| A pathogenic P4HTM gene variant in two brothers with autism spectrum disorder. | A pathogenic P4HTM gene variant in two brothers with autism spectrum disorder.
Gülcü Üstün NS. | 03/13/2024 |
| Biallelic Mutations in P4HTM Cause Syndromic Obesity. | Biallelic Mutations in P4HTM Cause Syndromic Obesity.
Saeed S, Ning L, Badreddine A, Mirza MU, Boissel M, Khanam R, Manzoor J, Janjua QM, Khan WI, Toussaint B, Vaillant E, Amanzougarene S, Derhourhi M, Trant JF, Siegert AM, Lam BYH, Yeo GSH, Chabraoui L, Touzani A, Kulkarni A, Farooqi IS, Bonnefond A, Arslan M, Froguel P. | 08/23/2023 |
| Structure of transmembrane prolyl 4-hydroxylase reveals unique organization of EF and dioxygenase domains. | Structure of transmembrane prolyl 4-hydroxylase reveals unique organization of EF and dioxygenase domains.
Myllykoski M, Sutinen A, Koski MK, Kallio JP, Raasakka A, Myllyharju J, Wierenga RK, Koivunen P., Free PMC Article | 09/4/2021 |
| Further delineation of HIDEA syndrome. | Further delineation of HIDEA syndrome.
Maddirevula S, Ben-Omran T, AlMureikhi M, Eyaid W, Arabi H, Alkuraya H, Alfaifi A, Alfalah AH, Alsaif HS, Abdulwahab F, Alfadhel M, Alkuraya FS. | 06/26/2021 |
| The results suggest that SESN2 increases degradation of HIF-1A via AMPK-PHD regulation that contributes to inhibition of in vitro and in vivo tumorigenesis. | Sestrin2 inhibits hypoxia-inducible factor-1α accumulation via AMPK-mediated prolyl hydroxylase regulation.
Seo K, Seo S, Ki SH, Shin SM. | 12/30/2017 |
| This review will expand our knowledge of biology of HIFs, PHDs, PHD inhibitors, and bone regeneration, and it may also aid the design of novel therapies for accelerating bone repair and regeneration or inhibiting bone tumours. [review] | The hypoxia-inducible factor pathway, prolyl hydroxylase domain protein inhibitors, and their roles in bone repair and regeneration.
Fan L, Li J, Yu Z, Dang X, Wang K., Free PMC Article | 01/17/2015 |
| Results suggest that increased expression of prolyl hydroxylase (PH) might play an role in the physiology of uterine leiomyoma during the menstrual cycle. | Human prolyl hydroxylase expression in uterine leiomyoma during the menstrual cycle.
Iwahashi M, Muragaki Y, Ino K., Free PMC Article | 08/31/2013 |
| crystal structure of the peptide-substrate-binding domain | The peptide-substrate-binding domain of collagen prolyl 4-hydroxylases is a tetratricopeptide repeat domain with functional aromatic residues.
Pekkala M, Hieta R, Bergmann U, Kivirikko KI, Wierenga RK, Myllyharju J. | 01/21/2010 |
| the longest and shortest isoenzymes have major transcripts encoding inactive polypeptides, which suggest novel regulation by alternative splicing. | Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor.
Hirsilä M, Koivunen P, Günzler V, Kivirikko KI, Myllyharju J. | 01/21/2010 |
| Data suggest that PH-4 is a novel hypoxia-inducible factor-prolyl hydroxylase that may be involved in the degradation of hypoxia-inducible transcription factors under normoxia. | Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors.
Oehme F, Ellinghaus P, Kolkhof P, Smith TJ, Ramakrishnan S, Hütter J, Schramm M, Flamme I. | 01/21/2010 |
| This review summarizes recent progress in elucidating the molecular mechanisms of hypoxia-inducible factor (HIF)-1 activation, focusing on the role of oxygen-dependent asparaginyl hydroxylase in hypoxia signal transduction. | Regulation of hypoxia-inducible factor 1 by prolyl and asparaginyl hydroxylases.
Hirota K, Semenza GL. | 01/21/2010 |