Results 141 to 150 of about 27,301 (195)
Pyruvate Carboxylase Attenuates Myocardial Ischemia-Reperfusion Injury in Heart Transplantation via Wnt/β-Catenin-Mediated Glutamine Metabolism. [PDF]
Wang Z +8 more
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Circ-CAMTA1 regulated by Ca<sup>2+</sup> influx inhibited pyruvate carboxylase activity and modulate T cell function in patients with systemic lupus erythematosus. [PDF]
Yu HC, Tseng HH, Huang HB, Lu MC.
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Melanoma-derived versican reactivates tumor-associated macrophages by upregulating pyruvate carboxylase through TLR2-MyD88-RelB axis under normoxia. [PDF]
Shu Y, Zhou L, Qian J, Zhu WG.
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FBXW7 alleviates c-MYC repression of pyruvate carboxylase to support metabolic flexibility
Lisci M +4 more
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International Journal of Biochemistry and Cell Biology, 1998
Pyruvate carboxylase [EC 6.4.1.1] is a member of the family of biotin-dependent carboxylases and is found widely among eukaryotic tissues and in many prokaryotic species. It catalyses the ATP-dependent carboxylation of pyruvate to form oxaloacetate which may be utilised in the synthesis of glucose, fat, some amino acids or their derivatives and several
Sarawut Jitrapakdee +2 more
exaly +4 more sources
Pyruvate carboxylase [EC 6.4.1.1] is a member of the family of biotin-dependent carboxylases and is found widely among eukaryotic tissues and in many prokaryotic species. It catalyses the ATP-dependent carboxylation of pyruvate to form oxaloacetate which may be utilised in the synthesis of glucose, fat, some amino acids or their derivatives and several
Sarawut Jitrapakdee +2 more
exaly +4 more sources
Pyruvate carboxylase deficiency
Journal of Inherited Metabolic Disease, 1984AbstractThe causes of congenital lactic acidaemia are outlined. Isolated pyruvate carboxylase deficiency is reviewed in detail with a report of a recent case and a discussion of the biochemical consequences. Other causes of defective pyruvate carboxylation are described, particularly the combined carboxylase defects.
K, Bartlett +4 more
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Substrate activation of pyruvate carboxylase by pyruvate
Biochemical and Biophysical Research Communications, 1969Abstract A kinetic analysis of pyruvate carboxylase isolated from sheep liver and using pyruvate as the variable substrate revealed non-Michaelis Menten kinetic. Double reciprocal plots were biphasic and R S values of 222 were obtained. Hill plots prepared from the initial velocity data showed that at low pyruvate concentrations, the slope of the ...
H, Taylor, J, Nielsen, D B, Keech
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