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Reexamination of the Intracellular Localization of de Novo Purine Synthesis in Cowpea Nodules.

Plant physiology

Atkins CA, Smith P, Storer PJ.
PMID: 12223595
Plant Physiol. 1997 Jan;113(1):127-135. doi: 10.1104/pp.113.1.127.

Sucrose and Percoll density gradient centrifugation were used to separate organelles from the central zone tissue of cowpea (Vigna unguiculata L. Walp. cv Vita 3: Bradyrhizobium strain CB 756) nodules. Enzyme activity analysis has shown that both plastids and...

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Atkins CA, Smith P, Storer PJ. Reexamination of the Intracellular Localization of de Novo Purine Synthesis in Cowpea Nodules. Plant Physiol. 1997;113(1):127-135doi: 10.1104/pp.113.1.127.
Atkins, C. A., Smith, P., & Storer, P. J. (1997). Reexamination of the Intracellular Localization of de Novo Purine Synthesis in Cowpea Nodules. Plant physiology, 113(1), 127-135. https://doi.org/10.1104/pp.113.1.127
Atkins, C. A., et al. "Reexamination of the Intracellular Localization of de Novo Purine Synthesis in Cowpea Nodules." Plant physiology vol. 113,1 (1997): 127-135. doi: https://doi.org/10.1104/pp.113.1.127
Atkins CA, Smith P, Storer PJ. Reexamination of the Intracellular Localization of de Novo Purine Synthesis in Cowpea Nodules. Plant Physiol. 1997 Jan;113(1):127-135. doi: 10.1104/pp.113.1.127. PMID: 12223595; PMCID: PMC158123.
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Untargeted metabolomics confirms and extends the understanding of the impact of aminoimidazole carboxamide ribotide (AICAR) in the metabolic network of .

Microbial cell (Graz, Austria)

Bazurto JV, Dearth SP, Tague ED, Campagna SR, Downs DM.
PMID: 29417056
Microb Cell. 2017 Nov 22;5(2):74-87. doi: 10.15698/mic2018.02.613.

In

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Bazurto JV, Dearth SP, Tague ED, et al. Untargeted metabolomics confirms and extends the understanding of the impact of aminoimidazole carboxamide ribotide (AICAR) in the metabolic network of . Microb Cell. 2017;5(2):74-87doi: 10.15698/mic2018.02.613.
Bazurto, J. V., Dearth, S. P., Tague, E. D., Campagna, S. R., & Downs, D. M. (2017). Untargeted metabolomics confirms and extends the understanding of the impact of aminoimidazole carboxamide ribotide (AICAR) in the metabolic network of . Microbial cell (Graz, Austria), 5(2), 74-87. https://doi.org/10.15698/mic2018.02.613
Bazurto, Jannell V, et al. "Untargeted metabolomics confirms and extends the understanding of the impact of aminoimidazole carboxamide ribotide (AICAR) in the metabolic network of ." Microbial cell (Graz, Austria) vol. 5,2 (2017): 74-87. doi: https://doi.org/10.15698/mic2018.02.613
Bazurto JV, Dearth SP, Tague ED, Campagna SR, Downs DM. Untargeted metabolomics confirms and extends the understanding of the impact of aminoimidazole carboxamide ribotide (AICAR) in the metabolic network of . Microb Cell. 2017 Nov 22;5(2):74-87. doi: 10.15698/mic2018.02.613. PMID: 29417056; PMCID: PMC5798407.
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Effects of activation of AMPK on human breast cancer cell lines with different genetic backgrounds.

Oncology letters

El-Masry OS, Brown BL, Dobson PR.
PMID: 22740885
Oncol Lett. 2012 Jan;3(1):224-228. doi: 10.3892/ol.2011.458. Epub 2011 Oct 21.

Breast cancer remains a therapeutic challenge, and this has intensified the search for new drug targets. The AMP-activated protein kinase (AMPK) signalling pathway is emerging as having potential for intervention. We assessed the possible different effects of AMPK action...

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El-Masry OS, Brown BL, Dobson PR. Effects of activation of AMPK on human breast cancer cell lines with different genetic backgrounds. Oncol Lett. 2011;3(1):224-228doi: 10.3892/ol.2011.458.
El-Masry, O. S., Brown, B. L., & Dobson, P. R. (2012). Effects of activation of AMPK on human breast cancer cell lines with different genetic backgrounds. Oncology letters, 3(1), 224-228. https://doi.org/10.3892/ol.2011.458
El-Masry, Omar S, et al. "Effects of activation of AMPK on human breast cancer cell lines with different genetic backgrounds." Oncology letters vol. 3,1 (2012): 224-228. doi: https://doi.org/10.3892/ol.2011.458
El-Masry OS, Brown BL, Dobson PR. Effects of activation of AMPK on human breast cancer cell lines with different genetic backgrounds. Oncol Lett. 2012 Jan;3(1):224-228. doi: 10.3892/ol.2011.458. Epub 2011 Oct 21. PMID: 22740885; PMCID: PMC3362498.
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De Novo Purine Synthesis in Nitrogen-Fixing Nodules of Cowpea (Vigna unguiculata [L.] Walp.) and Soybean (Glycine max [L.] Merr.).

Plant physiology

Atkins CA, Ritchie A, Rowe PB, McCairns E, Sauer D.
PMID: 16662479
Plant Physiol. 1982 Jul;70(1):55-60. doi: 10.1104/pp.70.1.55.

Partially purified, cell-free extracts from nodules of cowpea (Vigna unguiculata L. Walp. cv. Caloona) and soybean (Glycine max L. Merr. cv. Bragg) showed high rates of de novo purine nucleotide and purine base synthesis. Activity increased with rates of...

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Atkins CA, Ritchie A, Rowe PB, et al. De Novo Purine Synthesis in Nitrogen-Fixing Nodules of Cowpea (Vigna unguiculata [L.] Walp.) and Soybean (Glycine max [L.] Merr.). Plant Physiol. 1982;70(1):55-60doi: 10.1104/pp.70.1.55.
Atkins, C. A., Ritchie, A., Rowe, P. B., McCairns, E., & Sauer, D. (1982). De Novo Purine Synthesis in Nitrogen-Fixing Nodules of Cowpea (Vigna unguiculata [L.] Walp.) and Soybean (Glycine max [L.] Merr.). Plant physiology, 70(1), 55-60. https://doi.org/10.1104/pp.70.1.55
Atkins, C A, et al. "De Novo Purine Synthesis in Nitrogen-Fixing Nodules of Cowpea (Vigna unguiculata [L.] Walp.) and Soybean (Glycine max [L.] Merr.)." Plant physiology vol. 70,1 (1982): 55-60. doi: https://doi.org/10.1104/pp.70.1.55
Atkins CA, Ritchie A, Rowe PB, McCairns E, Sauer D. De Novo Purine Synthesis in Nitrogen-Fixing Nodules of Cowpea (Vigna unguiculata [L.] Walp.) and Soybean (Glycine max [L.] Merr.). Plant Physiol. 1982 Jul;70(1):55-60. doi: 10.1104/pp.70.1.55. PMID: 16662479; PMCID: PMC1067085.
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LKB1 and AMPKα1 are required in pancreatic alpha cells for the normal regulation of glucagon secretion and responses to hypoglycemia.

Molecular metabolism

Sun G, da Silva Xavier G, Gorman T, Priest C, Solomou A, Hodson DJ, Foretz M, Viollet B, Herrera PL, Parker H, Reimann F, Gribble FM, Migrenne S, Magnan C, Marley A, Rutter GA.
PMID: 25830091
Mol Metab. 2015 Jan 31;4(4):277-86. doi: 10.1016/j.molmet.2015.01.006. eCollection 2015 Apr.

AIMS/HYPOTHESIS: Glucagon release from pancreatic alpha cells is required for normal glucose homoeostasis and is dysregulated in both Type 1 and Type 2 diabetes. The tumour suppressor LKB1 (STK11) and the downstream kinase AMP-activated protein kinase (AMPK), modulate cellular...

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Sun G, da Silva Xavier G, Gorman T, et al. LKB1 and AMPKα1 are required in pancreatic alpha cells for the normal regulation of glucagon secretion and responses to hypoglycemia. Mol Metab. 2015;4(4):277-86doi: 10.1016/j.molmet.2015.01.006.
Sun, G., da Silva Xavier, G., Gorman, T., Priest, C., Solomou, A., Hodson, D. J., Foretz, M., Viollet, B., Herrera, P. L., Parker, H., Reimann, F., Gribble, F. M., Migrenne, S., Magnan, C., Marley, A., & Rutter, G. A. (2015). LKB1 and AMPKα1 are required in pancreatic alpha cells for the normal regulation of glucagon secretion and responses to hypoglycemia. Molecular metabolism, 4(4), 277-86. https://doi.org/10.1016/j.molmet.2015.01.006
Sun, Gao, et al. "LKB1 and AMPKα1 are required in pancreatic alpha cells for the normal regulation of glucagon secretion and responses to hypoglycemia." Molecular metabolism vol. 4,4 (2015): 277-86. doi: https://doi.org/10.1016/j.molmet.2015.01.006
Sun G, da Silva Xavier G, Gorman T, Priest C, Solomou A, Hodson DJ, Foretz M, Viollet B, Herrera PL, Parker H, Reimann F, Gribble FM, Migrenne S, Magnan C, Marley A, Rutter GA. LKB1 and AMPKα1 are required in pancreatic alpha cells for the normal regulation of glucagon secretion and responses to hypoglycemia. Mol Metab. 2015 Jan 31;4(4):277-86. doi: 10.1016/j.molmet.2015.01.006. eCollection 2015 Apr. PMID: 25830091; PMCID: PMC4354920.
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The effects of chronic AMPK activation on hepatic triglyceride accumulation and glycerol 3-phosphate acyltransferase activity with high fat feeding.

Diabetology & metabolic syndrome

Henriksen BS, Curtis ME, Fillmore N, Cardon BR, Thomson DM, Hancock CR.
PMID: 23725555
Diabetol Metab Syndr. 2013 May 31;5:29. doi: 10.1186/1758-5996-5-29. eCollection 2013.

BACKGROUND: High fat feeding increases hepatic fat accumulation and is associated with hepatic insulin resistance. AMP Activated Protein Kinase (AMPK) is thought to inhibit lipid synthesis by the acute inhibition of glycerol-3-phosphate acyltransferase (GPAT) activity and transcriptional regulation via...

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Henriksen BS, Curtis ME, Fillmore N, et al. The effects of chronic AMPK activation on hepatic triglyceride accumulation and glycerol 3-phosphate acyltransferase activity with high fat feeding. Diabetol Metab Syndr. 2013;5:29doi: 10.1186/1758-5996-5-29.
Henriksen, B. S., Curtis, M. E., Fillmore, N., Cardon, B. R., Thomson, D. M., & Hancock, C. R. (2013). The effects of chronic AMPK activation on hepatic triglyceride accumulation and glycerol 3-phosphate acyltransferase activity with high fat feeding. Diabetology & metabolic syndrome, 529. https://doi.org/10.1186/1758-5996-5-29
Henriksen, Bradley S, et al. "The effects of chronic AMPK activation on hepatic triglyceride accumulation and glycerol 3-phosphate acyltransferase activity with high fat feeding." Diabetology & metabolic syndrome vol. 5 (2013): 29. doi: https://doi.org/10.1186/1758-5996-5-29
Henriksen BS, Curtis ME, Fillmore N, Cardon BR, Thomson DM, Hancock CR. The effects of chronic AMPK activation on hepatic triglyceride accumulation and glycerol 3-phosphate acyltransferase activity with high fat feeding. Diabetol Metab Syndr. 2013 May 31;5:29. doi: 10.1186/1758-5996-5-29. eCollection 2013. PMID: 23725555; PMCID: PMC3679947.
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Showing 1 to 6 of 6 entries