Advanced Search
Display options
Filter resources
Text Availability
Article type
Publication date
Species
Language
Sex
Age
Showing 1 to 12 of 185 entries
Sorted by: Best Match Show Resources per page
Data supporting the co-expression of PDHA1 gene and of its paralogue PDHA2 in somatic cells of a family.

Data in brief

Pinheiro A, Silva MJ, Pavlu-Pereira H, Florindo C, Barroso M, Marques B, Correia H, Oliveira A, Gaspar A, Tavares de Almeida I, Rivera I.
PMID: 27656664
Data Brief. 2016 Aug 20;9:68-77. doi: 10.1016/j.dib.2016.08.029. eCollection 2016 Dec.

This article presents a dataset proving the simultaneous presence of a 5'UTR-truncated PDHA1 mRNA and a full-length PDHA2 mRNA in the somatic cells of a PDC-deficient female patient and all members of her immediate family (parents and brother). We...

Cite
Pinheiro A, Silva MJ, Pavlu-Pereira H, et al. Data supporting the co-expression of PDHA1 gene and of its paralogue PDHA2 in somatic cells of a family. Data Brief. 2016;9:68-77doi: 10.1016/j.dib.2016.08.029.
Pinheiro, A., Silva, M. J., Pavlu-Pereira, H., Florindo, C., Barroso, M., Marques, B., Correia, H., Oliveira, A., Gaspar, A., Tavares de Almeida, I., & Rivera, I. (2016). Data supporting the co-expression of PDHA1 gene and of its paralogue PDHA2 in somatic cells of a family. Data in brief, 968-77. https://doi.org/10.1016/j.dib.2016.08.029
Pinheiro, Ana, et al. "Data supporting the co-expression of PDHA1 gene and of its paralogue PDHA2 in somatic cells of a family." Data in brief vol. 9 (2016): 68-77. doi: https://doi.org/10.1016/j.dib.2016.08.029
Pinheiro A, Silva MJ, Pavlu-Pereira H, Florindo C, Barroso M, Marques B, Correia H, Oliveira A, Gaspar A, Tavares de Almeida I, Rivera I. Data supporting the co-expression of PDHA1 gene and of its paralogue PDHA2 in somatic cells of a family. Data Brief. 2016 Aug 20;9:68-77. doi: 10.1016/j.dib.2016.08.029. eCollection 2016 Dec. PMID: 27656664; PMCID: PMC5021711.
Copy Download .nbib Format: NLM
The role of pyruvate dehydrogenase kinase in diabetes and obesity.

Diabetes & metabolism journal

Lee IK.
PMID: 25003070
Diabetes Metab J. 2014 Jun;38(3):181-6. doi: 10.4093/dmj.2014.38.3.181.

The pyruvate dehydrogenase complex (PDC) is an emerging target for the treatment of metabolic syndrome. To maintain a steady-state concentration of adenosine triphosphate during the feed-fast cycle, cells require efficient utilization of fatty acid and glucose, which is controlled...

Cite
Lee IK. The role of pyruvate dehydrogenase kinase in diabetes and obesity. Diabetes Metab J. 2014;38(3):181-6doi: 10.4093/dmj.2014.38.3.181.
Lee, I. K. (2014). The role of pyruvate dehydrogenase kinase in diabetes and obesity. Diabetes & metabolism journal, 38(3), 181-6. https://doi.org/10.4093/dmj.2014.38.3.181
Lee, In-Kyu. "The role of pyruvate dehydrogenase kinase in diabetes and obesity." Diabetes & metabolism journal vol. 38,3 (2014): 181-6. doi: https://doi.org/10.4093/dmj.2014.38.3.181
Lee IK. The role of pyruvate dehydrogenase kinase in diabetes and obesity. Diabetes Metab J. 2014 Jun;38(3):181-6. doi: 10.4093/dmj.2014.38.3.181. PMID: 25003070; PMCID: PMC4083023.
Copy Download .nbib Format: NLM
Anti-mitochondrial M2 antibody-positive autoimmune hepatitis.

Experimental and therapeutic medicine

Tomizawa M, Shinozaki F, Fugo K, Motoyoshi Y, Sugiyama T, Yamamoto S, Kishimoto T, Ishige N.
PMID: 26622500
Exp Ther Med. 2015 Oct;10(4):1419-1422. doi: 10.3892/etm.2015.2694. Epub 2015 Aug 20.

Anti-mitochondrial M2 antibody (AMA-M2) is specific to primary biliary cirrhosis (PBC), but can also be found in certain patients with autoimmune hepatitis (AIH). Effective methods of differentiating between PBC and AIH are required, as their clinical course and management...

Cite
Tomizawa M, Shinozaki F, Fugo K, et al. Anti-mitochondrial M2 antibody-positive autoimmune hepatitis. Exp Ther Med. 2015;10(4):1419-1422doi: 10.3892/etm.2015.2694.
Tomizawa, M., Shinozaki, F., Fugo, K., Motoyoshi, Y., Sugiyama, T., Yamamoto, S., Kishimoto, T., & Ishige, N. (2015). Anti-mitochondrial M2 antibody-positive autoimmune hepatitis. Experimental and therapeutic medicine, 10(4), 1419-1422. https://doi.org/10.3892/etm.2015.2694
Tomizawa, Minoru, et al. "Anti-mitochondrial M2 antibody-positive autoimmune hepatitis." Experimental and therapeutic medicine vol. 10,4 (2015): 1419-1422. doi: https://doi.org/10.3892/etm.2015.2694
Tomizawa M, Shinozaki F, Fugo K, Motoyoshi Y, Sugiyama T, Yamamoto S, Kishimoto T, Ishige N. Anti-mitochondrial M2 antibody-positive autoimmune hepatitis. Exp Ther Med. 2015 Oct;10(4):1419-1422. doi: 10.3892/etm.2015.2694. Epub 2015 Aug 20. PMID: 26622500; PMCID: PMC4578094.
Copy Download .nbib Format: NLM
Structural alterations induced by ten disease-causing mutations of human dihydrolipoamide dehydrogenase analyzed by hydrogen/deuterium-exchange mass spectrometry: Implications for the structural basis of E3 deficiency.

Biochimica et biophysica acta

Ambrus A, Wang J, Mizsei R, Zambo Z, Torocsik B, Jordan F, Adam-Vizi V.
PMID: 27544700
Biochim Biophys Acta. 2016 Nov;1862(11):2098-2109. doi: 10.1016/j.bbadis.2016.08.013. Epub 2016 Aug 18.

Pathogenic amino acid substitutions of the common E3 component (hE3) of the human alpha-ketoglutarate dehydrogenase and the pyruvate dehydrogenase complexes lead to severe metabolic diseases (E3 deficiency), which usually manifest themselves in cardiological and/or neurological symptoms and often cause...

Cite
Ambrus A, Wang J, Mizsei R, et al. Structural alterations induced by ten disease-causing mutations of human dihydrolipoamide dehydrogenase analyzed by hydrogen/deuterium-exchange mass spectrometry: Implications for the structural basis of E3 deficiency. Biochim Biophys Acta. 2016;1862(11):2098-2109doi: 10.1016/j.bbadis.2016.08.013.
Ambrus, A., Wang, J., Mizsei, R., Zambo, Z., Torocsik, B., Jordan, F., & Adam-Vizi, V. (2016). Structural alterations induced by ten disease-causing mutations of human dihydrolipoamide dehydrogenase analyzed by hydrogen/deuterium-exchange mass spectrometry: Implications for the structural basis of E3 deficiency. Biochimica et biophysica acta, 1862(11), 2098-2109. https://doi.org/10.1016/j.bbadis.2016.08.013
Ambrus, Attila, et al. "Structural alterations induced by ten disease-causing mutations of human dihydrolipoamide dehydrogenase analyzed by hydrogen/deuterium-exchange mass spectrometry: Implications for the structural basis of E3 deficiency." Biochimica et biophysica acta vol. 1862,11 (2016): 2098-2109. doi: https://doi.org/10.1016/j.bbadis.2016.08.013
Ambrus A, Wang J, Mizsei R, Zambo Z, Torocsik B, Jordan F, Adam-Vizi V. Structural alterations induced by ten disease-causing mutations of human dihydrolipoamide dehydrogenase analyzed by hydrogen/deuterium-exchange mass spectrometry: Implications for the structural basis of E3 deficiency. Biochim Biophys Acta. 2016 Nov;1862(11):2098-2109. doi: 10.1016/j.bbadis.2016.08.013. Epub 2016 Aug 18. PMID: 27544700; PMCID: PMC5035230.
Copy Download .nbib Format: NLM
Mechanisms Involved in the Improvement of Lipotoxicity and Impaired Lipid Metabolism by Dietary α-Linolenic Acid Rich Salvia hispanica L (Salba) Seed in the Heart of Dyslipemic Insulin-Resistant Rats.

Journal of clinical medicine

Creus A, Ferreira MR, Oliva ME, Lombardo YB.
PMID: 26828527
J Clin Med. 2016 Jan 28;5(2). doi: 10.3390/jcm5020018.

This study explores the mechanisms underlying the altered lipid metabolism in the heart of dyslipemic insulin-resistant (IR) rats fed a sucrose-rich diet (SRD) and investigates if chia seeds (rich in α-linolenic acid 18:3, n-3 ALA) improve/reverse cardiac lipotoxicity. Wistar...

Cite
Creus A, Ferreira MR, Oliva ME, et al. Mechanisms Involved in the Improvement of Lipotoxicity and Impaired Lipid Metabolism by Dietary α-Linolenic Acid Rich Salvia hispanica L (Salba) Seed in the Heart of Dyslipemic Insulin-Resistant Rats. J Clin Med. 2016;5(2)doi: 10.3390/jcm5020018.
Creus, A., Ferreira, M. R., Oliva, M. E., & Lombardo, Y. B. (2016). Mechanisms Involved in the Improvement of Lipotoxicity and Impaired Lipid Metabolism by Dietary α-Linolenic Acid Rich Salvia hispanica L (Salba) Seed in the Heart of Dyslipemic Insulin-Resistant Rats. Journal of clinical medicine, 5(2), . https://doi.org/10.3390/jcm5020018
Creus, Agustina, et al. "Mechanisms Involved in the Improvement of Lipotoxicity and Impaired Lipid Metabolism by Dietary α-Linolenic Acid Rich Salvia hispanica L (Salba) Seed in the Heart of Dyslipemic Insulin-Resistant Rats." Journal of clinical medicine vol. 5,2 (2016). doi: https://doi.org/10.3390/jcm5020018
Creus A, Ferreira MR, Oliva ME, Lombardo YB. Mechanisms Involved in the Improvement of Lipotoxicity and Impaired Lipid Metabolism by Dietary α-Linolenic Acid Rich Salvia hispanica L (Salba) Seed in the Heart of Dyslipemic Insulin-Resistant Rats. J Clin Med. 2016 Jan 28;5(2). doi: 10.3390/jcm5020018. PMID: 26828527; PMCID: PMC4773774.
Copy Download .nbib Format: NLM
ECHS1 Deficiency as a Cause of Severe Neonatal Lactic Acidosis.

JIMD reports

Ganetzky RD, Bloom K, Ahrens-Nicklas R, Edmondson A, Deardorff MA, Bennett MJ, Ficicioglu C.
PMID: 26920905
JIMD Rep. 2016;30:33-37. doi: 10.1007/8904_2016_538. Epub 2016 Feb 27.

Mitochondrial short-chain enoyl-CoA hydratase deficiency (ECHS1D) is caused by mutations in ECHS1 (OMIM 602292) and is a recently identified inborn error of valine and fatty acid metabolism. This defect leads to secondary mitochondrial dysfunction. The majority of previously reported...

Cite
Ganetzky RD, Bloom K, Ahrens-Nicklas R, et al. ECHS1 Deficiency as a Cause of Severe Neonatal Lactic Acidosis. JIMD Rep. 2016;30:33-37doi: 10.1007/8904_2016_538.
Ganetzky, R. D., Bloom, K., Ahrens-Nicklas, R., Edmondson, A., Deardorff, M. A., Bennett, M. J., & Ficicioglu, C. (2016). ECHS1 Deficiency as a Cause of Severe Neonatal Lactic Acidosis. JIMD reports, 3033-37. https://doi.org/10.1007/8904_2016_538
Ganetzky, Rebecca D, et al. "ECHS1 Deficiency as a Cause of Severe Neonatal Lactic Acidosis." JIMD reports vol. 30 (2016): 33-37. doi: https://doi.org/10.1007/8904_2016_538
Ganetzky RD, Bloom K, Ahrens-Nicklas R, Edmondson A, Deardorff MA, Bennett MJ, Ficicioglu C. ECHS1 Deficiency as a Cause of Severe Neonatal Lactic Acidosis. JIMD Rep. 2016;30:33-37. doi: 10.1007/8904_2016_538. Epub 2016 Feb 27. PMID: 26920905; PMCID: PMC5110442.
Copy Download .nbib Format: NLM
Interactions between PPAR Gamma and the Canonical Wnt/Beta-Catenin Pathway in Type 2 Diabetes and Colon Cancer.

PPAR research

Lecarpentier Y, Claes V, Vallée A, Hébert JL.
PMID: 28298922
PPAR Res. 2017;2017:5879090. doi: 10.1155/2017/5879090. Epub 2017 Feb 19.

In both colon cancer and type 2 diabetes, metabolic changes induced by upregulation of the Wnt/beta-catenin signaling and downregulation of peroxisome proliferator-activated receptor gamma (PPAR gamma) may help account for the frequent association of these two diseases. In both...

Cite
Lecarpentier Y, Claes V, Vallée A, et al. Interactions between PPAR Gamma and the Canonical Wnt/Beta-Catenin Pathway in Type 2 Diabetes and Colon Cancer. PPAR Res. 2017;2017:5879090doi: 10.1155/2017/5879090.
Lecarpentier, Y., Claes, V., Vallée, A., & Hébert, J. L. (2017). Interactions between PPAR Gamma and the Canonical Wnt/Beta-Catenin Pathway in Type 2 Diabetes and Colon Cancer. PPAR research, 20175879090. https://doi.org/10.1155/2017/5879090
Lecarpentier, Yves, et al. "Interactions between PPAR Gamma and the Canonical Wnt/Beta-Catenin Pathway in Type 2 Diabetes and Colon Cancer." PPAR research vol. 2017 (2017): 5879090. doi: https://doi.org/10.1155/2017/5879090
Lecarpentier Y, Claes V, Vallée A, Hébert JL. Interactions between PPAR Gamma and the Canonical Wnt/Beta-Catenin Pathway in Type 2 Diabetes and Colon Cancer. PPAR Res. 2017;2017:5879090. doi: 10.1155/2017/5879090. Epub 2017 Feb 19. PMID: 28298922; PMCID: PMC5337359.
Copy Download .nbib Format: NLM
Fatty-acid synthesis in chloroplasts from mustard (Sinapis alba L.) cotyledons: formation of acetyl coenzyme A by intraplastid glycolytic enzymes and a pyruvate dehydrogenase complex.

Planta

Liedvogel B, Bäuerle R.
PMID: 24232754
Planta. 1986 Dec;169(4):481-9. doi: 10.1007/BF00392096.

Chloroplasts from the cotyledons of mustard (Sinapis alba L.) seedlings were isolated on Percoll gradients, and showed a high degree of intactness (92%) and purity as judged by electron microscopy and marker-enzyme analysis (cytoplasmic contamination lower than 0.4% on...

Cite
Liedvogel B, Bäuerle R. Fatty-acid synthesis in chloroplasts from mustard (Sinapis alba L.) cotyledons: formation of acetyl coenzyme A by intraplastid glycolytic enzymes and a pyruvate dehydrogenase complex. Planta. 1986;169(4):481-9doi: 10.1007/BF00392096.
Liedvogel, B., & Bäuerle, R. (1986). Fatty-acid synthesis in chloroplasts from mustard (Sinapis alba L.) cotyledons: formation of acetyl coenzyme A by intraplastid glycolytic enzymes and a pyruvate dehydrogenase complex. Planta, 169(4), 481-9. https://doi.org/10.1007/BF00392096
Liedvogel, B, and Bäuerle, R. "Fatty-acid synthesis in chloroplasts from mustard (Sinapis alba L.) cotyledons: formation of acetyl coenzyme A by intraplastid glycolytic enzymes and a pyruvate dehydrogenase complex." Planta vol. 169,4 (1986): 481-9. doi: https://doi.org/10.1007/BF00392096
Liedvogel B, Bäuerle R. Fatty-acid synthesis in chloroplasts from mustard (Sinapis alba L.) cotyledons: formation of acetyl coenzyme A by intraplastid glycolytic enzymes and a pyruvate dehydrogenase complex. Planta. 1986 Dec;169(4):481-9. doi: 10.1007/BF00392096. PMID: 24232754.
Copy Download .nbib Format: NLM
Delivery strategies for novel vaccine formulations.

World journal of virology

Trovato M, Krebs SJ, Haigwood NL, De Berardinis P.
PMID: 24175206
World J Virol. 2012 Feb 12;1(1):4-10. doi: 10.5501/wjv.v1.i1.4.

A major challenge in vaccine design is to identify antigen presentation and delivery systems capable of rapidly stimulating both the humoral and cellular components of the immune system to elicit a strong and sustained immunity against different viral isolates....

Cite
Trovato M, Krebs SJ, Haigwood NL, et al. Delivery strategies for novel vaccine formulations. World J Virol. 2012;1(1):4-10doi: 10.5501/wjv.v1.i1.4.
Trovato, M., Krebs, S. J., Haigwood, N. L., & De Berardinis, P. (2012). Delivery strategies for novel vaccine formulations. World journal of virology, 1(1), 4-10. https://doi.org/10.5501/wjv.v1.i1.4
Trovato, Maria, et al. "Delivery strategies for novel vaccine formulations." World journal of virology vol. 1,1 (2012): 4-10. doi: https://doi.org/10.5501/wjv.v1.i1.4
Trovato M, Krebs SJ, Haigwood NL, De Berardinis P. Delivery strategies for novel vaccine formulations. World J Virol. 2012 Feb 12;1(1):4-10. doi: 10.5501/wjv.v1.i1.4. PMID: 24175206; PMCID: PMC3782264.
Copy Download .nbib Format: NLM
Development of a new enzyme-linked immunosorbent assay for the detection of anti-M2 in primary biliary cirrhosis.

Hepatology research : the official journal of the Japan Society of Hepatology

Jong-Hon K, Yajima R, Karino Y, Yoshida J, Tsuji K, Watanabe S, Horada K, Itoh Y, Sekiguchi K, Toyoda S, Maekubo H.
PMID: 11470623
Hepatol Res. 2001 Sep;21(1):1-7. doi: 10.1016/s1386-6346(01)00075-4.

We developed a new enzyme-linked immunosorbent assay (ELISA) for the detection of antimitochondrial antibody (AMA)-M2 in sera from patients with primary biliary cirrhosis (PBC), using 2-oxo-acid dehydrogenase complex (2-OADC) purified from porcine myocardium as the antigen source. The immunoreactivity...

Cite
Jong-Hon K, Yajima R, Karino Y, et al. Development of a new enzyme-linked immunosorbent assay for the detection of anti-M2 in primary biliary cirrhosis. Hepatol Res. 2001;21(1):1-7doi: 10.1016/s1386-6346(01)00075-4.
Jong-Hon, K., Yajima, R., Karino, Y., Yoshida, J., Tsuji, K., Watanabe, S., Horada, K., Itoh, Y., Sekiguchi, K., Toyoda, S., & Maekubo, H. (2001). Development of a new enzyme-linked immunosorbent assay for the detection of anti-M2 in primary biliary cirrhosis. Hepatology research : the official journal of the Japan Society of Hepatology, 21(1), 1-7. https://doi.org/10.1016/s1386-6346(01)00075-4
Jong-Hon, K, et al. "Development of a new enzyme-linked immunosorbent assay for the detection of anti-M2 in primary biliary cirrhosis." Hepatology research : the official journal of the Japan Society of Hepatology vol. 21,1 (2001): 1-7. doi: https://doi.org/10.1016/s1386-6346(01)00075-4
Jong-Hon K, Yajima R, Karino Y, Yoshida J, Tsuji K, Watanabe S, Horada K, Itoh Y, Sekiguchi K, Toyoda S, Maekubo H. Development of a new enzyme-linked immunosorbent assay for the detection of anti-M2 in primary biliary cirrhosis. Hepatol Res. 2001 Sep;21(1):1-7. doi: 10.1016/s1386-6346(01)00075-4. PMID: 11470623.
Copy Download .nbib Format: NLM
The Regulation of Pyruvate Dehydrogenase Activity in Pea Leaf Mitochondria (The Effect of Respiration and Oxidative Phosphorylation).

Plant physiology

Moore AL, Gemel J, Randall DD.
PMID: 12232037
Plant Physiol. 1993 Dec;103(4):1431-1435. doi: 10.1104/pp.103.4.1431.

The regulation of the pea (Pisum sativum) leaf mitochondrial pyruvate dehydrogenase complex by respiratory rate and oxidative phosphorylation has been investigated by measuring the respiratory activity, the redox poise of the quinone pool (Q-pool), and mitochondrial pyruvate dehydrogenase (mtPDC)...

Cite
Moore AL, Gemel J, Randall DD. The Regulation of Pyruvate Dehydrogenase Activity in Pea Leaf Mitochondria (The Effect of Respiration and Oxidative Phosphorylation). Plant Physiol. 1993;103(4):1431-1435doi: 10.1104/pp.103.4.1431.
Moore, A. L., Gemel, J., & Randall, D. D. (1993). The Regulation of Pyruvate Dehydrogenase Activity in Pea Leaf Mitochondria (The Effect of Respiration and Oxidative Phosphorylation). Plant physiology, 103(4), 1431-1435. https://doi.org/10.1104/pp.103.4.1431
Moore, A. L., et al. "The Regulation of Pyruvate Dehydrogenase Activity in Pea Leaf Mitochondria (The Effect of Respiration and Oxidative Phosphorylation)." Plant physiology vol. 103,4 (1993): 1431-1435. doi: https://doi.org/10.1104/pp.103.4.1431
Moore AL, Gemel J, Randall DD. The Regulation of Pyruvate Dehydrogenase Activity in Pea Leaf Mitochondria (The Effect of Respiration and Oxidative Phosphorylation). Plant Physiol. 1993 Dec;103(4):1431-1435. doi: 10.1104/pp.103.4.1431. PMID: 12232037; PMCID: PMC159136.
Copy Download .nbib Format: NLM
Phosphotransacetylase associated with the pyruvate dehydrogenase complex from the nitrogen fixing Azotobacter vinelandii.

FEBS letters

Bresters TW, Krul J, Scheepens PC, Veeger C.
PMID: 11946624
FEBS Lett. 1972 May 15;22(3):305-309. doi: 10.1016/0014-5793(72)80257-6.

No abstract available.

Cite
Bresters TW, Krul J, Scheepens PC, et al. Phosphotransacetylase associated with the pyruvate dehydrogenase complex from the nitrogen fixing Azotobacter vinelandii. FEBS Lett. 1972;22(3):305-309doi: 10.1016/0014-5793(72)80257-6.
Bresters, T. W., Krul, J., Scheepens, P. C., & Veeger, C. (1972). Phosphotransacetylase associated with the pyruvate dehydrogenase complex from the nitrogen fixing Azotobacter vinelandii. FEBS letters, 22(3), 305-309. https://doi.org/10.1016/0014-5793(72)80257-6
Bresters, T W., et al. "Phosphotransacetylase associated with the pyruvate dehydrogenase complex from the nitrogen fixing Azotobacter vinelandii." FEBS letters vol. 22,3 (1972): 305-309. doi: https://doi.org/10.1016/0014-5793(72)80257-6
Bresters TW, Krul J, Scheepens PC, Veeger C. Phosphotransacetylase associated with the pyruvate dehydrogenase complex from the nitrogen fixing Azotobacter vinelandii. FEBS Lett. 1972 May 15;22(3):305-309. doi: 10.1016/0014-5793(72)80257-6. PMID: 11946624.
Copy Download .nbib Format: NLM
Showing 1 to 12 of 185 entries