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Showing 1 to 12 of 26 entries
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Understanding, Recognizing, and Treating Rett Syndrome.

Medscape women's health

Budden SS.
PMID: 9746685
Medscape Womens Health. 1997 Mar;2(3):3.

Formerly thought to be a neurodegenerative disease, Rett syndrome (RS) is a neurodevelopmental arrest of the brain that almost exclusively affects females and occurs in a variety of racial and ethnic groups worldwide. RS begins in late infancy and...

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Budden SS. Understanding, Recognizing, and Treating Rett Syndrome. Medscape Womens Health. 1997;2(3):3
Budden, S. S. (1997). Understanding, Recognizing, and Treating Rett Syndrome. Medscape women's health, 2(3), 3.
Budden. "Understanding, Recognizing, and Treating Rett Syndrome." Medscape women's health vol. 2,3 (1997): 3.
Budden SS. Understanding, Recognizing, and Treating Rett Syndrome. Medscape Womens Health. 1997 Mar;2(3):3. PMID: 9746685.
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Partial Purification and Properties of Ornithine Transcarbamoylase from Nostoc muscorum Kützing.

Plant physiology

Boggess SF, Naylor AW.
PMID: 16659361
Plant Physiol. 1975 Nov;56(5):640-4. doi: 10.1104/pp.56.5.640.

Ornithine transcarbamoylase (carbamoyl phosphate:l-ornithine carbamoyltransferase, EC 2.1.3.3) has been partially purified from the blue-green alga Nostoc muscorum Kützing, an organism in which the enzyme seems to be involved in a bicarbonate-fixing pathway leading to citrulline. Pertinent to possible regulation...

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Boggess SF, Naylor AW. Partial Purification and Properties of Ornithine Transcarbamoylase from Nostoc muscorum Kützing. Plant Physiol. 1975;56(5):640-4doi: 10.1104/pp.56.5.640.
Boggess, S. F., & Naylor, A. W. (1975). Partial Purification and Properties of Ornithine Transcarbamoylase from Nostoc muscorum Kützing. Plant physiology, 56(5), 640-4. https://doi.org/10.1104/pp.56.5.640
Boggess, S F, and Naylor, A W. "Partial Purification and Properties of Ornithine Transcarbamoylase from Nostoc muscorum Kützing." Plant physiology vol. 56,5 (1975): 640-4. doi: https://doi.org/10.1104/pp.56.5.640
Boggess SF, Naylor AW. Partial Purification and Properties of Ornithine Transcarbamoylase from Nostoc muscorum Kützing. Plant Physiol. 1975 Nov;56(5):640-4. doi: 10.1104/pp.56.5.640. PMID: 16659361; PMCID: PMC541888.
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Liver engraftment and repopulation by in vitro expanded adult derived human liver stem cells in a child with ornithine carbamoyltransferase deficiency.

JIMD reports

Sokal EM, Stéphenne X, Ottolenghi C, Jazouli N, Clapuyt P, Lacaille F, Najimi M, de Lonlay P, Smets F.
PMID: 24142276
JIMD Rep. 2014;13:65-72. doi: 10.1007/8904_2013_257. Epub 2013 Oct 20.

A 3-year-old girl suffering from ornithine carbamoyltransferase (OTC) deficiency was poorly equilibrated under conventional diet and scavenger treatment. Following unsuccessful cryopreserved hepatocyte transplantation, she received two infusions of Adult Derived Human Liver Stem/Progenitor Cells (ADHLSCs) expanded in vitro under...

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Sokal EM, Stéphenne X, Ottolenghi C, et al. Liver engraftment and repopulation by in vitro expanded adult derived human liver stem cells in a child with ornithine carbamoyltransferase deficiency. JIMD Rep. 2013;13:65-72doi: 10.1007/8904_2013_257.
Sokal, E. M., Stéphenne, X., Ottolenghi, C., Jazouli, N., Clapuyt, P., Lacaille, F., Najimi, M., de Lonlay, P., & Smets, F. (2014). Liver engraftment and repopulation by in vitro expanded adult derived human liver stem cells in a child with ornithine carbamoyltransferase deficiency. JIMD reports, 1365-72. https://doi.org/10.1007/8904_2013_257
Sokal, Etienne M, et al. "Liver engraftment and repopulation by in vitro expanded adult derived human liver stem cells in a child with ornithine carbamoyltransferase deficiency." JIMD reports vol. 13 (2014): 65-72. doi: https://doi.org/10.1007/8904_2013_257
Sokal EM, Stéphenne X, Ottolenghi C, Jazouli N, Clapuyt P, Lacaille F, Najimi M, de Lonlay P, Smets F. Liver engraftment and repopulation by in vitro expanded adult derived human liver stem cells in a child with ornithine carbamoyltransferase deficiency. JIMD Rep. 2014;13:65-72. doi: 10.1007/8904_2013_257. Epub 2013 Oct 20. PMID: 24142276; PMCID: PMC4110332.
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Cell death in a co-culture of hepatocellular carcinoma cells and human umbilical vascular endothelial cells in a medium lacking glucose and arginine.

Oncology letters

Tomizawa M, Shinozaki F, Motoyoshi Y, Sugiyama T, Yamamoto S, Ishige N.
PMID: 28123551
Oncol Lett. 2017 Jan;13(1):258-262. doi: 10.3892/ol.2016.5454. Epub 2016 Nov 30.

Human primary hepatocytes are able to survive in a medium without glucose and arginine that is instead supplemented with galactose and ornithine (hepatocyte selection medium; HSM). This is because the cells produce glucose and arginine by the action of...

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Tomizawa M, Shinozaki F, Motoyoshi Y, et al. Cell death in a co-culture of hepatocellular carcinoma cells and human umbilical vascular endothelial cells in a medium lacking glucose and arginine. Oncol Lett. 2016;13(1):258-262doi: 10.3892/ol.2016.5454.
Tomizawa, M., Shinozaki, F., Motoyoshi, Y., Sugiyama, T., Yamamoto, S., & Ishige, N. (2017). Cell death in a co-culture of hepatocellular carcinoma cells and human umbilical vascular endothelial cells in a medium lacking glucose and arginine. Oncology letters, 13(1), 258-262. https://doi.org/10.3892/ol.2016.5454
Tomizawa, Minoru, et al. "Cell death in a co-culture of hepatocellular carcinoma cells and human umbilical vascular endothelial cells in a medium lacking glucose and arginine." Oncology letters vol. 13,1 (2017): 258-262. doi: https://doi.org/10.3892/ol.2016.5454
Tomizawa M, Shinozaki F, Motoyoshi Y, Sugiyama T, Yamamoto S, Ishige N. Cell death in a co-culture of hepatocellular carcinoma cells and human umbilical vascular endothelial cells in a medium lacking glucose and arginine. Oncol Lett. 2017 Jan;13(1):258-262. doi: 10.3892/ol.2016.5454. Epub 2016 Nov 30. PMID: 28123551; PMCID: PMC5245067.
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Partial characterization of ornithine carbamoyltransferase in three microalgae : anabolic role only.

Plant physiology

Laliberté G, Hellebust JA.
PMID: 16667466
Plant Physiol. 1990 May;93(1):62-6. doi: 10.1104/pp.93.1.62.

Although the existence of isozymes of ornithine carbamoyltransferase (carbamoylphosphate:l-ornithine carbamoyltransferase, EC 2.1.3.3) in higher plants has been reported, and the possibility exists that one or more of these operates catabolically to produce ornithine and carbamoylphosphate from citrulline and inorganic...

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Laliberté G, Hellebust JA. Partial characterization of ornithine carbamoyltransferase in three microalgae : anabolic role only. Plant Physiol. 1990;93(1):62-6doi: 10.1104/pp.93.1.62.
Laliberté, G., & Hellebust, J. A. (1990). Partial characterization of ornithine carbamoyltransferase in three microalgae : anabolic role only. Plant physiology, 93(1), 62-6. https://doi.org/10.1104/pp.93.1.62
Laliberté, G, and Hellebust, J A. "Partial characterization of ornithine carbamoyltransferase in three microalgae : anabolic role only." Plant physiology vol. 93,1 (1990): 62-6. doi: https://doi.org/10.1104/pp.93.1.62
Laliberté G, Hellebust JA. Partial characterization of ornithine carbamoyltransferase in three microalgae : anabolic role only. Plant Physiol. 1990 May;93(1):62-6. doi: 10.1104/pp.93.1.62. PMID: 16667466; PMCID: PMC1062467.
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Activity of enzymes of arginine metabolism in the cotyledons of developing and germinating pea seeds.

Plant physiology

de Ruiter H, Kollöffel C.
PMID: 16662469
Plant Physiol. 1982 Jul;70(1):313-5. doi: 10.1104/pp.70.1.313.

Ornithine carbamoyltransferase, argininosuccinate synthetase, argininosuccinate lyase, and arginase activity were measured in extracts from cotyledons of developing and germinating seeds of Pisum sativum L. The course of activity of these four urea cycle enzymes showed a similar pattern during...

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de Ruiter H, Kollöffel C. Activity of enzymes of arginine metabolism in the cotyledons of developing and germinating pea seeds. Plant Physiol. 1982;70(1):313-5doi: 10.1104/pp.70.1.313.
de Ruiter, H., & Kollöffel, C. (1982). Activity of enzymes of arginine metabolism in the cotyledons of developing and germinating pea seeds. Plant physiology, 70(1), 313-5. https://doi.org/10.1104/pp.70.1.313
de Ruiter, H, and Kollöffel, C. "Activity of enzymes of arginine metabolism in the cotyledons of developing and germinating pea seeds." Plant physiology vol. 70,1 (1982): 313-5. doi: https://doi.org/10.1104/pp.70.1.313
de Ruiter H, Kollöffel C. Activity of enzymes of arginine metabolism in the cotyledons of developing and germinating pea seeds. Plant Physiol. 1982 Jul;70(1):313-5. doi: 10.1104/pp.70.1.313. PMID: 16662469; PMCID: PMC1067133.
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Regulation of citrulline synthesis in human enterocytes: Role of hypoxia and inflammation.

BioFactors (Oxford, England)

Couchet M, Pestour S, Breuillard C, Corne C, Rendu J, Fontaine E, Moinard C.
PMID: 34882863
Biofactors. 2021 Dec 09; doi: 10.1002/biof.1810. Epub 2021 Dec 09.

Intensive care unit patients and chronic airway inflammatory disease are characterized by chronic systemic hypoxia and inflammation inducing a decrease in nitric oxide release due to impaired l-arginine (ARG) homeostasis. As ARG is synthesized from circulating l-citrulline (CIT), an...

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Couchet M, Pestour S, Breuillard C, et al. Regulation of citrulline synthesis in human enterocytes: Role of hypoxia and inflammation. Biofactors. 2021;doi: 10.1002/biof.1810.
Couchet, M., Pestour, S., Breuillard, C., Corne, C., Rendu, J., Fontaine, E., & Moinard, C. (2021). Regulation of citrulline synthesis in human enterocytes: Role of hypoxia and inflammation. BioFactors (Oxford, England), . https://doi.org/10.1002/biof.1810
Couchet, Morgane, et al. "Regulation of citrulline synthesis in human enterocytes: Role of hypoxia and inflammation." BioFactors (Oxford, England) vol. (2021). doi: https://doi.org/10.1002/biof.1810
Couchet M, Pestour S, Breuillard C, Corne C, Rendu J, Fontaine E, Moinard C. Regulation of citrulline synthesis in human enterocytes: Role of hypoxia and inflammation. Biofactors. 2021 Dec 09; doi: 10.1002/biof.1810. Epub 2021 Dec 09. PMID: 34882863.
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Mode of Action of the Toxin from Pseudomonas phaseolicola: I. Toxin Specificity, Chlorosis, and Ornithine Accumulation.

Plant physiology

Patil SS, Tam LQ.
PMID: 16658052
Plant Physiol. 1972 May;49(5):803-7. doi: 10.1104/pp.49.5.803.

The specificity of the Pseudomonas phaseolicola toxin for enzyme inhibition and its relationship to toxin-induced chlorosis in bean leaves (Phaseolus vulgaris L.) was examined. The toxin showed no significant inhibitory activity against glutamine synthetase, glutamine transferase, carbamyl phosphate synthetase,...

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Patil SS, Tam LQ. Mode of Action of the Toxin from Pseudomonas phaseolicola: I. Toxin Specificity, Chlorosis, and Ornithine Accumulation. Plant Physiol. 1972;49(5):803-7doi: 10.1104/pp.49.5.803.
Patil, S. S., & Tam, L. Q. (1972). Mode of Action of the Toxin from Pseudomonas phaseolicola: I. Toxin Specificity, Chlorosis, and Ornithine Accumulation. Plant physiology, 49(5), 803-7. https://doi.org/10.1104/pp.49.5.803
Patil, S S, and Tam, L Q. "Mode of Action of the Toxin from Pseudomonas phaseolicola: I. Toxin Specificity, Chlorosis, and Ornithine Accumulation." Plant physiology vol. 49,5 (1972): 803-7. doi: https://doi.org/10.1104/pp.49.5.803
Patil SS, Tam LQ. Mode of Action of the Toxin from Pseudomonas phaseolicola: I. Toxin Specificity, Chlorosis, and Ornithine Accumulation. Plant Physiol. 1972 May;49(5):803-7. doi: 10.1104/pp.49.5.803. PMID: 16658052; PMCID: PMC366056.
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Mode of Action of the Toxin from Pseudomonas phaseolicola: II. Mechanism of Inhibition of Bean Ornithine Carbamoyltransferase.

Plant physiology

Tam LQ, Patil SS.
PMID: 16658053
Plant Physiol. 1972 May;49(5):808-12. doi: 10.1104/pp.49.5.808.

A chlorosis-inducing toxin of Pseudomonas phaseolicola was examined for inhibition of ornithine carbamoyltransferease prepared from acetone powder of bean (Phaseolus vulgaris L.) plants. The enzyme has a pH optimum at 8.5, involves a ternary complex reaction mechanism, and shows...

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Tam LQ, Patil SS. Mode of Action of the Toxin from Pseudomonas phaseolicola: II. Mechanism of Inhibition of Bean Ornithine Carbamoyltransferase. Plant Physiol. 1972;49(5):808-12doi: 10.1104/pp.49.5.808.
Tam, L. Q., & Patil, S. S. (1972). Mode of Action of the Toxin from Pseudomonas phaseolicola: II. Mechanism of Inhibition of Bean Ornithine Carbamoyltransferase. Plant physiology, 49(5), 808-12. https://doi.org/10.1104/pp.49.5.808
Tam, L Q, and Patil, S S. "Mode of Action of the Toxin from Pseudomonas phaseolicola: II. Mechanism of Inhibition of Bean Ornithine Carbamoyltransferase." Plant physiology vol. 49,5 (1972): 808-12. doi: https://doi.org/10.1104/pp.49.5.808
Tam LQ, Patil SS. Mode of Action of the Toxin from Pseudomonas phaseolicola: II. Mechanism of Inhibition of Bean Ornithine Carbamoyltransferase. Plant Physiol. 1972 May;49(5):808-12. doi: 10.1104/pp.49.5.808. PMID: 16658053; PMCID: PMC366057.
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The occurrence and nature of ornithine carbamoyltransferase in senescing apple leaf tissue.

Plant physiology

Spencer PW, Titus JS.
PMID: 16658894
Plant Physiol. 1974 Sep;54(3):382-5. doi: 10.1104/pp.54.3.382.

Ornithine carbamoyltransferase (EC 2.1.3.3) activity was detected in apple (Pyrus malus L.) leaf tissue from early June to November. Total activity remained relatively constant at 4.1 mumoles citrulline produced per hour per 10 cm(2) until mid-October when it sharply...

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Spencer PW, Titus JS. The occurrence and nature of ornithine carbamoyltransferase in senescing apple leaf tissue. Plant Physiol. 1974;54(3):382-5doi: 10.1104/pp.54.3.382.
Spencer, P. W., & Titus, J. S. (1974). The occurrence and nature of ornithine carbamoyltransferase in senescing apple leaf tissue. Plant physiology, 54(3), 382-5. https://doi.org/10.1104/pp.54.3.382
Spencer, P W, and Titus, J S. "The occurrence and nature of ornithine carbamoyltransferase in senescing apple leaf tissue." Plant physiology vol. 54,3 (1974): 382-5. doi: https://doi.org/10.1104/pp.54.3.382
Spencer PW, Titus JS. The occurrence and nature of ornithine carbamoyltransferase in senescing apple leaf tissue. Plant Physiol. 1974 Sep;54(3):382-5. doi: 10.1104/pp.54.3.382. PMID: 16658894; PMCID: PMC367417.
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Site of Synthesis of the Enzymes of the Pyrimidine Biosynthetic Pathway in Oat (Avena sativa L.) Leaves.

Plant physiology

Doremus HD, Jagendorf AT.
PMID: 16665303
Plant Physiol. 1987 Mar;83(3):657-8. doi: 10.1104/pp.83.3.657.

Heat-bleached oat (Avena sativa L. cv Porter) leaves lacking 70S chloroplast ribosomes have been used to demonstrate that four chloroplast-localized enzymes of pyrimidine nucleotide biosynthesis: aspartate carbamoyl-transferase, dihydroorotase, orotidine phosphoribosyl-transferase, and orotidine-5'-phosphate decarboxylase, are synthesized on cytoplasmic ribosomes. Two...

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Doremus HD, Jagendorf AT. Site of Synthesis of the Enzymes of the Pyrimidine Biosynthetic Pathway in Oat (Avena sativa L.) Leaves. Plant Physiol. 1987;83(3):657-8doi: 10.1104/pp.83.3.657.
Doremus, H. D., & Jagendorf, A. T. (1987). Site of Synthesis of the Enzymes of the Pyrimidine Biosynthetic Pathway in Oat (Avena sativa L.) Leaves. Plant physiology, 83(3), 657-8. https://doi.org/10.1104/pp.83.3.657
Doremus, H D, and Jagendorf, A T. "Site of Synthesis of the Enzymes of the Pyrimidine Biosynthetic Pathway in Oat (Avena sativa L.) Leaves." Plant physiology vol. 83,3 (1987): 657-8. doi: https://doi.org/10.1104/pp.83.3.657
Doremus HD, Jagendorf AT. Site of Synthesis of the Enzymes of the Pyrimidine Biosynthetic Pathway in Oat (Avena sativa L.) Leaves. Plant Physiol. 1987 Mar;83(3):657-8. doi: 10.1104/pp.83.3.657. PMID: 16665303; PMCID: PMC1056421.
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Preparation of isolated periportal or perivenous hepatocytes from rat liver.

Methods in molecular biology (Clifton, N.J.)

Quistorff B.
PMID: 21374125
Methods Mol Biol. 1990;5:177-87. doi: 10.1385/0-89603-150-0:177.

There are a number of functional, metabolic differences between periportal and perivenous hepatocytes in the mammalian liver resulting from zonal differences in the activity of several enzymes, and possibly from morphological differences as well (1). Examples of key enzymes...

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Quistorff B. Preparation of isolated periportal or perivenous hepatocytes from rat liver. Methods Mol Biol. 1990;5:177-87doi: 10.1385/0-89603-150-0:177.
Quistorff, B. (1990). Preparation of isolated periportal or perivenous hepatocytes from rat liver. Methods in molecular biology (Clifton, N.J.), 5177-87. https://doi.org/10.1385/0-89603-150-0:177
Quistorff, B. "Preparation of isolated periportal or perivenous hepatocytes from rat liver." Methods in molecular biology (Clifton, N.J.) vol. 5 (1990): 177-87. doi: https://doi.org/10.1385/0-89603-150-0:177
Quistorff B. Preparation of isolated periportal or perivenous hepatocytes from rat liver. Methods Mol Biol. 1990;5:177-87. doi: 10.1385/0-89603-150-0:177. PMID: 21374125.
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