Evidence map›Paper›PMID 38698065›Full record

ArticleScientific reports2024

Discovery of active mouse, plant and fungal cytochrome P450s in endogenous proteomes and upon expression in planta.

Maria Font-Farre, Daniel Brown, Reka Toth, Chidambareswaren Mahadevan, Melissa Brazier-Hicks, Kyoko Morimoto, Farnusch Kaschani, John Sinclair, Richard Dale, Samantha Hall and 5 more

Abstract read
In one paragraph

Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

15 authors.

Maria Font-FarreThe Plant Chemetics Laboratory, Department of Biology, University of Oxford, Oxford, UK.
Daniel BrownChemistry Research Laboratory, Department of Chemistry, University of Oxford, Oxford, UK.
Reka TothDepartment of Biology, University of Oxford, Oxford, UK.
Chidambareswaren MahadevanThe Plant Chemetics Laboratory, Department of Biology, University of Oxford, Oxford, UK.
Melissa Brazier-HicksBioscience, Syngenta, Jealotts Hill International Research Centre, Bracknell, UK.
Kyoko MorimotoThe Plant Chemetics Laboratory, Department of Biology, University of Oxford, Oxford, UK.
Farnusch KaschaniZMB Chemical Biology, Faculty of Biology, University of Duisburg-Essen, Essen, Germany.
John SinclairBioscience, Syngenta, Jealotts Hill International Research Centre, Bracknell, UK.
Richard DaleBioscience, Syngenta, Jealotts Hill International Research Centre, Bracknell, UK.
Samantha HallBioscience, Syngenta, Jealotts Hill International Research Centre, Bracknell, UK.
Melloney MorrisBioscience, Syngenta, Jealotts Hill International Research Centre, Bracknell, UK.
Markus KaiserZMB Chemical Biology, Faculty of Biology, University of Duisburg-Essen, Essen, Germany.
Aaron T WrightDepartment of Biology, Baylor University, Waco, TX, USA.
Jonathan BurtonChemistry Research Laboratory, Department of Chemistry, University of Oxford, Oxford, UK.
Renier A L van der HoornThe Plant Chemetics Laboratory, Department of Biology, University of Oxford, Oxford, UK. renier.vanderhoorn@biology.ox.ac.uk.

Funding

Biotechnology and Biological Sciences Research Council DDT00060European Research Council 101019324European Research Council 616449
6 · The paper itself

Abstract

Eukaryotes produce a large number of cytochrome P450s that mediate the synthesis and degradation of diverse endogenous and exogenous metabolites. Yet, most of these P450s are uncharacterized and global tools to study these challenging, membrane-resident enzymes remain to be exploited. Here, we applied activity profiling of plant, mouse and fungal P450s with chemical probes that become reactive when oxidized by P450 enzymes. Identification by mass spectrometry revealed labeling of a wide range of active P450s, including six plant P450s, 40 mouse P450s and 13 P450s of the fungal wheat pathogen Zymoseptoria tritici. We next used transient expression of GFP-tagged P450s by agroinfiltration to show ER-targeting and NADPH-dependent, activity-based labeling of plant, mouse and fungal P450s. Both global profiling and transient expression can be used to detect a broad range of active P450s to study e.g. their regulation and discover selective inhibitors.

Indexed as

Cytochrome P-450 Enzyme SystemFungal ProteinsProteomeAnimalsAscomycotaMicePlant ProteinsCytochrome P-450 Enzyme SystemFungal ProteinsPlant ProteinsProteomeActivity-based labelingAgroinfiltrationCytochrome P450HerbicideProteomics

Identifiers

PMID38698065
PMCPMC11066006

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Registered trials

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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.