Evidence map›Paper›PMID 40980994›Full record

ArticleProtein science : a publication of the Protein Society2025

Structural insights into the Pseudomonas aeruginosa ClpP1•ClpP2 heterocomplex and its interactions with the AAA+ ClpX unfoldase.

Alireza Ghanbarpour, Jia Jia Zhang, Joseph H Davis, Tania A Baker, Robert T Sauer

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. ClpP2 modulates ClpXP assembly to promote multiple pathogenic phenotypes inProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Characterization ofVeterinary sciences · 2026
    Article
  3. 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

5 authors.

Alireza GhanbarpourDepartment of Biochemistry and Molecular Biophysics, Washington University in St. Louis, St. Louis, Missouri, USA.ORCID 0000-0002-7485-029X
Jia Jia ZhangDepartment of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.
Joseph H DavisDepartment of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.
Tania A BakerDepartment of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.
Robert T SauerDepartment of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.ORCID 0000-0002-1719-5399

Funding

Tools to determine and analyze the structures of molecular machines in motionR01GM144542 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI Joseph Davis · 2022 to 2026
$1.6M
Structure and function of ClpXPR35GM141517 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SAUER, ROBERT T · 2021 to 2024
$1.5M
Decoding Mitochondrial AAA Protease SpecificityR35GM160328 · NIGMS · WASHINGTON UNIVERSITY · PI Alireza Ghanbarpour · 2025 to 2026
$808k
Department of Biochemistry and Molecular Biophysics at Washington University School of MedicineNIGMS NIH HHS R01 GM144542NIGMS NIH HHS R35 GM141517NIGMS NIH HHS R35 GM160328NIH HHS R01-GM144542NIH HHS R35-GM141517NIH HHS R35GM160328NSF-CAREER 2046778
6 · The paper itself

Abstract

ClpXP and other AAA+ proteases play central roles in bacterial proteostasis by degrading misfolded and regulatory proteins. In Pseudomonas aeruginosa, ClpXP consists of the ClpX unfoldase and ClpP peptidase, which influence critical adaptive processes contributing to stress resistance. P. aeruginosa

Indexed as

Bacterial ProteinsEndopeptidase ClpPseudomonas aeruginosaCryoelectron MicroscopyCrystallography, X-RayModels, MolecularProtein BindingProtein ConformationSerine EndopeptidasesBacterial ProteinsClpP2 protein, bacteriaEndopeptidase ClpSerine Endopeptidasesmolecular machines in pathogensproteolytic activationproteostasis regulation

Identifiers

PMID40980994
PMCPMC12451819

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.