Results 281 to 290 of about 543,196 (314)
Advanced Science, EarlyView.LGR6 overexpression ameliorates cardiac hypertrophy by regulating metabolic reprogramming through USP4‐PPARα pathway. Abstract Metabolic reprogramming is a pivotal mechanism in the pathogenesis of pathological cardiac hypertrophy. Leucine‐rich repeat‐containing G protein‐coupled receptor 6 (Lgr6) has emerged as a significant player in cardiovascular ...
Mengmeng Zhao +7 more
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Nature, 1961
IT has previously1,2 been reported that there is an enzymatic cycle of inorganic nitrogen. In the present work, we have demonstrated that the dehydrogenating system in the cyclic processes can be separated from the reducing one, and that each dehydrogenase behaves specifically towards different inhibitors.
Kazuo Yamafuji, Yutaka Osajima
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IT has previously1,2 been reported that there is an enzymatic cycle of inorganic nitrogen. In the present work, we have demonstrated that the dehydrogenating system in the cyclic processes can be separated from the reducing one, and that each dehydrogenase behaves specifically towards different inhibitors.
Kazuo Yamafuji, Yutaka Osajima
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Stability of dehydrogenases III. malate dehydrogenases
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982Cytoplasmic and mitochondrial malate dehydrogenases from pig and chicken were studied by chemical modification of amino groups, hybridization of immobilization. Determination of thermal stability was used to characterize the different species. Modification of amino groups was found to decrease thermal stability especially when neutralization of the ...
Joachim Müller, C. Klein
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Glutamate dehydrogenase-malate dehydrogenase complex
Archives of Biochemistry and Biophysics, 1979Abstract Kinetic and Sephadex gel filtration epxeriments indicate that in the presence of palmitoyl-CoA, glutamate dehydrogenase forms a complex with mitochondrial malate dehydrogenase. In this complex, palmitoyl-CoA is bound to glutamate dehydrogenase but is not bound to malate dehydrogenase.
Linda Lou Smith +2 more
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Biochemical Journal, 2002
The kinetics of furfural inhibition of the enzymes alcohol dehydrogenase (ADH; EC 1.1.1.1), aldehyde dehydrogenase (AlDH; EC 1.2.1.5) and the pyruvate dehydrogenase (PDH) complex were studied in vitro. At a concentration of less than 2mM furfural was found to decrease the activity of both PDH and AlDH by more than 90%, whereas the ADH activity ...
Tobias Modig +2 more
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The kinetics of furfural inhibition of the enzymes alcohol dehydrogenase (ADH; EC 1.1.1.1), aldehyde dehydrogenase (AlDH; EC 1.2.1.5) and the pyruvate dehydrogenase (PDH) complex were studied in vitro. At a concentration of less than 2mM furfural was found to decrease the activity of both PDH and AlDH by more than 90%, whereas the ADH activity ...
Tobias Modig +2 more
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Serum isocitric dehydrogenase and glutamic dehydrogenase in schistosomiasis
Transactions of the Royal Society of Tropical Medicine and Hygiene, 1969Abstract 19 patients with schistosomiasis were studied for serum ICDH and GLDH activities; they were divided into two groups according to the presence or absence of hepatic involvement. Serum ICDH levels were normal, except in one patient with advanced hepatic decompensation.
M.S. Shoeb +4 more
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Annual Review of Microbiology, 1995
Structurally and functionally diverse CO dehydrogenases are key components of various energy-yielding pathways in aerobic and anaerobic microbes from the Bacteria and Archaea domains. Aerobic microbes utilize Mo-Fe-flavin CO dehydrogenases to oxidize CO in respiratory pathways.
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Structurally and functionally diverse CO dehydrogenases are key components of various energy-yielding pathways in aerobic and anaerobic microbes from the Bacteria and Archaea domains. Aerobic microbes utilize Mo-Fe-flavin CO dehydrogenases to oxidize CO in respiratory pathways.
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2015
Circulating glucocorticoid (GC) levels are controlled by the Hypothalamo-Pituitary-Adrenal (HPA) axis, but within tissues, GC availability is controlled by the isoforms of 11β (Beta)-Hydroxysteroid Dehydrogenase 11β (Beta)-HSD that interconvert inactive cortisone and active cortisol.
Jeremy W. Tomlinson, Conor Woods
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Circulating glucocorticoid (GC) levels are controlled by the Hypothalamo-Pituitary-Adrenal (HPA) axis, but within tissues, GC availability is controlled by the isoforms of 11β (Beta)-Hydroxysteroid Dehydrogenase 11β (Beta)-HSD that interconvert inactive cortisone and active cortisol.
Jeremy W. Tomlinson, Conor Woods
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1963
Publisher Summary Dehydrogenases catalyze the hydrogen transfer with pyridine nucleotides as coenzymes. Most of them are involved in the process of biological oxidation and belong to the group that is named “key pathway” enzymes. There exist numerous different apodehydrogenases in human, animal, and plant tissues, most of them catalyze oxidation ...
Werners Ph, Burns Fh
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Publisher Summary Dehydrogenases catalyze the hydrogen transfer with pyridine nucleotides as coenzymes. Most of them are involved in the process of biological oxidation and belong to the group that is named “key pathway” enzymes. There exist numerous different apodehydrogenases in human, animal, and plant tissues, most of them catalyze oxidation ...
Werners Ph, Burns Fh
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