Evidence map›Paper›PMID 39838014›Full record

ReviewReviews of physiology, biochemistry and pharmacology2025

Making Proteins with Electricity.

Colin D McCaig

Abstract readReview
PubMed Publisher
In one paragraph

Review in Reviews of physiology, biochemistry and pharmacology, 2025. 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

1 author.

Colin D McCaigInstitute of Medical Sciences, University of Aberdeen, Aberdeen, Scotland, UK.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribosomes use multiple electrical forces to regulate new protein construction, to ensure efficient protein cotranslation, chaperoning, and folding. When these electrical regulatory forces are disrupted as in point charge mutations, specific disease occurs from aberrantly folded proteins. α1 antitrypsin deficiency is perhaps the best-known misfolded protein disease and is covered in some detail.

Indexed as

ProteinsRibosomesalpha 1-Antitrypsinalpha 1-Antitrypsin DeficiencyAnimalsElectricityHumansProtein Foldingalpha 1-AntitrypsinProteinsChaperoneMagnesium sensingNascent chainsProteinProtein foldingProtein translationRibosomeTrigger factor

Identifiers

PMID39838014

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.