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ProteomicsAnalysis of proline and lysine post-translational modifications of collagen from prolyl 3-hydroxylase 3 and lysyl hydroxylase 1 null mice
We performed shotgun proteomic analysis of type V collagens purified from wild-type mice and prolyl 3-hydroxylase 3 or lysyl hydroxylase 1 null mice by LC-MS after trypsin digestion for identification of lysine glycosylation sites.
ORGANISM(S): Mus Musculus (mouse) 
2021-02-19 | PXD019748 | JPOST Repository
ProteomicsTargeting Prolyl 3-hydroxylase 1 Inhibits Pancreatic Cancer Progression and Macrophage Immunity
Using transcriptome sequencing, proteomic analyses and engineered mouse model, we have revealed a novel and pivotal role of Prolyl 3-hydroxylase 1 (P3H1) in PDAC. The expression of P3H1 is elevated in PDAC and correlates with poor outcomes in human patients. The genetic deletion of P3H1 in KPC mouse...
ORGANISM(S): Homo sapiens (Human) 
2026-02-13 | PXD070325 | Pride
P3h1 Plk1 Chemotherapy Tumor microenvironment Pancreatic ductal adenocarcinoma 
TranscriptomicsTuning the transcriptional response to hypoxia through HIF prolyl- and asparaginyl-hydroxylase inhibition:Sequencing Data
The hypoxia inducible factor (HIF) system orchestrates cellular responses to hypoxia in animals. HIF is an /-heterodimeric transcription factor that regulates the expression of hundreds of genes in a context dependent manner. A hypoxia-sensing component of the HIF system involves oxygen-dependent ca...
ORGANISM(S): Homo sapiens 
2016-10-25 | E-MTAB-4264 | biostudies-arrayexpress
ProteomicsPHD3 and FIH substrates cluster in distinct signalling pathways
Amino acid hydroxylation is a common post-translational modification which regulates intra and inter-molecular protein-protein interactions. The modifications are regulated by a family of 2-oxoglutarate (2OG) dependent enzymes and although the biochemistry is well understood, until now only a few su...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080766 | MassIVE
ProteomicsSite-specific quantification of collagen post-translational modifications reveals profound disruption of the collagen biosynthetic network upon prolyl-3-hydroxylase 1 deficiency
Type I collagen is the main structural protein in mammals and other vertebrate life forms. During the biosynthesis of collagens, prolyl-3-hydroxylase 1 (P3H1) catalyzes 3-hydroxylation of proline residues and acts as a chaperone. Deficiency of P3H1 causes Osteogenesis Imperfecta (OI), a hereditary d...
ORGANISM(S): Mus musculus (Mouse) 
2026-04-02 | PXD053751 | Pride
Glycosylation Collagen Tendon Post-translational modification (ptm) Prolyl-3-hydroxylase Hydroxyproline 
UnknownProlyl hydroxylase 3 controls the intestine goblet cell generation through stabilizing ATOH1.
Not available
S-EPMC7308305 | biostudies-literature
GenomicsEndothelial Prolyl Hydroxylase 3 Mitigates Maladaptive Inflammation to Promote Post-Ischemic Kidney Repair
Endothelial Prolyl Hydroxylase 3 Mitigates Maladaptive Inflammation to Promote Post-Ischemic Kidney Repair
PRJNA1251356 | ENA
UnknownProlyl 3-hydroxylase 1 and CRTAP are mutually stabilizing in the endoplasmic reticulum collagen prolyl 3-hydroxylation complex.
Not available
S-EPMC2796888 | biostudies-literature
UnknownProlyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone disorder resembling lethal/severe osteogenesis imperfecta.
Not available
S-EPMC7510175 | biostudies-literature
UnknownProlyl 3-Hydroxylase 2 Is a Molecular Player of Angiogenesis.
Not available
S-EPMC8069486 | biostudies-literature
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