Evidence map›Paper›PMID 42117458›Full record

ReviewBiochemistry2026

Keeping Wavering Bonds: Deactivation-Induced Signaling by Reactive Electrophiles.

Marcus J C Long, Yaren Karakoç, Yimon Aye

Abstract readReview
In one paragraph

Review in Biochemistry, 2026. 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

3 authors.

Marcus J C LongDepartment of Chemistry, University of Oxford, Oxford OX1 3TA, U.K.
Yaren KarakoçDepartment of Chemistry, University of Oxford, Oxford OX1 3TA, U.K.
Yimon AyeDepartment of Chemistry, University of Oxford, Oxford OX1 3TA, U.K.ORCID 0000-0002-1256-4159

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Discovered ∼60years ago, the lipid metabolite 4-hydroxynonenal (HNE) is linked to a plethora of macromolecular targets and biological functions. For a molecule that weighs 156 Da and possesses a single H-bond donor, this is quite a feat. Despite its chemical simplicity, HNE contains an α,β-unsaturated aldehyde system, endowing it with the capability to react covalently with numerous biological functional groups and bestowing on it pleiotropic properties. Regardless of the specific entity engaging with HNE, it is covalent bond formation that has dominated thought on HNE behavior. Indeed, cells possess a flurry of detoxifying enzymes that convert HNE to less reactive chemicals lacking the α,β-unsaturated aldehyde. For instance, the cell can either reduce or oxidize the aldehyde within HNE, deactivating HNE's chemical reactivity. Here, we discuss one of our recent papers that discovered that HNE can modify the detoxification enzyme, Cyp-33e1, in

Indexed as

AldehydesCytochrome P-450 Enzyme SystemSignal TransductionAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsHumansOxidation-Reduction4-hydroxy-2-nonenalAldehydesCaenorhabditis elegans ProteinsCytochrome P-450 Enzyme System

Identifiers

PMID42117458
PMCPMC13235545

What OpenQuestion holds

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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.