Results 241 to 250 of about 94,058 (273)

Lactate dehydrogenase A-coupled NAD+ regeneration is critical for acute myeloid leukemia cell survival

Erdem A, Kaye S, Caligiore F, Johanns M, Leguay F, Schuringa JJ, Ito K, Bommer G, van Gastel N.   +8 more
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TCA cycle rewiring underpins implantation and histone acetylation programming

Kafkia E, Pladevall-Morera D, Argemi-Muntadas L, Wang G, Noberini R, Bagés-Arnal S, Anagho-Mattanovich M, Silvério-Alves R, Bonaldi T, Rabelink TJ, Moritz T, Żylicz JJ.   +11 more
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Mitochondrial pyruvate dehydrogenase phosphatase metabolism disorder in malignant tumors

Oncology Research
: This review focuses on the metabolic issues related to mitochondrial pyruvate dehydrogenase phosphatase (PDP) in malignant tumors and its potential mechanisms.
Yufeng Wang, Hui-Feng Dang, Qianqian Wang, Shuxiao Wu, Lei Han, XU Luo, Yingxia Tian, Hailin Tang   +7 more
semanticscholar   +1 more source

The relationship between human skeletal muscle pyruvate dehydrogenase phosphatase activity and muscle aerobic capacity.

Journal of applied physiology, 2011
Pyruvate dehydrogenase (PDH) is a mitochondrial enzyme responsible for regulating the conversion of pyruvate to acetyl-CoA for use in the tricarboxylic acid cycle.
L. K. Love, P. LeBlanc, J. G. Inglis, N. Bradley, J. Choptiany, G. Heigenhauser, S. Peters   +6 more
semanticscholar   +1 more source

Purification and characterization of pyruvate-dehydrogenase phosphatase from pig-heart muscle.

European Journal of Biochemistry, 1972
1 Pyruvate-dehydrogenase phosphatase was extensively purified from pig heart muscle. 2 The molecular weight was determined to be in the range between 92000 and 95000.
E. Siess, O. Wieland
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Purification and properties of pyruvate dehydrogenase phosphatase from bovine heart and kidney.

Biochemistry, 1982
Pyruvate dehydrogenase phosphatase was purified to apparent homogeneity from bovine heart and kidney mitochondria. The phosphatase has a sedimentation coefficient (S20,w) of about 7.4 S and a molecular weight (Mr) of about 150 000 as determined by ...
W. M. Teague, F. Pettit, T. Wu, S. R. Silberman, L. Reed   +4 more
semanticscholar   +1 more source

Molecular cloning and expression of the catalytic subunit of bovine pyruvate dehydrogenase phosphatase and sequence similarity with protein phosphatase 2C.

Biochemistry, 1993
After many unsuccessful attempts to detect cDNA encoding the catalytic subunit of bovine pyruvate dehydrogenase phosphatase (PDPc) in bovine cDNA libraries, an approach based on the polymerase chain reaction (PCR) was undertaken.
J. E. Lawson, X. Niu, K. Browning, H. L. Trong, J. Yan, L. Reed   +5 more
semanticscholar   +1 more source

Formation of a complex of the catalytic subunit of pyruvate dehydrogenase phosphatase isoform 1 (PDP1c) and the L2 domain forms a Ca2+ binding site and captures PDP1c as a monomer.

Biochemistry, 2004
Pyruvate dehydrogenase phosphatase isoform 1 (PDP1) is a heterodimer with a catalytic subunit (PDP1c) and a regulatory subunit (PDP1r). The activities of PDP1 or just PDP1c are greatly increased by Ca(2+)-dependent binding to the L2 (inner lipoyl) domain
A. Turkan, Y. Hiromasa, T. Roche
semanticscholar   +1 more source

Skeletal muscle type comparison of pyruvate dehydrogenase phosphatase activity and isoform expression: effects of obesity and endurance training.

American Journal of Physiology. Regulatory Integrative and Comparative Physiology, 2008
Pyruvate dehydrogenase (PDH) plays an important role in regulating carbohydrate metabolism in skeletal muscle. PDH is activated by PDH phosphatase (PDP) and deactivated by PDH kinase (PDK).
Dale Inglis, Brian D Martin, Sandra J Roy, Paul J Peters, Matthew Leblanc, Anamaria Mulligan, Laura Antolic, J. Macpherson, Greig   +8 more
semanticscholar   +1 more source