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
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MeSH Number(s) |
D08.811.682.690.708
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Concept/Terms |
Mixed Function Oxygenases- Mixed Function Oxygenases
- Oxygenases, Mixed Function
- Monooxygenases
- Hydroxylases
- Mixed Function Oxidases
- Oxidases, Mixed Function
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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 |
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1991 | 0 | 1 | 1 | 1998 | 1 | 2 | 3 | 1999 | 0 | 1 | 1 | 2000 | 1 | 0 | 1 | 2003 | 1 | 0 | 1 | 2004 | 3 | 0 | 3 | 2005 | 1 | 0 | 1 | 2006 | 2 | 1 | 3 | 2008 | 2 | 1 | 3 | 2009 | 0 | 2 | 2 | 2010 | 2 | 1 | 3 | 2011 | 1 | 1 | 2 | 2012 | 2 | 0 | 2 | 2013 | 0 | 4 | 4 | 2014 | 2 | 2 | 4 | 2015 | 1 | 1 | 2 | 2016 | 1 | 1 | 2 | 2017 | 1 | 0 | 1 | 2018 | 1 | 1 | 2 | 2021 | 1 | 0 | 1 | 2022 | 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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Hains AE, Uppal S, Cao JZ, Salwen HR, Applebaum MA, Cohn SL, Godley LA. MYCN and HIF-1 directly regulate TET1 expression to control 5-hmC gains and enhance neuroblastoma cell migration in hypoxia. Epigenetics. 2022 Dec; 17(13):2056-2074.
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Wang Y, Katanski CD, Watkins C, Pan JN, Dai Q, Jiang Z, Pan T. A high-throughput screening method for evolving a demethylase enzyme with improved and new functionalities. Nucleic Acids Res. 2021 03 18; 49(5):e30.
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Xicola RM, Manojlovic Z, Augustus GJ, Kupfer SS, Emmadi R, Alagiozian-Angelova V, Triche T, Salhia B, Carpten J, Llor X, Ellis NA. Lack of APC somatic mutation is associated with early-onset colorectal cancer in African Americans. Carcinogenesis. 2018 12 13; 39(11):1331-1341.
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Good CR, Panjarian S, Kelly AD, Madzo J, Patel B, Jelinek J, Issa JJ. TET1-Mediated Hypomethylation Activates Oncogenic Signaling in Triple-Negative Breast Cancer. Cancer Res. 2018 08 01; 78(15):4126-4137.
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Good CR, Madzo J, Patel B, Maegawa S, Engel N, Jelinek J, Issa JJ. A novel isoform of TET1 that lacks a CXXC domain is overexpressed in cancer. Nucleic Acids Res. 2017 Aug 21; 45(14):8269-8281.
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Yang YA, Zhao JC, Fong KW, Kim J, Li S, Song C, Song B, Zheng B, He C, Yu J. FOXA1 potentiates lineage-specific enhancer activation through modulating TET1 expression and function. Nucleic Acids Res. 2016 09 30; 44(17):8153-64.
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Huang H, Jiang X, Wang J, Li Y, Song CX, Chen P, Li S, Gurbuxani S, Arnovitz S, Wang Y, Weng H, Neilly MB, He C, Li Z, Chen J. Identification of MLL-fusion/MYC?miR-26?TET1 signaling circuit in MLL-rearranged leukemia. Cancer Lett. 2016 Mar 28; 372(2):157-65.
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Laukka T, Mariani CJ, Ihantola T, Cao JZ, Hokkanen J, Kaelin WG, Godley LA, Koivunen P. Fumarate and Succinate Regulate Expression of Hypoxia-inducible Genes via TET Enzymes. J Biol Chem. 2016 Feb 19; 291(8):4256-65.
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Chapman CG, Mariani CJ, Wu F, Meckel K, Butun F, Chuang A, Madzo J, Bissonnette MB, Kwon JH, Godley LA. TET-catalyzed 5-hydroxymethylcytosine regulates gene expression in differentiating colonocytes and colon cancer. Sci Rep. 2015 Dec 03; 5:17568.
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Acheson JF, Bailey LJ, Elsen NL, Fox BG. Structural basis for biomolecular recognition in overlapping binding sites in a diiron enzyme system. Nat Commun. 2014 Sep 24; 5:5009.
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