| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| S W French, R J Mayer, F Bardag-Gorce, M Ingelman-Sundberg, H Rouach, E Neve And, H Higashitsuj. The ubiquitin-proteasome 26s pathway in liver cell protein turnover: effect of ethanol and drugs. Alcoholism, clinical and experimental research. vol 25. issue 5 Suppl ISBRA. 2001-09-06. PMID:11391075. |
the presentations were (1) the ubiquitin-proteasome 26s pathway in liver cell protein turnover: effect of alcohol and drugs, by samuel w. french and f. bardag-gorce; (2) the role of cyp2e1 phosphorylation and degradation pathway in the induction of the enzyme, by magnus ingelman-sundberg; (3) role of proteasome in the proteolysis of oxidized proteins in experimental chronic alcoholism, by helen rouach; (4) alcohol, proteolysis and liver cancer, by r. j. mayer; (5) effect of ethanol feeding on the atp-ubiquitin-proteasome pathway in the liver cell, by f. bardag-gorce; (6) novel mechanisms and targets for intracellular transport of cyp2e1, by e. neve; and (7) gankyrin, an oncoprotein commonly over expressed in hepatoma, by h. higashitsuji. |
2001-09-06 |
2023-08-12 |
Not clear |
| E Plee-Gautier, F Foresto, R Ferrara, P Bodénez, B Simon, M Manno, F Berthou, D Luca. Genetic repeat polymorphism in the regulating region of CYP2E1: frequency and relationship with enzymatic activity in alcoholics. Alcoholism, clinical and experimental research. vol 25. issue 6. 2001-08-02. PMID:11410713. |
differences in the regulatory region of the cyp2e1 gene could be responsible for the interindividual variation in the cytochrome p-450 2e1 (cyp2e1) involved in ethanol oxidation. |
2001-08-02 |
2023-08-12 |
human |
| E Plee-Gautier, F Foresto, R Ferrara, P Bodénez, B Simon, M Manno, F Berthou, D Luca. Genetic repeat polymorphism in the regulating region of CYP2E1: frequency and relationship with enzymatic activity in alcoholics. Alcoholism, clinical and experimental research. vol 25. issue 6. 2001-08-02. PMID:11410713. |
its relationship with the previously described psti/rsai or drai cyp2e1 polymorphisms, alcoholism, alcoholic liver disease, and inducibility of cyp2e1 by ethanol was examined. |
2001-08-02 |
2023-08-12 |
human |
| C S Liebe. Liver diseases by alcohol and hepatitis C: early detection and new insights in pathogenesis lead to improved treatment. The American journal on addictions. vol 10. issue s1. 2001-07-26. PMID:11268819. |
chronic ethanol consumption increases cyp2e1, resulting in increased generation of toxic acetaldehyde and free radicals, tolerance to ethanol and other drugs, and multiple ethanol-drug interactions. |
2001-07-26 |
2023-08-12 |
Not clear |
| S Harad. [Classification of alcohol metabolizing enzymes and polymorphisms--specificity in Japanese]. Nihon Arukoru Yakubutsu Igakkai zasshi = Japanese journal of alcohol studies & drug dependence. vol 36. issue 2. 2001-07-19. PMID:11398342. |
the cytochrome p450 2e1 (cyp2e1) gene, which is mapped to chromosome 10q24.3-qter contributes also the conversion of ethanol to acetaldehyde. |
2001-07-19 |
2023-08-12 |
human |
| D G McCarve. ADH2 and CYP2E1 genetic polymorphisms: risk factors for alcohol-related birth defects. Drug metabolism and disposition: the biological fate of chemicals. vol 29. issue 4 Pt 2. 2001-06-14. PMID:11259352. |
the mechanism underlying this varying susceptibility may involve genetic differences in ethanol metabolism catalyzed by alcohol dehydrogenase (adh) and cytochrome p450 2e1 (cyp2e1). |
2001-06-14 |
2023-08-12 |
Not clear |
| D G McCarve. ADH2 and CYP2E1 genetic polymorphisms: risk factors for alcohol-related birth defects. Drug metabolism and disposition: the biological fate of chemicals. vol 29. issue 4 Pt 2. 2001-06-14. PMID:11259352. |
we recently described a 96-bp insertion polymorphism in the cyp2e1 regulatory region that is associated with enhanced cyp2e1 metabolic ability in the presence of ethanol intake or obesity, conditions associated with cyp2e1 induction (p < 0.01, both). |
2001-06-14 |
2023-08-12 |
Not clear |
| D Wu, A I Cederbau. Removal of glutathione produces apoptosis and necrosis in HepG2 cells overexpressing CYP2E1. Alcoholism, clinical and experimental research. vol 25. issue 4. 2001-06-14. PMID:11329505. |
previous studies have shown that addition of ethanol, iron, or arachidonic acid to hepg2 cells expressing cyp2e1 produced a loss in cell viability and caused apoptosis. |
2001-06-14 |
2023-08-12 |
Not clear |
| A Y Sun, G Y Su. Ethanol and oxidative mechanisms in the brain. Journal of biomedical science. vol 8. issue 1. 2001-05-31. PMID:11173974. |
although not yet well understood, ethanol may enhance ros production in brain through a number of pathways including increased generation of hydroxyethyl radicals, induction of cyp2e1, alteration of the cytokine signaling pathways for induction of inos and spla(2), and production of prostanoids through the pla(2)/cox pathways. |
2001-05-31 |
2023-08-12 |
Not clear |
| M Marí, D Wu, N Nieto, A I Cederbau. CYP2E1-dependent toxicity and up-regulation of antioxidant genes. Journal of biomedical science. vol 8. issue 1. 2001-05-31. PMID:11173976. |
induction of cytochrome p450 2e1 (cyp2e1) by ethanol appears to be one of the central pathways by which ethanol generates a state of oxidative stress. |
2001-05-31 |
2023-08-12 |
human |
| K S Salmela, I B Tsyrlov, C S Liebe. Azide inhibits human cytochrome P -4502E1, 1A2, and 3A4. Alcoholism, clinical and experimental research. vol 25. issue 2. 2001-04-26. PMID:11236840. |
recently, we showed that, in addition to cytochrome p-4502e1 (cyp2e1), cyp1a2 and cyp3a4 also contribute to the microsomal ethanol oxidizing system (meos). |
2001-04-26 |
2023-08-12 |
human |
| M Marí, A I Cederbau. Induction of catalase, alpha, and microsomal glutathione S-transferase in CYP2E1 overexpressing HepG2 cells and protection against short-term oxidative stress. Hepatology (Baltimore, Md.). vol 33. issue 3. 2001-04-12. PMID:11230746. |
induction of cytochrome p450 2e1 (cyp2e1) and the formation of reactive oxygen species (ros) appear to be one of the mechanisms by which ethanol is hepatotoxic. |
2001-04-12 |
2023-08-12 |
Not clear |
| M F McCart. Inhibition of CYP2E1 with natural agents may be a feasible strategy for minimizing the hepatotoxicity of ethanol. Medical hypotheses. vol 56. issue 1. 2001-03-01. PMID:11133247. |
inhibition of cyp2e1 with natural agents may be a feasible strategy for minimizing the hepatotoxicity of ethanol. |
2001-03-01 |
2023-08-12 |
Not clear |
| M F McCart. Inhibition of CYP2E1 with natural agents may be a feasible strategy for minimizing the hepatotoxicity of ethanol. Medical hypotheses. vol 56. issue 1. 2001-03-01. PMID:11133247. |
cyp2e1, induced in hepatocytes by heavy consumption of ethanol and certain other drugs, is a potent generator of superoxide, and is thereby thought to mediate the gravest aspects of alcoholic hepatotoxicity. |
2001-03-01 |
2023-08-12 |
Not clear |
| O Niemelä, S Parkkila, R O Juvonen, K Viitala, H V Gelboin, M Pasane. Cytochromes P450 2A6, 2E1, and 3A and production of protein-aldehyde adducts in the liver of patients with alcoholic and non-alcoholic liver diseases. Journal of hepatology. vol 33. issue 6. 2001-02-22. PMID:11131450. |
interaction between cyp2e1, ethanol metabolites, and enhanced lipid peroxidation is linked to the pathogenesis of alcoholic liver disease. |
2001-02-22 |
2023-08-12 |
Not clear |
| G J Gattás, J A Soares-Vieir. Cytochrome P450-2E1 and glutathione S-transferase mu polymorphisms among Caucasians and mulattoes from Brazil. Occupational medicine (Oxford, England). vol 50. issue 7. 2001-02-01. PMID:11198676. |
cytochrome p450 2e1 (cyp2e1) is a secondary enzyme that can metabolize ethanol, and glutathione s-transferase (gstm1) is thought to be involved in the detoxification of epoxides and polycyclic aromatic hydrocarbons. |
2001-02-01 |
2023-08-12 |
human |
| K S Jeong, Y Soh, J Jeng, M R Felder, J P Hardwick, B J Son. Cytochrome P450 2E1 (CYP2E1)-dependent production of a 37-kDa acetaldehyde-protein adduct in the rat liver. Archives of biochemistry and biophysics. vol 384. issue 1. 2001-01-25. PMID:11147839. |
ethanol-inducible cytochrome p450 2e1 (cyp2e1) has been shown to be involved in the metabolism of both ethanol and acetaldehyde. |
2001-01-25 |
2023-08-12 |
rat |
| R E Person, H Chen, A G Fantel, M R Jucha. Enzymic catalysis of the accumulation of acetaldehyde from ethanol in human prenatal cephalic tissues: evaluation of the relative contributions of CYP2E1, alcohol dehydrogenase, and catalase/peroxidases. Alcoholism, clinical and experimental research. vol 24. issue 9. 2001-01-18. PMID:11003211. |
enzymic catalysis of the accumulation of acetaldehyde from ethanol in human prenatal cephalic tissues: evaluation of the relative contributions of cyp2e1, alcohol dehydrogenase, and catalase/peroxidases. |
2001-01-18 |
2023-08-12 |
human |
| F Bardag-Gorce, Q X Yuan, J Li, B A French, C Fang, M Ingelman-Sundberg, S W Frenc. The effect of ethanol-induced cytochrome p4502E1 on the inhibition of proteasome activity by alcohol. Biochemical and biophysical research communications. vol 279. issue 1. 2001-01-18. PMID:11112412. |
the present investigation was undertaken to determine the effect of cyp2e1 induction by ethanol on the inhibition of proteasomal activity in wild-type and cyp2e1 knockout c57 black mice. |
2001-01-18 |
2023-08-12 |
mouse |
| F Bardag-Gorce, Q X Yuan, J Li, B A French, C Fang, M Ingelman-Sundberg, S W Frenc. The effect of ethanol-induced cytochrome p4502E1 on the inhibition of proteasome activity by alcohol. Biochemical and biophysical research communications. vol 279. issue 1. 2001-01-18. PMID:11112412. |
taken together, these results suggest that cyp2e1 induction was responsible for the decrease in proteasome activity seen in the wild-type mice which head to the accumulation of oxidized proteins which were increased as the result of free radicals generated by cyp2e1 metabolism of ethanol. |
2001-01-18 |
2023-08-12 |
mouse |