Coxibs interfere with the action of aspirin by binding tightly to one monomer of cyclooxygenase-1 - Wikidata - awgldk - TriplyDB

Coxibs interfere with the action of aspirin by binding tightly to one monomer of cyclooxygenase-1

Coxibs interfere with the action of aspirin by binding tightly to one monomer of cyclooxygenase-1

http://www.wikidata.org/entity/Q27658412

about

Enzymes of the cyclooxygenase pathways of prostanoid biosynthesis Human cyclooxygenase-2 is a sequence homodimer that functions as a conformational heterodimer Impairment of aspirin antiplatelet effects by non-opioid analgesic medication Endocannabinoid oxygenation by cyclooxygenases, lipoxygenases, and cytochromes P450: cross-talk between the eicosanoid and endocannabinoid signaling pathways Structural Basis for L-Lysine Feedback Inhibition of Homocitrate Synthase Comparison of Cyclooxygenase-1 Crystal Structures: Cross-Talk between Monomers Comprising Cyclooxygenase-1 Homodimers,Substrate-Selective Inhibition of Cyclooxygenase-2: Development and Evaluation of Achiral Profen Probes (R)-Profens are substrate-selective inhibitors of endocannabinoid oxygenation by COX-2 Exploring the molecular determinants of substrate-selective inhibition of cyclooxygenase-2 by lumiracoxib Prediction of the potency of mammalian cyclooxygenase inhibitors with ensemble proteochemometric modeling.Chemically Aware Model Builder (camb): an R package for property and bioactivity modelling of small molecules Mass spectrometry-based approaches to targeted quantitative proteomics in cardiovascular disease Molecular basis of cyclooxygenase enzymes (COXs) selective inhibition Aspirin modulates innate inflammatory response and inhibits the entry of Trypanosoma cruzi in mouse peritoneal macrophages.Asymmetric acetylation of the cyclooxygenase-2 homodimer by aspirin and its effects on the oxygenation of arachidonic, eicosapentaenoic, and docosahexaenoic acids.An overview of the key routes to the best selling 5-membered ring heterocyclic pharmaceuticals.Differential impairment of aspirin-dependent platelet cyclooxygenase acetylation by nonsteroidal antiinflammatory drugs.Etoricoxibium picrate Prevention of upper gastrointestinal haemorrhage: current controversies and clinical guidance Action at a distance: mutations of peripheral residues transform rapid reversible inhibitors to slow, tight binders of cyclooxygenase-2.Prospective performance evaluation of selected common virtual screening tools. Case study: Cyclooxygenase (COX) 1 and 2.Classification of scaffold-hopping approaches Human cyclooxygenase-1 activity and its responses to COX inhibitors are allosterically regulated by nonsubstrate fatty acids.Decreased cyclooxygenase inhibition by aspirin in polymorphic variants of human prostaglandin H synthase-1.Different Fatty Acids Compete with Arachidonic Acid for Binding to the Allosteric or Catalytic Subunits of Cyclooxygenases to Regulate Prostanoid Synthesis.Crystal Structure of Aspirin-Acetylated Human Cyclooxygenase-2: Insight into the Formation of Products with Reversed Stereochemistry.Celecoxib interferes to a limited extent with aspirin-mediated inhibition of platelets aggregation.Pre-existent asymmetry in the human cyclooxygenase-2 sequence homodimer.Mechanistic and pharmacological issues of aspirin as an anticancer agent.Computational Drug Target Screening through Protein Interaction Profiles.Drug-drug interaction between NSAIDS and low-dose aspirin: a focus on cardiovascular and GI toxicity.Competition between low-dose aspirin and other NSAIDs for COX-1 binding and its clinical consequences for the drugs' antiplatelet effects.Cyclooxygenase-2 catalysis and inhibition in lipid bilayer nanodiscs Celecoxib for the treatment of atherosclerosis.Inhibition of cyclooxygenase-1 and cyclooxygenase-2 impairs Trypanosoma cruzi entry into cardiac cells and promotes differential modulation of the inflammatory response.A network integration approach for drug-target interaction prediction and computational drug repositioning from heterogeneous information.[Unexpected hemorrhage complications in association with celecoxib. Spontaneously reported case series after perioperative pain treatment in gynecological operations].Fatty Acid Binding to the Allosteric Subunit of Cyclooxygenase-2 Relieves a Tonic Inhibition of the Catalytic Subunit.Toward the understanding of the molecular basis for the inhibition of COX-1 and COX-2 by phenolic compounds present in Uruguayan propolis and grape pomace.Discovery of a potent cyclooxygenase-2 inhibitor, S4, through docking-based pharmacophore screening, in vivo and in vitro estimations.

P2860

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P2860

Coxibs interfere with the action of aspirin by binding tightly to one monomer of cyclooxygenase-1

http://www.wikidata.org/entity/Q27658412

description

2010 nî lūn-bûn

@nan

2010 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2010 թվականի հունվարին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Coxibs interfere with the acti ...... ne monomer of cyclooxygenase-1

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Coxibs interfere with the acti ...... ne monomer of cyclooxygenase-1

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Coxibs interfere with the acti ...... ne monomer of cyclooxygenase-1

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Coxibs interfere with the acti ...... ne monomer of cyclooxygenase-1

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Coxibs interfere with the acti ...... ne monomer of cyclooxygenase-1

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Proceedings of the National Academy of Sciences of the United States of America

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Coxibs interfere with the acti ...... ne monomer of cyclooxygenase-1

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Benedict R Lucchesi

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Chong Yuan

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D Adam Lauver

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Gilad Rimon

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Jullia Y Lee

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Narayan P Sharma

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Ranjinder S Sidhu

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Raymond C Trievel

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Ryan A Frieler

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William L Smith

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P2860

Differential sensitivity and mechanism of inhibition of COX-2 oxygenation of arachidonic acid and 2-arachidonoylglycerol by ibuprofen and mefenamic acid

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids

PROCHECK: a program to check the stereochemical quality of protein structures

Processing of X-ray diffraction data collected in oscillation mode

The productive conformation of arachidonic acid bound to prostaglandin synthase

Structural basis of enantioselective inhibition of cyclooxygenase-1 by S-alpha-substituted indomethacin ethanolamides

Structural basis for selective inhibition of cyclooxygenase-2 by anti-inflammatory agents

Coot: model-building tools for molecular graphics

PRODRG: a tool for high-throughput crystallography of protein-ligand complexes

Likelihood-enhanced fast translation functions

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19955429

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