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On the performance of trimetazidine and vitamin e as pharmacoprotection agents in cyclosporin a-induced toxicity.

ISRN pharmacology

Cristina de LC, Del Rosario RM, Carmen Rosa A, Ana Veronica O.
PMID: 23691353
ISRN Pharmacol. 2013 Apr 11;2013:605640. doi: 10.1155/2013/605640. Print 2013.

The immunosuppressant drug cyclosporin A (CyA) has been used in diseases with immunological basis and in transplant patients. Nephrotoxicity and hepatotoxicity are the main adverse effects of this drug. To find a protective drug against those effects we assayed...

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Cristina de LC, Del Rosario RM, Carmen Rosa A, et al. On the performance of trimetazidine and vitamin e as pharmacoprotection agents in cyclosporin a-induced toxicity. ISRN Pharmacol. 2013;2013:605640doi: 10.1155/2013/605640.
Cristina, d. e. . L. C., Del Rosario, R. M., Carmen Rosa, A., & Ana Veronica, O. (2013). On the performance of trimetazidine and vitamin e as pharmacoprotection agents in cyclosporin a-induced toxicity. ISRN pharmacology, 2013605640. https://doi.org/10.1155/2013/605640
Cristina, De la Cruz Rodríguez Lilia, et al. "On the performance of trimetazidine and vitamin e as pharmacoprotection agents in cyclosporin a-induced toxicity." ISRN pharmacology vol. 2013 (2013): 605640. doi: https://doi.org/10.1155/2013/605640
Cristina de LC, Del Rosario RM, Carmen Rosa A, Ana Veronica O. On the performance of trimetazidine and vitamin e as pharmacoprotection agents in cyclosporin a-induced toxicity. ISRN Pharmacol. 2013 Apr 11;2013:605640. doi: 10.1155/2013/605640. Print 2013. PMID: 23691353; PMCID: PMC3654278.
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Decreased sirtuin 4 expression is associated with poor prognosis in patients with invasive breast cancer.

Oncology letters

Shi Q, Liu T, Zhang X, Geng J, He X, Nu M, Pang D.
PMID: 27698834
Oncol Lett. 2016 Oct;12(4):2606-2612. doi: 10.3892/ol.2016.5021. Epub 2016 Aug 16.

Aberrant metabolism is a hallmark of human cancer. Glutamine metabolism has been identified as a central metabolic pathway in cancer and thus, targeting glutamine metabolism may exhibit therapeutic potential. Sirtuin 4 (SIRT4) is an important molecule that mediates the...

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Shi Q, Liu T, Zhang X, et al. Decreased sirtuin 4 expression is associated with poor prognosis in patients with invasive breast cancer. Oncol Lett. 2016;12(4):2606-2612doi: 10.3892/ol.2016.5021.
Shi, Q., Liu, T., Zhang, X., Geng, J., He, X., Nu, M., & Pang, D. (2016). Decreased sirtuin 4 expression is associated with poor prognosis in patients with invasive breast cancer. Oncology letters, 12(4), 2606-2612. https://doi.org/10.3892/ol.2016.5021
Shi, Qingyu, et al. "Decreased sirtuin 4 expression is associated with poor prognosis in patients with invasive breast cancer." Oncology letters vol. 12,4 (2016): 2606-2612. doi: https://doi.org/10.3892/ol.2016.5021
Shi Q, Liu T, Zhang X, Geng J, He X, Nu M, Pang D. Decreased sirtuin 4 expression is associated with poor prognosis in patients with invasive breast cancer. Oncol Lett. 2016 Oct;12(4):2606-2612. doi: 10.3892/ol.2016.5021. Epub 2016 Aug 16. PMID: 27698834; PMCID: PMC5038587.
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Enzymes of nitrogen assimilation in maize roots.

Planta

Oaks A, Stulen I, Jones K, Winspear MJ, Misra S, Boesel IL.
PMID: 24310191
Planta. 1980 Oct;148(5):477-84. doi: 10.1007/BF00552663.

The enzymes nitrate reductase (NR), glutamate dehydrogenase (GDH), glutamate synthase (GOGAT), glutamine synthetase (GS) and asparagine synthetase (AS) have been assayed in various regions along the seedling root ofZea mays L. In the intact attached root and calculated on...

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Oaks A, Stulen I, Jones K, et al. Enzymes of nitrogen assimilation in maize roots. Planta. 1980;148(5):477-84doi: 10.1007/BF00552663.
Oaks, A., Stulen, I., Jones, K., Winspear, M. J., Misra, S., & Boesel, I. L. (1980). Enzymes of nitrogen assimilation in maize roots. Planta, 148(5), 477-84. https://doi.org/10.1007/BF00552663
Oaks, A, et al. "Enzymes of nitrogen assimilation in maize roots." Planta vol. 148,5 (1980): 477-84. doi: https://doi.org/10.1007/BF00552663
Oaks A, Stulen I, Jones K, Winspear MJ, Misra S, Boesel IL. Enzymes of nitrogen assimilation in maize roots. Planta. 1980 Oct;148(5):477-84. doi: 10.1007/BF00552663. PMID: 24310191.
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Overproduction of the membrane-bound [NiFe]-hydrogenase in Thermococcus kodakarensis and its effect on hydrogen production.

Frontiers in microbiology

Kanai T, Simons JR, Tsukamoto R, Nakajima A, Omori Y, Matsuoka R, Beppu H, Imanaka T, Atomi H.
PMID: 26379632
Front Microbiol. 2015 Aug 26;6:847. doi: 10.3389/fmicb.2015.00847. eCollection 2015.

The hyperthermophilic archaeon Thermococcus kodakarensis can utilize sugars or pyruvate for growth. In the absence of elemental sulfur, the electrons via oxidation of these substrates are accepted by protons, generating molecular hydrogen (H2). The hydrogenase responsible for this reaction...

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Kanai T, Simons JR, Tsukamoto R, et al. Overproduction of the membrane-bound [NiFe]-hydrogenase in Thermococcus kodakarensis and its effect on hydrogen production. Front Microbiol. 2015;6:847doi: 10.3389/fmicb.2015.00847.
Kanai, T., Simons, J. R., Tsukamoto, R., Nakajima, A., Omori, Y., Matsuoka, R., Beppu, H., Imanaka, T., & Atomi, H. (2015). Overproduction of the membrane-bound [NiFe]-hydrogenase in Thermococcus kodakarensis and its effect on hydrogen production. Frontiers in microbiology, 6847. https://doi.org/10.3389/fmicb.2015.00847
Kanai, Tamotsu, et al. "Overproduction of the membrane-bound [NiFe]-hydrogenase in Thermococcus kodakarensis and its effect on hydrogen production." Frontiers in microbiology vol. 6 (2015): 847. doi: https://doi.org/10.3389/fmicb.2015.00847
Kanai T, Simons JR, Tsukamoto R, Nakajima A, Omori Y, Matsuoka R, Beppu H, Imanaka T, Atomi H. Overproduction of the membrane-bound [NiFe]-hydrogenase in Thermococcus kodakarensis and its effect on hydrogen production. Front Microbiol. 2015 Aug 26;6:847. doi: 10.3389/fmicb.2015.00847. eCollection 2015. PMID: 26379632; PMCID: PMC4549637.
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Proteomic profiling of HBV infected liver biopsies with different fibrotic stages.

Proteome science

Katrinli S, Ozdil K, Sahin A, Ozturk O, Kir G, Baykal AT, Akgun E, Sarac OS, Sokmen M, Doğanay HL, Dinler Doğanay G.
PMID: 28439208
Proteome Sci. 2017 Apr 20;15:7. doi: 10.1186/s12953-017-0114-4. eCollection 2016.

BACKGROUND: Hepatitis B virus (HBV) is a global health problem, and infected patients if left untreated may develop cirrhosis and eventually hepatocellular carcinoma. This study aims to enlighten pathways associated with HBV related liver fibrosis for delineation of potential...

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Katrinli S, Ozdil K, Sahin A, et al. Proteomic profiling of HBV infected liver biopsies with different fibrotic stages. Proteome Sci. 2017;15:7doi: 10.1186/s12953-017-0114-4.
Katrinli, S., Ozdil, K., Sahin, A., Ozturk, O., Kir, G., Baykal, A. T., Akgun, E., Sarac, O. S., Sokmen, M., Doğanay, H. L., & Dinler Doğanay, G. (2016). Proteomic profiling of HBV infected liver biopsies with different fibrotic stages. Proteome science, 157. https://doi.org/10.1186/s12953-017-0114-4
Katrinli, Seyma, et al. "Proteomic profiling of HBV infected liver biopsies with different fibrotic stages." Proteome science vol. 15 (2016): 7. doi: https://doi.org/10.1186/s12953-017-0114-4
Katrinli S, Ozdil K, Sahin A, Ozturk O, Kir G, Baykal AT, Akgun E, Sarac OS, Sokmen M, Doğanay HL, Dinler Doğanay G. Proteomic profiling of HBV infected liver biopsies with different fibrotic stages. Proteome Sci. 2017 Apr 20;15:7. doi: 10.1186/s12953-017-0114-4. eCollection 2016. PMID: 28439208; PMCID: PMC5399407.
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Glutamate dehydrogenase from Pisum sativum L. : Localization of the multiple forms and of glutamate formation in isolated mitochondria.

Planta

Nauen W, Hartmann T.
PMID: 24311259
Planta. 1980 Feb;148(1):7-16. doi: 10.1007/BF00385435.

A 2-8-fold increase in the activity of glutamate dehydrogenase (GDH), accompanied by an alteration of the GDH isoenzyme pattern, was observed in detached pea shoots floated on tap water (preincubated shoots). Sugars supressed the process, whereas NH + (4)...

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Nauen W, Hartmann T. Glutamate dehydrogenase from Pisum sativum L. : Localization of the multiple forms and of glutamate formation in isolated mitochondria. Planta. 1980;148(1):7-16doi: 10.1007/BF00385435.
Nauen, W., & Hartmann, T. (1980). Glutamate dehydrogenase from Pisum sativum L. : Localization of the multiple forms and of glutamate formation in isolated mitochondria. Planta, 148(1), 7-16. https://doi.org/10.1007/BF00385435
Nauen, W, and Hartmann, T. "Glutamate dehydrogenase from Pisum sativum L. : Localization of the multiple forms and of glutamate formation in isolated mitochondria." Planta vol. 148,1 (1980): 7-16. doi: https://doi.org/10.1007/BF00385435
Nauen W, Hartmann T. Glutamate dehydrogenase from Pisum sativum L. : Localization of the multiple forms and of glutamate formation in isolated mitochondria. Planta. 1980 Feb;148(1):7-16. doi: 10.1007/BF00385435. PMID: 24311259.
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Carbon and nitrogen metabolism in a barley (Hordeum vulgare L.) mutant with impaired chloroplast dicarboxylate transport.

Planta

Wallsgrove RM, Kendall AC, Hall NP, Turner JC, Lea PJ.
PMID: 24232140
Planta. 1986 Sep;168(3):324-9. doi: 10.1007/BF00392356.

A mutant line, RPr79/2, of barley (Hordeum vulgare L. cv. Maris Mink) has been isolated that has an apparent defect in photorespiratory nitrogen metabolism. The metabolism of (14)C-labelled glutamine, glutamate and 2-oxoglutarate indicates that the mutant has a greatly...

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Wallsgrove RM, Kendall AC, Hall NP, et al. Carbon and nitrogen metabolism in a barley (Hordeum vulgare L.) mutant with impaired chloroplast dicarboxylate transport. Planta. 1986;168(3):324-9doi: 10.1007/BF00392356.
Wallsgrove, R. M., Kendall, A. C., Hall, N. P., Turner, J. C., & Lea, P. J. (1986). Carbon and nitrogen metabolism in a barley (Hordeum vulgare L.) mutant with impaired chloroplast dicarboxylate transport. Planta, 168(3), 324-9. https://doi.org/10.1007/BF00392356
Wallsgrove, R M, et al. "Carbon and nitrogen metabolism in a barley (Hordeum vulgare L.) mutant with impaired chloroplast dicarboxylate transport." Planta vol. 168,3 (1986): 324-9. doi: https://doi.org/10.1007/BF00392356
Wallsgrove RM, Kendall AC, Hall NP, Turner JC, Lea PJ. Carbon and nitrogen metabolism in a barley (Hordeum vulgare L.) mutant with impaired chloroplast dicarboxylate transport. Planta. 1986 Sep;168(3):324-9. doi: 10.1007/BF00392356. PMID: 24232140.
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Studies on ammonium-assimilating enzymes of Platymonas striata Butcher (Prasinophyceae).

Planta

Edge PA, Ricketts TR.
PMID: 24414005
Planta. 1978 Jan;138(2):123-5. doi: 10.1007/BF00391167.

Platymonas striata Butcher displays significant levels of glutamate synthase (GS) (EC 2.6.1.53) and glutamine synthetase (GOGAT) (EC 6.3.1.2.), but very low levels of glutamate dehydrogenase (GDH) (EC 1.4.1.4). This suggests that the GS/GOGAT pathway is important for nitrogen assimilation....

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Edge PA, Ricketts TR. Studies on ammonium-assimilating enzymes of Platymonas striata Butcher (Prasinophyceae). Planta. 1978;138(2):123-5doi: 10.1007/BF00391167.
Edge, P. A., & Ricketts, T. R. (1978). Studies on ammonium-assimilating enzymes of Platymonas striata Butcher (Prasinophyceae). Planta, 138(2), 123-5. https://doi.org/10.1007/BF00391167
Edge, P A, and Ricketts, T R. "Studies on ammonium-assimilating enzymes of Platymonas striata Butcher (Prasinophyceae)." Planta vol. 138,2 (1978): 123-5. doi: https://doi.org/10.1007/BF00391167
Edge PA, Ricketts TR. Studies on ammonium-assimilating enzymes of Platymonas striata Butcher (Prasinophyceae). Planta. 1978 Jan;138(2):123-5. doi: 10.1007/BF00391167. PMID: 24414005.
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On the use of glutamate dehydrogenase as a mitochondrial marker enzyme for the determination of the intracellular distribution of rat liver pyruvate carboxylase.

FEBS letters

Walter P, Anabitarte M.
PMID: 11945602
FEBS Lett. 1971 Jan 30;12(5):289-292. doi: 10.1016/0014-5793(71)80201-6.

No abstract available.

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Walter P, Anabitarte M. On the use of glutamate dehydrogenase as a mitochondrial marker enzyme for the determination of the intracellular distribution of rat liver pyruvate carboxylase. FEBS Lett. 1971;12(5):289-292doi: 10.1016/0014-5793(71)80201-6.
Walter, P., & Anabitarte, M. (1971). On the use of glutamate dehydrogenase as a mitochondrial marker enzyme for the determination of the intracellular distribution of rat liver pyruvate carboxylase. FEBS letters, 12(5), 289-292. https://doi.org/10.1016/0014-5793(71)80201-6
Walter, P, and Anabitarte, M. "On the use of glutamate dehydrogenase as a mitochondrial marker enzyme for the determination of the intracellular distribution of rat liver pyruvate carboxylase." FEBS letters vol. 12,5 (1971): 289-292. doi: https://doi.org/10.1016/0014-5793(71)80201-6
Walter P, Anabitarte M. On the use of glutamate dehydrogenase as a mitochondrial marker enzyme for the determination of the intracellular distribution of rat liver pyruvate carboxylase. FEBS Lett. 1971 Jan 30;12(5):289-292. doi: 10.1016/0014-5793(71)80201-6. PMID: 11945602.
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Circular dichroism studies on the complex between beef liver glutamate dehydrogenase and NADH.

FEBS letters

Koberstein R, Sund H.
PMID: 11946198
FEBS Lett. 1971 Dec 01;19(2):149-151. doi: 10.1016/0014-5793(71)80500-8.

No abstract available.

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Koberstein R, Sund H. Circular dichroism studies on the complex between beef liver glutamate dehydrogenase and NADH. FEBS Lett. 1971;19(2):149-151doi: 10.1016/0014-5793(71)80500-8.
Koberstein, R., & Sund, H. (1971). Circular dichroism studies on the complex between beef liver glutamate dehydrogenase and NADH. FEBS letters, 19(2), 149-151. https://doi.org/10.1016/0014-5793(71)80500-8
Koberstein, R, and Sund, H. "Circular dichroism studies on the complex between beef liver glutamate dehydrogenase and NADH." FEBS letters vol. 19,2 (1971): 149-151. doi: https://doi.org/10.1016/0014-5793(71)80500-8
Koberstein R, Sund H. Circular dichroism studies on the complex between beef liver glutamate dehydrogenase and NADH. FEBS Lett. 1971 Dec 01;19(2):149-151. doi: 10.1016/0014-5793(71)80500-8. PMID: 11946198.
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Salinity induced behavioural changes in malate dehydrogenase and glutamate dehydrogenase activities in rice seedlings of differing salt tolerance.

Plant science : an international journal of experimental plant biology

Kumar RG, Shah K, Dubey RS.
PMID: 10908802
Plant Sci. 2000 Jul 14;156(1):23-34. doi: 10.1016/s0168-9452(00)00224-7.

The activities of malate dehydrogenase in whole tissue extract (NAD(+)-MDH) as well as in mitochondrial (NAD(+)-MDH) and chloroplastic (NADP(+)-MDH) preparations of aminating (NADH-GDH) and deaminating(NAD(+)-GDH) glutamate dehydrogenases were studied in two sets of rice cultivars differing in salt tolerance...

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Kumar RG, Shah K, Dubey RS. Salinity induced behavioural changes in malate dehydrogenase and glutamate dehydrogenase activities in rice seedlings of differing salt tolerance. Plant Sci. 2000;156(1):23-34doi: 10.1016/s0168-9452(00)00224-7.
Kumar, R. G., Shah, K., & Dubey, R. S. (2000). Salinity induced behavioural changes in malate dehydrogenase and glutamate dehydrogenase activities in rice seedlings of differing salt tolerance. Plant science : an international journal of experimental plant biology, 156(1), 23-34. https://doi.org/10.1016/s0168-9452(00)00224-7
Kumar, et al. "Salinity induced behavioural changes in malate dehydrogenase and glutamate dehydrogenase activities in rice seedlings of differing salt tolerance." Plant science : an international journal of experimental plant biology vol. 156,1 (2000): 23-34. doi: https://doi.org/10.1016/s0168-9452(00)00224-7
Kumar RG, Shah K, Dubey RS. Salinity induced behavioural changes in malate dehydrogenase and glutamate dehydrogenase activities in rice seedlings of differing salt tolerance. Plant Sci. 2000 Jul 14;156(1):23-34. doi: 10.1016/s0168-9452(00)00224-7. PMID: 10908802.
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Nitrogen-assimilating enzymes in land plants and algae: phylogenic and physiological perspectives.

Physiologia plantarum

Inokuchi R, Kuma KI, Miyata T, Okada M.
PMID: 12207656
Physiol Plant. 2002 Sep;116(1):1-11. doi: 10.1034/j.1399-3054.2002.1160101.x.

An important biochemical feature of autotrophs, land plants and algae, is their incorporation of inorganic nitrogen, nitrate and ammonium, into the carbon skeleton. Nitrate and ammonium are converted into glutamine and glutamate to produce organic nitrogen compounds, for example...

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Inokuchi R, Kuma KI, Miyata T, et al. Nitrogen-assimilating enzymes in land plants and algae: phylogenic and physiological perspectives. Physiol Plant. 2002;116(1):1-11doi: 10.1034/j.1399-3054.2002.1160101.x.
Inokuchi, R., Kuma, K. I., Miyata, T., & Okada, M. (2002). Nitrogen-assimilating enzymes in land plants and algae: phylogenic and physiological perspectives. Physiologia plantarum, 116(1), 1-11. https://doi.org/10.1034/j.1399-3054.2002.1160101.x
Inokuchi, Ritsuko, et al. "Nitrogen-assimilating enzymes in land plants and algae: phylogenic and physiological perspectives." Physiologia plantarum vol. 116,1 (2002): 1-11. doi: https://doi.org/10.1034/j.1399-3054.2002.1160101.x
Inokuchi R, Kuma KI, Miyata T, Okada M. Nitrogen-assimilating enzymes in land plants and algae: phylogenic and physiological perspectives. Physiol Plant. 2002 Sep;116(1):1-11. doi: 10.1034/j.1399-3054.2002.1160101.x. PMID: 12207656.
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Showing 1 to 12 of 540 entries