Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural and Biophysical Analyses of Human Prostamide/Prostaglandin F Synthase with Two Active Form-Mimicking Mutations.

Biomolecules - 7 Feb 2026

Cheon Sang Won, Nguyen Yen Thi Kim, Kang Jin Mo, Yu Youngbeom, Heo Yoonyoung, Kim Hyoun Sook, Han Byung Woo

Abstract excerpt

Human prostamide/prostaglandin F synthase (PGFS) catalyzes the NADPH-dependent conversion of prostaglandin H2 (PGH2) to prostaglandin F2α that plays a key role in regulating intraocular pressure and labor. Despite its physiological importance, structural and biochemical information of the human PGFS has been limited because of difficulties in obtaining sufficient quality of PGFS wild-type crystal and short...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Catalytic Domain
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Dynamics Simulation

Share to Mutation

Share to Protein Conformation

Source

Open in PubMed Open full text

Identifiers

PMID: 41750332
DOI: 10.3390/biom16020262
PMCID: PMC12938796

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and Biophysical Analyses of Human Prostamide/Prostaglandin F Synthase with Two Active Form-Mimicking Mutations.PMID 41750332Read ↗

Structural and mutational analysis of Trypanosoma brucei prostaglandin H2 reductase provides insight into the catalytic mechanism of aldo-ketoreductases.Semantic proximity Read ↗

Structural and functional characterization of human microsomal prostaglandin E synthase-1 by computational modeling and site-directed mutagenesis.Semantic proximity Read ↗

Characterization of the substrate mimic bound to engineered prostacyclin synthase in solution using high-resolution NMR spectroscopy and mutagenesis: implication of the molecular mechanism in biosynthesis of prostacyclin.Semantic proximity Read ↗

Human furin Cys198 imposes dihedral and positional restraints on His194 for optimal Ser386-proton transfer.Semantic proximity Read ↗

Structure-function analysis of human l-prostaglandin D synthase bound with fatty acid molecules.Semantic proximity Read ↗

Recapitulating the frataxin activation mechanism in an engineered bacterial cysteine desulfurase supports the architectural switch modelSemantic proximity Read ↗

High-resolution structures of mutants of residues that affect access to the ligand-binding cavity of human lipocalin-type prostaglandin D synthase.Semantic proximity Read ↗

Decreased cyclooxygenase inhibition by aspirin in polymorphic variants of human prostaglandin H synthase-1.Semantic proximity Read ↗

Lattice stabilization and enhanced diffraction in human p38 alpha crystals by protein engineering.Semantic proximity Read ↗

Identification of thromboxane synthase amino acid residues involved in heme-propionate binding.Semantic proximity Read ↗

Structure of human steroid 5α-reductase 2 with anti-androgen drug finasterideSemantic proximity Read ↗

Crystal structure and possible catalytic mechanism of microsomal prostaglandin E synthase type 2 (mPGES-2).Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.