Evidence map›Paper›PMID 41312160›Full record

ReviewmicroLife2025

Functional diversity and molecular interactions of small membrane proteins in bacteria.

Jing Yuan, Hans-Georg Koch, Bork A Berghoff

Abstract readReview
In one paragraph

Review in microLife, 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. 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

3 authors.

Jing YuanMax Planck Institute for Terrestrial Microbiology, 35043 Marburg, Germany.ORCID https://orcid.org/0000-0003-1219-3316
Hans-Georg KochInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, Albert-Ludwigs University Freiburg, 79104 Freiburg, Germany.ORCID https://orcid.org/0000-0001-5913-0334
Bork A BerghoffInstitute of Molecular Biology and Biotechnology of Prokaryotes, University of Ulm, 89069 Ulm, Germany.ORCID https://orcid.org/0000-0002-6299-419X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacteria constantly adapt to changing environmental conditions through diverse processes that involve numerous regulator and effector proteins. In this regard, small proteins play a significant role in promoting stress adaptation in bacteria. Although they were largely overlooked in early genome annotations, recent technological advances and a growing recognition of their significance have paved the way for the increasing identification and characterization of this intriguing class of proteins. Many small proteins contain a transmembrane domain and are integral to the cytoplasmic membrane. Others interact with and modulate membrane protein complexes. In this review, we focus on the current knowledge of these small membrane proteins, with an emphasis on their interactions, membrane insertion pathways, and toxicity.

Indexed as

membrane insertionrespiratory complexessensor kinasessmall membrane proteinstoxin-antitoxin systems

Identifiers

PMID41312160
PMCPMC12648545

What OpenQuestion holds

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LicenceCC BY-NC
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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.