Results 201 to 210 of about 491,817 (253)
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Monoamine Oxidase and Mitochondrial Respiration

Journal of Neurochemistry, 1999
Abstract : Mitochondrial defects encompassing complexes I‐IV of the electron transport chain characterize a relatively large number of neurodegenerative diseases. The relationships between mitochondrial lesions and recently described genetic alterations have not yet been defined.
G, Cohen, N, Kesler
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Regulation of Mitochondrial Respiration in Liver

1986
In studies on the control of mitochondrial respiration carried out in the past 10 years, particular attention has been focussed on cytochrome c oxidase and the adenine nucleotide translocator as rate-controlling steps. On the basis of the observation that the first two phosphorylation sites of the respiratory chain are in near equilibrium with the ...
Verhoeven, A. J.   +5 more
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Parathyroid Hormone and Mitochondrial Respiration

Endocrinology, 1964
Parathyroid hormone added in vitro stimulates anion-dependent respiration in isolated liver and kidney mitochondria. This response depends upon Mg++ (or Mn++) and substrate and is inhibited by uncouplers and inhibitors of electron transport but not by oligomycin or triethyltin, inhibitors of oxidative phosphorylation.
M, FANG, H, RASMUSSEN
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p53 Regulates Mitochondrial Respiration

Science, 2006
The energy that sustains cancer cells is derived preferentially from glycolysis. This metabolic change, the Warburg effect, was one of the first alterations in cancer cells recognized as conferring a survival advantage. Here, we show that p53, one of the most frequently mutated genes in cancers, modulates the balance between the ...
Satoaki, Matoba   +8 more
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Ochratoxin A: Inhibition of Mitochondrial Respiration

Science, 1970
Ochratoxin A is a fungal metabolite which induces pathological changes in animals. The toxin was isolated from cultures of Aspergillus ochraceus and purified by thin-layer chromatography. Ochratoxin A and one of its hydrolysis products, dihydroisocoumarin, severely inhibited coupled respiration when applied at low ...
J H, Moore, B, Truelove
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Regulation of mitochondrial respiration in senescence

Journal of Cellular Physiology, 1972
AbstractThe ADP‐stimulated (State 3) respiration of myocardial mitochondria with glutamate‐malate, glutamate‐pyruvate, palmitylcarnitine and β‐hydroxybutyrate as substrates declined in rats after the age of 20 months. There was no significant decline in pyruvate‐malate, α‐oxoglutarate, palmityl‐CoA, succinate and ascorbate cytochrome c oxidation ...
J C, Chen, J B, Warshaw, D R, Sanadi
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Control of mitochondrial respiration in muscle

Molecular and Cellular Biochemistry, 1988
Control of mitochondrial respiration depends on ADP availability to the F1-ATPase. An electrochemical gradient of ADP and ATP across the mitochondrial inner membrane is maintained by the adenine nucleotide translocase which provides ADP to the matrix for ATP synthesis and ATP for energy-dependent processes in the cytosol.
J B, McMillin, D F, Pauly
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Uncoupling Mitochondrial Respiration for Diabesity

Rejuvenation Research, 2016
Until recently, the mechanism of adaptive thermogenesis was ascribed to the expression of uncoupling protein 1 (UCP1) in brown and beige adipocytes. UCP1 is known to catalyze a proton leak of the inner mitochondrial membrane, resulting in uncoupled oxidative metabolism with no production of adenosine triphosphate and increased energy expenditure.
James W, Larrick   +2 more
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Effect of Ryanodine on Mitochondrial Respiration

Pharmacology, 2008
Ryanodine is a pharmacological agent that stimulates calcium leakage into the cytoplasm resulting in an increase in tension. In skeletal muscle, ryanodine acts primarily on the sarcoplasmic reticulum whereas in smooth muscle, the sites of action are less clear.
R M, Levin   +4 more
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The effect of acetaldehyde on mitochondrial respiration

Experimental Cell Research, 1963
Abstract The inhibiting effect of acetaldehyde on the pyruvate oxidation in mitochondria from various tissues has been investigated. The following sequence was found as to the degree of aldehyde inhibition: liver Liver and kidney mitochondria oxidize acetaldehyde rapidly compared with muscle and brain mitochondria.
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