Evidence map›Paper›PMID 40024995›Full record

ArticleJournal of biomolecular NMR2025

Counterintuitive method improves yields of isotopically labelled proteins expressed in flask-cultured Escherichia coli.

Miguel Ángel Treviño

Abstract read
In one paragraph

Article in Journal of biomolecular NMR, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. In sample pH measurement byEuropean biophysics journal : EBJ · 2026
    Article
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.

Miguel Ángel TreviñoInstituto de Química Física Blas Cabrera, Consejo Superior de Investigaciones Científicas, Serrano 119, Madrid, Spain. mtrevino@iqf.csic.es.ORCID http://orcid.org/0000-0002-0738-5973

Funding

MCIN/AEI/10.13039/501100011033 PID2020-112821GB-I00
6 · The paper itself

Abstract

NMR is a powerful tool for the structural and dynamic study of proteins. One of the necessary conditions for the study of these proteins is their isotopic labelling with

Indexed as

Escherichia coliIsotope LabelingNuclear Magnetic Resonance, BiomolecularCarbon IsotopesGlucoseNitrogen IsotopesRecombinant ProteinsCarbon IsotopesGlucoseNitrogen IsotopesRecombinant Proteins13C labellingCost reductionGlucose consumptionMinimal active timeProtein expression

Identifiers

PMID40024995
PMCPMC12078410

What OpenQuestion holds

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LicenceCC BY
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.