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Metabolomics1H HR-MAS NMR based metabolomics of cancer cells responding to two different doses of the diruthenium trithiolato complex [(p-MeC6H4iPr)2Ru2(SC6H4-p-But)3]+ (DiRu-1)
The trithiolato bridged diruthenium complex DiRu-1 [(p-MeC6H4iPr)2Ru2(SC6H4-p-But)3]+ is highly cytotoxic against various cancer cell lines, but its exact mode of action remained unknown. The present 1H HR-MAS NMR based metabolomic study performed on the ovarian cancer cell lines A2780, its cisPt re...
2019-07-04 | MTBLS1014 | MetaboLights
Genomics
P3H1 in esophageal squamous cell carcinoma
PRJNA985267 | ENA
UnknownCharacterization of PPIB interaction in the P3H1 ternary complex and implications for its pathological mutations.
Not available
S-EPMC11105654 | biostudies-literature
UnknownThe structural basis for the collagen processing by human P3H1/CRTAP/PPIB ternary complex.
Not available
S-EPMC11381544 | biostudies-literature
UnknownP3H1 promotes malignant progression of esophageal squamous cell carcinoma (ESCC) and modulates the immune microenvironment.
Not available
S-EPMC12603417 | biostudies-literature
UnknownPhenotypic Variation in Vietnamese Osteogenesis Imperfecta Patients Sharing a Recessive P3H1 Pathogenic Variant.
Not available
S-EPMC8950175 | biostudies-literature
UnknownA Founder Intronic Variant in P3H1 Likely Results in Aberrant Splicing and Protein Truncation in Patients of Karen Descent with Osteogenesis Imperfecta Type VIII.
Not available
S-EPMC9956579 | biostudies-literature
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 
UnknownMilder presentation of osteogenesis imperfecta type VIII due to compound heterozygosity for a predicted loss-of-function variant and novel missense variant in P3H1-further expansion of the phenotypic spectrum.
Not available
S-EPMC10111797 | biostudies-literature
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 
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