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 |
|---|
| 2001 | 0 | 1 | 1 |
| 2004 | 1 | 0 | 1 |
| 2006 | 1 | 0 | 1 |
| 2007 | 3 | 0 | 3 |
| 2008 | 0 | 1 | 1 |
| 2009 | 1 | 1 | 2 |
| 2012 | 0 | 1 | 1 |
| 2016 | 1 | 0 | 1 |
| 2019 | 3 | 0 | 3 |
| 2020 | 0 | 1 | 1 |
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Below are the most recent publications written about "Mixed Function Oxygenases" by people in Profiles.
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miR-543 regulates the epigenetic landscape of myelofibrosis by targeting TET1 and TET2. JCI Insight. 2020 01 16; 5(1).
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ASPH-notch Axis guided Exosomal delivery of Prometastatic Secretome renders breast Cancer multi-organ metastasis. Mol Cancer. 2019 11 07; 18(1):156.
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Structural Origin of the Large Redox-Linked Reorganization in the 2-Oxoglutarate Dependent Oxygenase, TauD. J Am Chem Soc. 2019 09 25; 141(38):15318-15326.
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Strongly Coupled Redox-Linked Conformational Switching at the Active Site of the Non-Heme Iron-Dependent Dioxygenase, TauD. J Phys Chem B. 2019 09 19; 123(37):7785-7793.
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Spectroscopic analyses of 2-oxoglutarate-dependent oxygenases: TauD as a case study. J Biol Inorg Chem. 2017 04; 22(2-3):367-379.
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Bacillus anthracis lethal toxin reduces human alveolar epithelial barrier function. Infect Immun. 2012 Dec; 80(12):4374-87.
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Metal and substrate binding to an Fe(II) dioxygenase resolved by UV spectroscopy with global regression analysis. Anal Biochem. 2010 Apr 01; 399(1):64-71.
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Aberrant regulation of pVHL levels by microRNA promotes the HIF/VEGF axis in CLL B cells. Blood. 2009 May 28; 113(22):5568-74.
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Imidazole substituent effects on oxidative reactivity of tripodal(imid)2(thioether)CuI complexes. Inorg Chem. 2008 May 19; 47(10):4356-67.
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Succinate inhibition of alpha-ketoglutarate-dependent enzymes in a yeast model of paraganglioma. Hum Mol Genet. 2007 Dec 15; 16(24):3136-48.