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

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

Pharmacogenetics and genomics - 1 Jul 2012

Liu Wen, Poole Elizabeth M, Ulrich Cornelia M, Kulmacz Richard J

Abstract excerpt

OBJECTIVES: Aspirin (ASA), a major antiplatelet and cancer-preventing drug, irreversibly blocks the cyclooxygenase (COX) activity of prostaglandin H synthase-1 (PGHS-1). Considerable differences in ASA effectiveness are observed between individuals, and some of this variability may be due to PGHS-1 protein variants. Our overall aim is to determine which, if any, of the known variants in the mature PGHS-1 protein...

Read the complete abstract on PubMed

Topics

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

Share to Aspirin
Share to Binding Sites
Share to Cyclooxygenase 1

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cyclooxygenase Inhibitors

Share to Genetic Variation

Share to Hydrolysis

Share to Kinetics

Share to Models, Theoretical

Source

Open in PubMed Open full text

Identifiers

PMID: 22513397
DOI: 10.1097/FPC.0b013e32835366f6
PMCID: PMC3376194

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Decreased cyclooxygenase inhibition by aspirin in polymorphic variants of human prostaglandin H synthase-1.PMID 22513397Read ↗

Identification and functional characterization of polymorphisms in human cyclooxygenase-1 (PTGS1).Semantic proximity Read ↗

Genetic variation in cyclooxygenase 1: Effects on response to aspirinSemantic proximity Read ↗

Functional analysis of human thromboxane synthase polymorphic variants.Semantic proximity Read ↗

Arginine 120 of prostaglandin G/H synthase-1 is required for the inhibition by nonsteroidal anti-inflammatory drugs containing a carboxylic acid moiety.Semantic proximity Read ↗

Analysis of genetic polymorphism and biochemical characterization of a functionally decreased variant in prostacyclin synthase gene (CYP8A1) in humans.Semantic proximity Read ↗

Prostaglandin endoperoxide synthase. The aspirin acetylation region.Semantic proximity Read ↗

A computational prospect to aspirin side effects: aspirin and COX-1 interaction analysis based on non-synonymous SNPs.Semantic proximity Read ↗

Pharmacogenomics in aspirin intolerance.Semantic proximity Read ↗

Frequency of Genetic Polymorphisms of COX1 , GPIIIa and P2Y1 in a Chinese Population and Association with Attenuated Response to AspirinSemantic proximity Read ↗

Cyclooxygenase 1(COX1) polymorphisms in African-American and caucasian populationsSemantic proximity Read ↗

Role of Tyr348 in Tyr385 radical dynamics and cyclooxygenase inhibitor interactions in prostaglandin H synthase-2.Semantic proximity Read ↗

Human platelet 12-lipoxygenase: naturally occurring Q261/R261 variants and N544L mutant show altered activity but unaffected substrate binding and membrane association behavior.Semantic proximity Read ↗

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