Advanced Search
Display options
Filter resources
Text Availability
Article type
Publication date
Species
Language
Sex
Age
Showing 1 to 12 of 121 entries
Sorted by: Best Match Show Resources per page
Fluxomics of the eastern oyster for environmental stress studies.

Metabolites

Tikunov AP, Stoskopf MK, Macdonald JM.
PMID: 24958387
Metabolites. 2014 Jan 07;4(1):53-70. doi: 10.3390/metabo4010053.

The metabolism of 2-13C/15N-glycine and U-13C-glucose was determined in four tissue blocks (adductor muscle, stomach and digestive gland, mantle, and gills) of the Eastern oyster (Crassostrea virginica) using proton (1H) and carbon-13 (13C) nuclear magnetic resonance (NMR) spectroscopy. The...

Cite
Tikunov AP, Stoskopf MK, Macdonald JM. Fluxomics of the eastern oyster for environmental stress studies. Metabolites. 2014;4(1):53-70doi: 10.3390/metabo4010053.
Tikunov, A. P., Stoskopf, M. K., & Macdonald, J. M. (2014). Fluxomics of the eastern oyster for environmental stress studies. Metabolites, 4(1), 53-70. https://doi.org/10.3390/metabo4010053
Tikunov, Andrey P, et al. "Fluxomics of the eastern oyster for environmental stress studies." Metabolites vol. 4,1 (2014): 53-70. doi: https://doi.org/10.3390/metabo4010053
Tikunov AP, Stoskopf MK, Macdonald JM. Fluxomics of the eastern oyster for environmental stress studies. Metabolites. 2014 Jan 07;4(1):53-70. doi: 10.3390/metabo4010053. PMID: 24958387; PMCID: PMC4018674.
Copy Download .nbib Format: NLM
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.

Cite
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.
Copy Download .nbib Format: NLM
Distribution of pyruvate carboxylase and phosphoenol-pyruvate carboxikinase in human liver.

FEBS letters

Wieland O, Evertz-Prüsse E, Stukowski B.
PMID: 11946259
FEBS Lett. 1968 Nov;2(1):26-28. doi: 10.1016/0014-5793(68)80091-2.

No abstract available.

Cite
Wieland O, Evertz-Prüsse E, Stukowski B. Distribution of pyruvate carboxylase and phosphoenol-pyruvate carboxikinase in human liver. FEBS Lett. 1968;2(1):26-28doi: 10.1016/0014-5793(68)80091-2.
Wieland, O., Evertz-Prüsse, E., & Stukowski, B. (1968). Distribution of pyruvate carboxylase and phosphoenol-pyruvate carboxikinase in human liver. FEBS letters, 2(1), 26-28. https://doi.org/10.1016/0014-5793(68)80091-2
Wieland, O, et al. "Distribution of pyruvate carboxylase and phosphoenol-pyruvate carboxikinase in human liver." FEBS letters vol. 2,1 (1968): 26-28. doi: https://doi.org/10.1016/0014-5793(68)80091-2
Wieland O, Evertz-Prüsse E, Stukowski B. Distribution of pyruvate carboxylase and phosphoenol-pyruvate carboxikinase in human liver. FEBS Lett. 1968 Nov;2(1):26-28. doi: 10.1016/0014-5793(68)80091-2. PMID: 11946259.
Copy Download .nbib Format: NLM
Mutants of Aspergillus nidulans lacking pyruvate carboxylase.

FEBS letters

Skinner VM, Armitt S.
PMID: 11946370
FEBS Lett. 1972 Jan 15;20(1):16-18. doi: 10.1016/0014-5793(72)80005-x.

No abstract available.

Cite
Skinner VM, Armitt S. Mutants of Aspergillus nidulans lacking pyruvate carboxylase. FEBS Lett. 1972;20(1):16-18doi: 10.1016/0014-5793(72)80005-x.
Skinner, V. M., & Armitt, S. (1972). Mutants of Aspergillus nidulans lacking pyruvate carboxylase. FEBS letters, 20(1), 16-18. https://doi.org/10.1016/0014-5793(72)80005-x
Skinner, V M., and Armitt, S. "Mutants of Aspergillus nidulans lacking pyruvate carboxylase." FEBS letters vol. 20,1 (1972): 16-18. doi: https://doi.org/10.1016/0014-5793(72)80005-x
Skinner VM, Armitt S. Mutants of Aspergillus nidulans lacking pyruvate carboxylase. FEBS Lett. 1972 Jan 15;20(1):16-18. doi: 10.1016/0014-5793(72)80005-x. PMID: 11946370.
Copy Download .nbib Format: NLM
Differential Accumulation of Biotin Enzymes during Carrot Somatic Embryogenesis.

Plant physiology

Wurtele ES, Nikolau BJ.
PMID: 16669096
Plant Physiol. 1992 Aug;99(4):1699-703. doi: 10.1104/pp.99.4.1699.

The activities of four biotin enzymes, acetyl-coenzyme A (CoA) carboxylase, 3-methylcrotonyl-CoA carboxylase, pyruvate carboxylase, and propionyl-CoA carboxylase, and the accumulation of six biotin-containing polypeptides were determined during development of somatic embryos of carrot (Daucus carota). Acetyl-CoA carboxylase activity increased...

Cite
Wurtele ES, Nikolau BJ. Differential Accumulation of Biotin Enzymes during Carrot Somatic Embryogenesis. Plant Physiol. 1992;99(4):1699-703doi: 10.1104/pp.99.4.1699.
Wurtele, E. S., & Nikolau, B. J. (1992). Differential Accumulation of Biotin Enzymes during Carrot Somatic Embryogenesis. Plant physiology, 99(4), 1699-703. https://doi.org/10.1104/pp.99.4.1699
Wurtele, E S, and Nikolau, B J. "Differential Accumulation of Biotin Enzymes during Carrot Somatic Embryogenesis." Plant physiology vol. 99,4 (1992): 1699-703. doi: https://doi.org/10.1104/pp.99.4.1699
Wurtele ES, Nikolau BJ. Differential Accumulation of Biotin Enzymes during Carrot Somatic Embryogenesis. Plant Physiol. 1992 Aug;99(4):1699-703. doi: 10.1104/pp.99.4.1699. PMID: 16669096; PMCID: PMC1080686.
Copy Download .nbib Format: NLM
Influence of Light Intensity on Reductive Pentose Phosphate Cycle Activity during Photoheterotrophic Growth of Rhodospirillum rubrum.

Plant physiology

Porter J, Merrett MJ.
PMID: 16658151
Plant Physiol. 1972 Aug;50(2):252-5. doi: 10.1104/pp.50.2.252.

Light intensity during growth affects the proportion of carbon dioxide fixed by the reductive pentose phosphate cycle relative to that incorporated via C(4) acids in acetate phototrophs of Rhodospirillum rubrum. With cells grown at high light intensity (9000 lux)...

Cite
Porter J, Merrett MJ. Influence of Light Intensity on Reductive Pentose Phosphate Cycle Activity during Photoheterotrophic Growth of Rhodospirillum rubrum. Plant Physiol. 1972;50(2):252-5doi: 10.1104/pp.50.2.252.
Porter, J., & Merrett, M. J. (1972). Influence of Light Intensity on Reductive Pentose Phosphate Cycle Activity during Photoheterotrophic Growth of Rhodospirillum rubrum. Plant physiology, 50(2), 252-5. https://doi.org/10.1104/pp.50.2.252
Porter, J, and Merrett, M J. "Influence of Light Intensity on Reductive Pentose Phosphate Cycle Activity during Photoheterotrophic Growth of Rhodospirillum rubrum." Plant physiology vol. 50,2 (1972): 252-5. doi: https://doi.org/10.1104/pp.50.2.252
Porter J, Merrett MJ. Influence of Light Intensity on Reductive Pentose Phosphate Cycle Activity during Photoheterotrophic Growth of Rhodospirillum rubrum. Plant Physiol. 1972 Aug;50(2):252-5. doi: 10.1104/pp.50.2.252. PMID: 16658151; PMCID: PMC366119.
Copy Download .nbib Format: NLM
Biochemical aspects of bovine ketosis.

The Biochemical journal

Baird GD, Hibbitt KG, Hunter GD.
PMID: 16742590
Biochem J. 1968 May;107(5):683-9. doi: 10.1042/bj1070683.

1. The concentrations of acetoacetate, beta-hydroxybutyrate and metabolites related to gluconeogenesis were determined in biopsy samples of the livers of ketotic, normal lactating and normal non-lactating cows. Key enzymes of gluconeogenesis in the liver were also assayed. 2. Significant...

Cite
Baird GD, Hibbitt KG, Hunter GD. Biochemical aspects of bovine ketosis. Biochem J. 1968;107(5):683-9doi: 10.1042/bj1070683.
Baird, G. D., Hibbitt, K. G., & Hunter, G. D. (1968). Biochemical aspects of bovine ketosis. The Biochemical journal, 107(5), 683-9. https://doi.org/10.1042/bj1070683
Baird, G D, et al. "Biochemical aspects of bovine ketosis." The Biochemical journal vol. 107,5 (1968): 683-9. doi: https://doi.org/10.1042/bj1070683
Baird GD, Hibbitt KG, Hunter GD. Biochemical aspects of bovine ketosis. Biochem J. 1968 May;107(5):683-9. doi: 10.1042/bj1070683. PMID: 16742590; PMCID: PMC1198721.
Copy Download .nbib Format: NLM
Study on roles of anaplerotic pathways in glutamate overproduction of Corynebacterium glutamicum by metabolic flux analysis.

Microbial cell factories

Shirai T, Fujimura K, Furusawa C, Nagahisa K, Shioya S, Shimizu H.
PMID: 17587457
Microb Cell Fact. 2007 Jun 23;6:19. doi: 10.1186/1475-2859-6-19.

BACKGROUND: Corynebacterium glutamicum has several anaplerotic pathways (anaplerosis), which are essential for the productions of amino acids, such as lysine and glutamate. It is still not clear how flux changes in anaplerotic pathways happen when glutamate production is induced...

Cite
Shirai T, Fujimura K, Furusawa C, et al. Study on roles of anaplerotic pathways in glutamate overproduction of Corynebacterium glutamicum by metabolic flux analysis. Microb Cell Fact. 2007;6:19doi: 10.1186/1475-2859-6-19.
Shirai, T., Fujimura, K., Furusawa, C., Nagahisa, K., Shioya, S., & Shimizu, H. (2007). Study on roles of anaplerotic pathways in glutamate overproduction of Corynebacterium glutamicum by metabolic flux analysis. Microbial cell factories, 619. https://doi.org/10.1186/1475-2859-6-19
Shirai, Tomokazu, et al. "Study on roles of anaplerotic pathways in glutamate overproduction of Corynebacterium glutamicum by metabolic flux analysis." Microbial cell factories vol. 6 (2007): 19. doi: https://doi.org/10.1186/1475-2859-6-19
Shirai T, Fujimura K, Furusawa C, Nagahisa K, Shioya S, Shimizu H. Study on roles of anaplerotic pathways in glutamate overproduction of Corynebacterium glutamicum by metabolic flux analysis. Microb Cell Fact. 2007 Jun 23;6:19. doi: 10.1186/1475-2859-6-19. PMID: 17587457; PMCID: PMC1919393.
Copy Download .nbib Format: NLM
Analysis of size characterized manganese species from liver extracts using capillary zone electrophoresis coupled to inductively coupled plasma mass spectrometry (CZE-ICP-MS).

Analytica chimica acta

Quintana M, Klouda AD, Gondikas A, Ochsenkühn-Petropoulou M, Michalke B.
PMID: 17723521
Anal Chim Acta. 2006 Jul 28;573:172-80. doi: 10.1016/j.aca.2006.02.045. Epub 2006 Apr 04.

Mn is of toxicological concern because overexposure can lead to progressive, permanent neurodegenerative damage. Monomethyl-Mn-pentadienyl-tricarbonyl (MMT) is used as an anti-knock agent in fuel. Exhausted Mn compounds are absorbed in the lung and transported to the liver. Extended exposure...

Cite
Quintana M, Klouda AD, Gondikas A, et al. Analysis of size characterized manganese species from liver extracts using capillary zone electrophoresis coupled to inductively coupled plasma mass spectrometry (CZE-ICP-MS). Anal Chim Acta. 2006;573:172-80doi: 10.1016/j.aca.2006.02.045.
Quintana, M., Klouda, A. D., Gondikas, A., Ochsenkühn-Petropoulou, M., & Michalke, B. (2006). Analysis of size characterized manganese species from liver extracts using capillary zone electrophoresis coupled to inductively coupled plasma mass spectrometry (CZE-ICP-MS). Analytica chimica acta, 573172-80. https://doi.org/10.1016/j.aca.2006.02.045
Quintana, Mercedes, et al. "Analysis of size characterized manganese species from liver extracts using capillary zone electrophoresis coupled to inductively coupled plasma mass spectrometry (CZE-ICP-MS)." Analytica chimica acta vol. 573 (2006): 172-80. doi: https://doi.org/10.1016/j.aca.2006.02.045
Quintana M, Klouda AD, Gondikas A, Ochsenkühn-Petropoulou M, Michalke B. Analysis of size characterized manganese species from liver extracts using capillary zone electrophoresis coupled to inductively coupled plasma mass spectrometry (CZE-ICP-MS). Anal Chim Acta. 2006 Jul 28;573:172-80. doi: 10.1016/j.aca.2006.02.045. Epub 2006 Apr 04. PMID: 17723521.
Copy Download .nbib Format: NLM
Metabolic responses to pyruvate kinase deletion in lysine producing Corynebacterium glutamicum.

Microbial cell factories

Becker J, Klopprogge C, Wittmann C.
PMID: 18339202
Microb Cell Fact. 2008 Mar 13;7:8. doi: 10.1186/1475-2859-7-8.

BACKGROUND: Pyruvate kinase is an important element in flux control of the intermediate metabolism. It catalyzes the irreversible conversion of phosphoenolpyruvate into pyruvate and is under allosteric control. In Corynebacterium glutamicum, this enzyme was regarded as promising target for...

Cite
Becker J, Klopprogge C, Wittmann C. Metabolic responses to pyruvate kinase deletion in lysine producing Corynebacterium glutamicum. Microb Cell Fact. 2008;7:8doi: 10.1186/1475-2859-7-8.
Becker, J., Klopprogge, C., & Wittmann, C. (2008). Metabolic responses to pyruvate kinase deletion in lysine producing Corynebacterium glutamicum. Microbial cell factories, 78. https://doi.org/10.1186/1475-2859-7-8
Becker, Judith, et al. "Metabolic responses to pyruvate kinase deletion in lysine producing Corynebacterium glutamicum." Microbial cell factories vol. 7 (2008): 8. doi: https://doi.org/10.1186/1475-2859-7-8
Becker J, Klopprogge C, Wittmann C. Metabolic responses to pyruvate kinase deletion in lysine producing Corynebacterium glutamicum. Microb Cell Fact. 2008 Mar 13;7:8. doi: 10.1186/1475-2859-7-8. PMID: 18339202; PMCID: PMC2322953.
Copy Download .nbib Format: NLM
Inhibitors of Pyruvate Carboxylase.

The open enzyme inhibition journal

Zeczycki TN, Maurice MS, Attwood PV.
PMID: 22180764
Open Enzym Inhib J. 2010;3:8-26. doi: 10.2174/1874940201003010008.

This review aims to discuss the varied types of inhibitors of biotin-dependent carboxylases, with an emphasis on the inhibitors of pyruvate carboxylase. Some of these inhibitors are physiologically relevant, in that they provide ways of regulating the cellular activities...

Cite
Zeczycki TN, Maurice MS, Attwood PV. Inhibitors of Pyruvate Carboxylase. Open Enzym Inhib J. 2010;3:8-26doi: 10.2174/1874940201003010008.
Zeczycki, T. N., Maurice, M. S., & Attwood, P. V. (2010). Inhibitors of Pyruvate Carboxylase. The open enzyme inhibition journal, 38-26. https://doi.org/10.2174/1874940201003010008
Zeczycki, Tonya N, et al. "Inhibitors of Pyruvate Carboxylase." The open enzyme inhibition journal vol. 3 (2010): 8-26. doi: https://doi.org/10.2174/1874940201003010008
Zeczycki TN, Maurice MS, Attwood PV. Inhibitors of Pyruvate Carboxylase. Open Enzym Inhib J. 2010;3:8-26. doi: 10.2174/1874940201003010008. PMID: 22180764; PMCID: PMC3238542.
Copy Download .nbib Format: NLM
Phosphoenol Pyruvate Carboxylase in Parasitic Plants: Further Characterization in Various Species and Localization at the Level of Cells and Tissues in Lathraea clandestina L.

Journal of plant physiology

Renaudin S, Thalouarn P, Rey L, Vidal J, Larher F.
PMID: 23195386
J Plant Physiol. 1984 Nov;116(5):455-65. doi: 10.1016/S0176-1617(84)80137-6. Epub 2012 Jan 20.

Phosphoenolpyruvate carboxylase (PEP carboxylase, EC 4.1.1.31) activity was demonstrated in a range of holo and hemiparasitic phanerogams. Lathraea clandestina was used as a model for a more detailed study. Enzyme activity levels were determined in the various plant parts....

Cite
Renaudin S, Thalouarn P, Rey L, et al. Phosphoenol Pyruvate Carboxylase in Parasitic Plants: Further Characterization in Various Species and Localization at the Level of Cells and Tissues in Lathraea clandestina L. J Plant Physiol. 2012;116(5):455-65doi: 10.1016/S0176-1617(84)80137-6.
Renaudin, S., Thalouarn, P., Rey, L., Vidal, J., & Larher, F. (1984). Phosphoenol Pyruvate Carboxylase in Parasitic Plants: Further Characterization in Various Species and Localization at the Level of Cells and Tissues in Lathraea clandestina L. Journal of plant physiology, 116(5), 455-65. https://doi.org/10.1016/S0176-1617(84)80137-6
Renaudin, S, et al. "Phosphoenol Pyruvate Carboxylase in Parasitic Plants: Further Characterization in Various Species and Localization at the Level of Cells and Tissues in Lathraea clandestina L." Journal of plant physiology vol. 116,5 (1984): 455-65. doi: https://doi.org/10.1016/S0176-1617(84)80137-6
Renaudin S, Thalouarn P, Rey L, Vidal J, Larher F. Phosphoenol Pyruvate Carboxylase in Parasitic Plants: Further Characterization in Various Species and Localization at the Level of Cells and Tissues in Lathraea clandestina L. J Plant Physiol. 1984 Nov;116(5):455-65. doi: 10.1016/S0176-1617(84)80137-6. Epub 2012 Jan 20. PMID: 23195386.
Copy Download .nbib Format: NLM
Showing 1 to 12 of 121 entries