cyclopentenone has been researched along with 4-hydroxy-2-nonenal in 3 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 3 (100.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Uchida, K | 1 |
Edes, K; Fitzpatrick, FA; Moos, PJ; Mullally, JE | 1 |
Fitzpatrick, FA; Mullally, JE; Wagner, TM | 1 |
1 review(s) available for cyclopentenone and 4-hydroxy-2-nonenal
Article | Year |
---|---|
Cellular response to bioactive lipid peroxidation products.
Topics: Aldehydes; Animals; Cyclooxygenase 2; Cyclopentanes; Gene Expression; Glutathione Transferase; Humans; Isoenzymes; Lipid Peroxidation; Membrane Proteins; Oxidative Stress; Prostaglandin-Endoperoxide Synthases; Signal Transduction | 2000 |
2 other study(ies) available for cyclopentenone and 4-hydroxy-2-nonenal
Article | Year |
---|---|
Cyclopentenone prostaglandins of the J series inhibit the ubiquitin isopeptidase activity of the proteasome pathway.
Topics: Aldehydes; Apoptosis; Biopolymers; Cyclin-Dependent Kinase Inhibitor p21; Cyclins; Cyclopentanes; Cysteine Endopeptidases; Cysteine Proteinase Inhibitors; Dose-Response Relationship, Drug; Endopeptidases; Epitopes; Genes, p53; Humans; Immunohistochemistry; Ketones; Models, Biological; Models, Chemical; Multienzyme Complexes; Peptide Hydrolases; Phosphorylation; Polyubiquitin; Prostaglandins; Proteasome Endopeptidase Complex; Protein Binding; Protein Conformation; Time Factors; Transcription, Genetic; Transcriptional Activation; Transfection; Tumor Cells, Cultured; Tumor Suppressor Protein p53; Ubiquitins | 2001 |
Reactive lipid species from cyclooxygenase-2 inactivate tumor suppressor LKB1/STK11: cyclopentenone prostaglandins and 4-hydroxy-2-nonenal covalently modify and inhibit the AMP-kinase kinase that modulates cellular energy homeostasis and protein translati
Topics: Aldehydes; AMP-Activated Protein Kinase Kinases; Cell Line, Tumor; Cyclooxygenase 2; Cyclopentanes; Energy Metabolism; Humans; Lipids; Mutagenesis, Site-Directed; Phosphotransferases (Phosphate Group Acceptor); Prostaglandins; Protein Biosynthesis; Protein Serine-Threonine Kinases | 2006 |