Evidence map›Paper›PMID 41580080›Full record

ArticleThe Journal of biological chemistry2026

Bacteriocin biophysics: From protein-protein interaction models to navigators of the bacterial cell envelope.

Colin Kleanthous

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. NIR-Assisted Multimodal Strategies for Enhanced Antibacterial Therapy.Small (Weinheim an der Bergstrasse, Germany) · 2026
    Review
  2. Review
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 KleanthousDepartment of Biochemistry, University of Oxford, UK. Electronic address: colin.kleanthous@bioch.ox.ac.uk.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacteriocins are toxins deployed by bacteria to kill their competitors. Here, I reflect on my laboratory's work on protein bacteriocins and their immunity proteins from Gram-negative bacteria. We uncovered the structural and biophysical principles that underpin the 10-log stability range of protective immunity proteins for cytotoxic nuclease bacteriocins. We went on to elucidate how bacteriocins that kill Escherichia coli, Pseudomonas aeruginosa, and Klebsiella pneumoniae subvert outer membrane proteins and periplasmic energy transduction systems to drive their import. We leveraged our understanding of bacteriocin structure and function to probe the nature of the bacterial outer membrane. These studies revealed the outer membrane of E. coli to be an asymmetric proteolipid membrane, not an asymmetric lipid membrane as has been accepted dogma for the last 50 years. I contextualize the work with background on my career, collaborations, and academic leadership roles that influenced my development as a scientist.

Indexed as

BacteriocinsCell MembraneGram-Negative BacteriaBacterial Outer Membrane ProteinsBacterial Outer Membrane ProteinsBacteriocinsBacteriabacteriocincell envelopeimmunityimportouter membrane

Identifiers

PMID41580080
PMCPMC12927319

What OpenQuestion holds

Textmetadata
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.