Evidence map›Paper›PMID 42157495›Full record

ArticleBiophysical journal2026

Anurag Priyadarshi, Anne-Frances Miller

Abstract read
In one paragraph

Article in Biophysical journal, 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

2 authors.

Anurag PriyadarshiDepartment of Chemistry, University of Kentucky, Lexington, KY, USA.
Anne-Frances MillerDepartment of Chemistry, University of Kentucky, Lexington, KY, USA. Electronic address: afmill3r2@gmail.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bifurcating electron transfer flavoproteins (bETFs) accept a pair of modestly reducing electrons and produce a more potent electron carrier based on energy derived from favorable transfer of the other electron. A domain-scale conformational change is believed to gate electron transfer within the bETF, allowing only one electron to use the favorable path. 80° rotation of the so-called head domain carries the electron transfer flavin adenine dinucleotide (ET-FAD) from near the bifurcating FAD in bETF's closed conformation to a position >35 Å away in bETF's open conformation. In this, the ET-FAD is positioned to transfer electrons to partner proteins. Because conformation change is critical to bETF activity, understanding the motions and drivers of the conformational change is crucial to harnessing bifurcating enzymes for practical applications. After placing 5-

Indexed as

Electron-Transferring FlavoproteinsFluorineElectron TransportFlavin-Adenine DinucleotideMagnetic Resonance SpectroscopyModels, MolecularProtein ConformationTryptophanElectron-Transferring FlavoproteinsFlavin-Adenine DinucleotideFluorineTryptophan(19)F NMRconformational ensembleelectron transfer flavoproteinparamagnetic relaxation enhancement

Identifiers

PMID42157495
PMCPMC13507390

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.