Evidence map›Paper›PMID 40243364›Full record

ArticlemBio2025

Lysine polyphosphate modifications contribute to virulence factors in

Kirsten Lehotsky, Nolan Neville, Isabella Martins, Keith Poole, Zongchao Jia

Erratum issuedAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in mBio, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Inorganic Polyphosphate and Human Diseases.Progress in molecular and subcellular biology · 2026
    Review
  4. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Kirsten LehotskyDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario, Canada.
Nolan NevilleDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario, Canada.
Isabella MartinsDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario, Canada.
Keith PooleDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario, Canada.
Zongchao JiaDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario, Canada.ORCID 0000-0002-9322-9394

Funding

Cystic Fibrosis CanadaNatural Sciences and Engineering Research Council of Canada
6 · The paper itself

Abstract

Inorganic polyphosphate (polyP) is a universally conserved polymer involved in various biological processes, but its role as a direct protein regulator remains largely unexplored. Lysine polyphosphate modification (KPM), a strong but non-covalent interaction between polyP and lysine-rich protein sequences, has not been functionally characterized until now. In this study, we present the first investigation into KPM's biological significance using

Indexed as

LysinePolyphosphatesPseudomonas aeruginosaVirulence FactorsBacterial ProteinsBiofilmsGene Expression Regulation, BacterialHumansOligopeptidesPyocyanineVirulenceBacterial ProteinsLysineOligopeptidesPolyphosphatesPyocyaninepyoverdinVirulence Factorsbiofilm formationEngA and SrmBlysine polyphosphate modificationlysine-rich motifPseudomonas aeruginosa virulence

Identifiers

PMID40243364
PMCPMC12077175

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.