Hypoxia-Inducible Factor-Proline Dioxygenases
"Hypoxia-Inducible Factor-Proline Dioxygenases" 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.
Dioxygenase enzymes that specifically hydroxylate a PROLINE residue on the HYPOXIA-INDUCIBLE FACTOR 1, ALPHA SUBUNIT. They are OXYGEN-dependent enzymes that play an important role in mediating cellular adaptive responses to HYPOXIA.
| Descriptor ID |
D064799
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| MeSH Number(s) |
D08.811.682.690.416.617.500 D08.811.682.690.708.694.500
|
| Concept/Terms |
Hypoxia-Inducible Factor-Proline Dioxygenases- Hypoxia-Inducible Factor-Proline Dioxygenases
- Dioxygenases, Hypoxia-Inducible Factor-Proline
- Factor-Proline Dioxygenases, Hypoxia-Inducible
- Hypoxia Inducible Factor Proline Dioxygenases
- HIF Prolyl-4-Hydroxylases
- HIF Prolyl 4 Hydroxylases
- Prolyl-4-Hydroxylases, HIF
- Hypoxia-Inducible Factor-Proline Dioxygenase
- Dioxygenase, Hypoxia-Inducible Factor-Proline
- Factor-Proline Dioxygenase, Hypoxia-Inducible
- Hypoxia Inducible Factor Proline Dioxygenase
- HIF Prolyl-4-Hydroxylase
- HIF Prolyl 4 Hydroxylase
- Prolyl-4-Hydroxylase, HIF
|
Below are MeSH descriptors whose meaning is more general than "Hypoxia-Inducible Factor-Proline Dioxygenases".
Below are MeSH descriptors whose meaning is more specific than "Hypoxia-Inducible Factor-Proline Dioxygenases".
This graph shows the total number of publications written about "Hypoxia-Inducible Factor-Proline Dioxygenases" by people in this website by year, and whether "Hypoxia-Inducible Factor-Proline Dioxygenases" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2012 | 0 | 1 | 1 |
| 2014 | 1 | 0 | 1 |
| 2015 | 0 | 1 | 1 |
| 2016 | 0 | 1 | 1 |
| 2020 | 1 | 0 | 1 |
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Below are the most recent publications written about "Hypoxia-Inducible Factor-Proline Dioxygenases" by people in Profiles.
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Fong LY, Taccioli C, Palamarchuk A, Tagliazucchi GM, Jing R, Smalley KJ, Fan S, Altemus J, Fiehn O, Huebner K, Farber JL, Croce CM. Abrogation of esophageal carcinoma development in miR-31 knockout rats. Proc Natl Acad Sci U S A. 2020 03 17; 117(11):6075-6085.
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Schoepflin ZR, Shapiro IM, Risbud MV. Class I and IIa HDACs Mediate HIF-1a Stability Through PHD2-Dependent Mechanism, While HDAC6, a Class IIb Member, Promotes HIF-1a Transcriptional Activity in Nucleus Pulposus Cells of the Intervertebral Disc. J Bone Miner Res. 2016 06; 31(6):1287-99.
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Zhang J, Wang C, Chen X, Takada M, Fan C, Zheng X, Wen H, Liu Y, Wang C, Pestell RG, Aird KM, Kaelin WG, Liu XS, Zhang Q. EglN2 associates with the NRF1-PGC1a complex and controls mitochondrial function in breast cancer. EMBO J. 2015 Dec 02; 34(23):2953-70.
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Li J, Yuan W, Jiang S, Ye W, Yang H, Shapiro IM, Risbud MV. Prolyl-4-hydroxylase domain protein 2 controls NF-?B/p65 transactivation and enhances the catabolic effects of inflammatory cytokines on cells of the nucleus pulposus. J Biol Chem. 2015 Mar 13; 290(11):7195-207.
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Fujita N, Hirose Y, Tran CM, Chiba K, Miyamoto T, Toyama Y, Shapiro IM, Risbud MV. HIF-1-PHD2 axis controls expression of syndecan 4 in nucleus pulposus cells. FASEB J. 2014 Jun; 28(6):2455-65.
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Fujita N, Gogate SS, Chiba K, Toyama Y, Shapiro IM, Risbud MV. Prolyl hydroxylase 3 (PHD3) modulates catabolic effects of tumor necrosis factor-a (TNF-a) on cells of the nucleus pulposus through co-activation of nuclear factor ?B (NF-?B)/p65 signaling. J Biol Chem. 2012 Nov 16; 287(47):39942-53.