Evidence map›Paper›PMID 26565028›Full record

ArticleThe Journal of biological chemistry2016

A Revised Mechanism for Human Cyclooxygenase-2.

Yi Liu, Justine P Roth

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.4field-weighted citation impact, top 18% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

9 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Structural basis for endoperoxide-forming oxygenases.Beilstein journal of organic chemistry · 2022
    Review
  3. Article
  4. The enzymology of the human prostanoid pathway.Molecular biology reports · 2020
    Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Yi LiuFrom the Department of Chemistry, The Johns Hopkins University, Baltimore, Maryland 21218.
Justine P RothFrom the Department of Chemistry, The Johns Hopkins University, Baltimore, Maryland 21218 jproth@jhu.edu.
Johns Hopkins University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mechanism of ω-6 polyunsaturated fatty acid oxidation by wild-type cyclooxygenase 2 and the Y334F variant, lacking a conserved hydrogen bond to the catalytic tyrosyl radical/tyrosine, was examined for the first time under physiologically relevant conditions. The enzymes show apparent bimolecular rate constants and deuterium kinetic isotope effects that increase in proportion to co-substrate concentrations before converging to limiting values. The trends exclude multiple dioxygenase mechanisms as well as the proposal that initial hydrogen atom abstraction from the fatty acid is the first irreversible step in catalysis. Temperature dependent kinetic studies reinforce the novel finding that hydrogen transfer from the reduced catalytic tyrosine to a terminal peroxyl radical is the first irreversible step that controls regio- and stereospecific product formation.

Indexed as

Arachidonic AcidChromatography, High Pressure LiquidCyclooxygenase 2DeuteriumHumansKineticsLinoleic AcidMass SpectrometryMutant ProteinsOxidation-ReductionOxygen ConsumptionSolventsTemperatureViscosityArachidonic AcidCyclooxygenase 2DeuteriumLinoleic AcidMutant ProteinsSolventsdioxygenaseenzyme mechanismfatty acidisotope effectprostaglandin

Identifiers

PMID26565028
PMCPMC4705412
OpenAlexW2151674009

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.