 Oxidoreductases Acting on CH-NH Group Donors
"Oxidoreductases Acting on CH-NH Group Donors" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Enzymes catalyzing the dehydrogenation of secondary amines, introducing a C=N double bond as the primary reaction. In some cases this is later hydrolyzed.
| Descriptor ID |
D000587
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| MeSH Number(s) |
D08.811.682.662
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| Concept/Terms |
Oxidoreductases Acting on CH-NH Group Donors- Oxidoreductases Acting on CH-NH Group Donors
- Oxidoreductases Acting on CH NH Group Donors
- Secondary Amine Oxidoreductases
- Amine Oxidoreductases, Secondary
- Oxidoreductases, Secondary Amine
- Amine Oxidoreductases, Secondary Amine
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Below are MeSH descriptors whose meaning is more general than "Oxidoreductases Acting on CH-NH Group Donors".
Below are MeSH descriptors whose meaning is more specific than "Oxidoreductases Acting on CH-NH Group Donors".
This graph shows the total number of publications written about "Oxidoreductases Acting on CH-NH Group Donors" by people in this website by year, and whether "Oxidoreductases Acting on CH-NH Group Donors" was a major or minor topic of these publications.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 2001 | 0 | 1 | 1 | | 2008 | 1 | 0 | 1 |
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Below are the most recent publications written about "Oxidoreductases Acting on CH-NH Group Donors" by people in Profiles.
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Bongers KS, Fox DK, Kunkel SD, Stebounova LV, Murry DJ, Pufall MA, Ebert SM, Dyle MC, Bullard SA, Dierdorff JM, Adams CM. Spermine oxidase maintains basal skeletal muscle gene expression and fiber size and is strongly repressed by conditions that cause skeletal muscle atrophy. Am J Physiol Endocrinol Metab. 2015 Jan 15; 308(2):E144-58.
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Swanson MA, Usselman RJ, Frerman FE, Eaton GR, Eaton SS. The iron-sulfur cluster of electron transfer flavoprotein-ubiquinone oxidoreductase is the electron acceptor for electron transfer flavoprotein. Biochemistry. 2008 Aug 26; 47(34):8894-901.
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Goodman SI. Prenatal diagnosis of glutaric acidemias. Prenat Diagn. 2001 Dec; 21(13):1167-8.
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Thompson HR, Jones GM, Narkewicz MR. Ontogeny of hepatic enzymes involved in serine- and folate-dependent one-carbon metabolism in rabbits. Am J Physiol Gastrointest Liver Physiol. 2001 May; 280(5):G873-8.
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Beard SE, Goodman SI, Bemelen K, Frerman FE. Characterization of a mutation that abolishes quinone reduction by electron transfer flavoprotein-ubiquinone oxidoreductase. Hum Mol Genet. 1995 Feb; 4(2):157-61.
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Goodman SI, Axtell KM, Bindoff LA, Beard SE, Gill RE, Frerman FE. Molecular cloning and expression of a cDNA encoding human electron transfer flavoprotein-ubiquinone oxidoreductase. Eur J Biochem. 1994 Jan 15; 219(1-2):277-86.
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Goodman SI, Bemelen KF, Frerman FE. Human cDNA encoding ETF dehydrogenase (ETF:ubiquinone oxido-reductase), and mutations in glutaric acidemia type II. Prog Clin Biol Res. 1992; 375:567-72.
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Bell RB, Brownell AK, Roe CR, Engel AG, Goodman SI, Frerman FE, Seccombe DW, Snyder FF. Electron transfer flavoprotein: ubiquinone oxidoreductase (ETF:QO) deficiency in an adult. Neurology. 1990 Nov; 40(11):1779-82.
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Loehr JP, Goodman SI, Frerman FE. Glutaric acidemia type II: heterogeneity of clinical and biochemical phenotypes. Pediatr Res. 1990 Mar; 27(3):311-5.
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Kamiya M, Eimoto T, Kishimoto H, Tsudzuki T, Morishita H, Wada Y, Wakabayashi T, Hashimoto T, Goodman SI, Frerman FE, et al. Glutaric aciduria type II: autopsy study of a case with electron-transferring flavoprotein dehydrogenase deficiency. Pediatr Pathol. 1990; 10(6):1007-19.
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