Evidence map›Paper›PMID 28363790›Full record

ArticleBiochimica et biophysica acta. Molecular and cell biology of lipids2017

A fungal catalase reacts selectively with the 13S fatty acid hydroperoxide products of the adjacent lipoxygenase gene and exhibits 13S-hydroperoxide-dependent peroxidase activity.

Tarvi Teder, William E Boeglin, Claus Schneider, Alan R Brash

Abstract read
In one paragraph

Article in Biochimica et biophysica acta. Molecular and cell biology of lipids, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

6 citing papers in PubMed, 15 citations in OpenAlex.

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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

4 authors at 1 institution in 1 country.

Tarvi TederDepartment of Pharmacology and the Vanderbilt Institute of Chemical Biology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA. Electronic address: tarvi.teder@ttu.ee.
William E BoeglinDepartment of Pharmacology and the Vanderbilt Institute of Chemical Biology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA. Electronic address: william.boeglin@vanderbilt.edu.
Claus SchneiderDepartment of Pharmacology and the Vanderbilt Institute of Chemical Biology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA. Electronic address: claus.schneider@vanderbilt.edu.
Alan R BrashDepartment of Pharmacology and the Vanderbilt Institute of Chemical Biology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA. Electronic address: alan.brash@vanderbilt.edu.
Vanderbilt University · US

Funding

THE PHARMACOLOGY OF INHIBITORS OF HEME PROTEIN-CATALYZED LIPID PEROXIDATIONP50GM015431 · NIGMS · VANDERBILT UNIVERSITY · PI CAPRIOLI, RICHARD M · 1985 to 2010
$15.0M
Therapeutic Modulation of Endothelial Cell TetrahydrobiopterinP01GM015431 · NIGMS · VANDERBILT UNIVERSITY · PI MARNETT, LAWRENCE J. · 2011 to 2015
$9.5M
Convergence of the COX-2 and 5-lipoxygenase pathwaysR01GM076592 · NIGMS · VANDERBILT UNIVERSITY · PI SCHNEIDER, CLAUS · 2007 to 2021
$4.0M
Novel Catalases and their ProductsR01GM074888 · NIGMS · VANDERBILT UNIVERSITY · PI BRASH, ALAN R. · 2006 to 2013
$2.4M
NIGMS NIH HHS P01 GM015431NIGMS NIH HHS P50 GM015431NIGMS NIH HHS R01 GM074888NIGMS NIH HHS R01 GM076592
6 · The paper itself

Abstract

The genome of the fungal plant pathogen Fusarium graminearum harbors six catalases, one of which has the sequence characteristics of a fatty acid peroxide-metabolizing catalase. We cloned and expressed this hemoprotein (designated as Fg-cat) along with its immediate neighbor, a 13S-lipoxygenase (cf. Brodhun et al., PloS One, e64919, 2013) that we considered might supply a fatty acid hydroperoxide substrate. Indeed, Fg-cat reacts abruptly with the 13S-hydroperoxide of linoleic acid (13S-HPODE) with an initial rate of 700-1300s

Indexed as

CatalaseCyclopentanesFatty AcidsFungal ProteinsHydrogen PeroxideIntramolecular OxidoreductasesLinoleic AcidLipid PeroxidesLipoxygenaseOleic AcidsOxidation-ReductionOxylipinsPeroxidaseStereoisomerismtert-ButylhydroperoxideYeasts13-lipoxygenase13-octadecenoic acidCatalaseCyclopentanesFatty AcidsFungal ProteinsHydrogen Peroxidehydroperoxide isomeraseIntramolecular Oxidoreductasesjasmonic acidLinoleic AcidLipid PeroxidesLipoxygenaseOleic AcidsOxylipinsPeroxidasetert-ButylhydroperoxideABTS assayCatalaseFusariumHPODELipoxygenaseNMRPeroxidase

Identifiers

PMID28363790
PMCPMC5481161
OpenAlexW2602396989

What OpenQuestion holds

Textmetadata
LicenceTDM
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.