Mixed Function Oxygenases
"Mixed Function Oxygenases" 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.
Widely distributed enzymes that carry out oxidation-reduction reactions in which one atom of the oxygen molecule is incorporated into the organic substrate; the other oxygen atom is reduced and combined with hydrogen ions to form water. They are also known as monooxygenases or hydroxylases. These reactions require two substrates as reductants for each of the two oxygen atoms. There are different classes of monooxygenases depending on the type of hydrogen-providing cosubstrate (COENZYMES) required in the mixed-function oxidation.
| Descriptor ID |
D006899
|
| MeSH Number(s) |
D08.811.682.690.708
|
| Concept/Terms |
Mixed Function Oxygenases- Mixed Function Oxygenases
- Oxygenases, Mixed Function
- Monooxygenases
- Hydroxylases
- Mixed Function Oxidases
- Oxidases, Mixed Function
|
Below are MeSH descriptors whose meaning is more general than "Mixed Function Oxygenases".
Below are MeSH descriptors whose meaning is more specific than "Mixed Function Oxygenases".
This graph shows the total number of publications written about "Mixed Function Oxygenases" by people in this website by year, and whether "Mixed Function Oxygenases" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2002 | 0 | 1 | 1 |
| 2008 | 0 | 1 | 1 |
| 2009 | 0 | 1 | 1 |
| 2013 | 0 | 1 | 1 |
| 2015 | 0 | 1 | 1 |
| 2016 | 1 | 0 | 1 |
| 2020 | 1 | 0 | 1 |
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Below are the most recent publications written about "Mixed Function Oxygenases" by people in Profiles.
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Kalay Yildizhan I, G?kpinar Ili E, Onoufriadis A, Kocyigit P, Kesidou E, Simpson MA, McGrath JA, Kutlay NY, Kundakci N. New Homozygous Missense MSMO1 Mutation in Two Siblings with SC4MOL Deficiency Presenting with Psoriasiform Dermatitis. Cytogenet Genome Res. 2020; 160(9):523-530.
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Soehn AS, Rattay TW, Beck-W?dl S, Sch?ferhoff K, Monk D, D?bler-Neumann M, H?rtnagel K, Schl?ter A, Ruiz M, Pujol A, Z?chner S, Riess O, Sch?le R, Bauer P, Sch?ls L. Uniparental disomy of chromosome 16 unmasks recessive mutations of FA2H/SPG35 in 4 families. Neurology. 2016 Jul 12; 87(2):186-91.
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Carlson K, Pomerantz SC, Vafa O, Naso M, Strohl W, Mains RE, Eipper BA. Optimizing production of Fc-amidated peptides by Chinese hamster ovary cells. BMC Biotechnol. 2015 Oct 16; 15:95.
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Hashimoto H, Pais JE, Zhang X, Saleh L, Fu ZQ, Dai N, Corr?a IR, Zheng Y, Cheng X. Structure of a Naegleria Tet-like dioxygenase in complex with 5-methylcytosine DNA. Nature. 2014 Feb 20; 506(7488):391-5.
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Ellis DJ, Usman MH, Milner PG, Canafax DM, Ezekowitz MD. The first evaluation of a novel vitamin K antagonist, tecarfarin (ATI-5923), in patients with atrial fibrillation. Circulation. 2009 Sep 22; 120(12):1029-35, 2 p following 1035.
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Li Q, Schurgers LJ, Smith AC, Tsokos M, Uitto J, Cowen EW. Co-existent pseudoxanthoma elasticum and vitamin K-dependent coagulation factor deficiency: compound heterozygosity for mutations in the GGCX gene. Am J Pathol. 2009 Feb; 174(2):534-40.
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Rodrigues AD, Rushmore TH. Cytochrome P450 pharmacogenetics in drug development: in vitro studies and clinical consequences. Curr Drug Metab. 2002 Jun; 3(3):289-309.