-resident proteins throughout the cytoplasm in NRK cells as followed by immunocytochemical staining of ManII and TGN38, respectively. The action of AACOCF(3) was partly blocked by other PLA(2) antagonists, suggesting it be not caused by a general inhibition of phospholipase A(2). AACOCF(3) neither dissociated beta-COP from membranes nor prevented brefeldin A-induced beta-COP release. Action of AACOCF(3) on the Golgi stack and TGN is different from that of brefeldin A and nordihydroguaiaretic acid. The most prominent difference is that the Golgi stack and TGN showed a similar sensitivity to AACOCF(3), while the TGN was dispersed more slowly than the Golgi stack in brefeldin A- or nordihydroguaiaretic acid-treated NRK cells. This novel action of AACOCF(3) may be used as pharmacological tool and give new insights into vesicle-mediated traffic and Golgi membrane dynamics. Topics: Aminobenzoates; Animals; Arachidonic Acids; Biological Transport; Brefeldin A; Cell Line; Chlorobenzoates; Cinnamates; Coatomer Protein; Cytoplasm; Dose-Response Relationship, Drug; Endoplasmic Reticulum; Enzyme Inhibitors; Golgi Apparatus; Masoprocol; Membrane Proteins; Microscopy, Fluorescence; Naphthalenes; ortho-Aminobenzoates; Phospholipases A; Pyrones; Time Factors	2001

Article

Year

Cytosolic Phospholipase A

Infection and immunity, 2017, Volume: 85, Issue:11

Pulmonary infection by

Topics: Animals; Arachidonic Acid; Bacteremia; Cell Line, Tumor; Chemotactic Factors; Chlorobenzoates; Cinnamates; Cyclohexanones; Enzyme Inhibitors; Epithelial Cells; Group IV Phospholipases A2; Host-Pathogen Interactions; Humans; Lung; Mice; Mice, Inbred BALB C; Mice, Knockout; Neutrophil Infiltration; Neutrophils; ortho-Aminobenzoates; Pneumococcal Infections; Pneumonia, Bacterial; Streptococcus pneumoniae; Survival Analysis; Transendothelial and Transepithelial Migration

2017

Arachidonyltrifluoromethy ketone, a phospholipase A(2) antagonist, induces dispersal of both Golgi stack- and trans Golgi network-resident proteins throughout the cytoplasm.

Biochemical and biophysical research communications, 2001, Feb-23, Volume: 281, Issue:2

Arachidonyltrifluoromethy ketone (AACOCF(3)), a phospholipase A(2) antagonist, reversibly induced dispersal of Golgi stack- and trans Golgi network (TGN)-resident proteins throughout the cytoplasm in NRK cells as followed by immunocytochemical staining of ManII and TGN38, respectively. The action of AACOCF(3) was partly blocked by other PLA(2) antagonists, suggesting it be not caused by a general inhibition of phospholipase A(2). AACOCF(3) neither dissociated beta-COP from membranes nor prevented brefeldin A-induced beta-COP release. Action of AACOCF(3) on the Golgi stack and TGN is different from that of brefeldin A and nordihydroguaiaretic acid. The most prominent difference is that the Golgi stack and TGN showed a similar sensitivity to AACOCF(3), while the TGN was dispersed more slowly than the Golgi stack in brefeldin A- or nordihydroguaiaretic acid-treated NRK cells. This novel action of AACOCF(3) may be used as pharmacological tool and give new insights into vesicle-mediated traffic and Golgi membrane dynamics.

Topics: Aminobenzoates; Animals; Arachidonic Acids; Biological Transport; Brefeldin A; Cell Line; Chlorobenzoates; Cinnamates; Coatomer Protein; Cytoplasm; Dose-Response Relationship, Drug; Endoplasmic Reticulum; Enzyme Inhibitors; Golgi Apparatus; Masoprocol; Membrane Proteins; Microscopy, Fluorescence; Naphthalenes; ortho-Aminobenzoates; Phospholipases A; Pyrones; Time Factors

2001