Evidence map›Paper›PMID 42840504›Full record

ArticleBiophysics and physicobiology2026

Structural basis for substrate specificity switching revealed by the FlhA(A489E) suppressor mutation.

Motoshi Sakai, Miki Kinoshita, Norihiro Takekawa, Keiichi Namba, Katsumi Imada, Tohru Minamino

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biophysics and physicobiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

6 authors.

Motoshi SakaiDepartment of Macromolecular Science, Graduate School of Science, The University of Osaka, Toyonaka, Osaka 560-0043, Japan.
Miki KinoshitaGraduate School of Frontier Biosciences, The University of Osaka, Suita, Osaka 565-0871, Japan.
Norihiro TakekawaDepartment of Macromolecular Science, Graduate School of Science, The University of Osaka, Toyonaka, Osaka 560-0043, Japan.
Keiichi NambaGraduate School of Frontier Biosciences, The University of Osaka, Suita, Osaka 565-0871, Japan.
Katsumi ImadaDepartment of Macromolecular Science, Graduate School of Science, The University of Osaka, Toyonaka, Osaka 560-0043, Japan.
Tohru MinaminoGraduate School of Frontier Biosciences, The University of Osaka, Suita, Osaka 565-0871, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The flagellar type III secretion system (fT3SS) switches its substrate specificity from hook-type to filament-type upon completion of hook assembly. This process is regulated by the coordinated actions of FliK, FlhB, and FlhA, but the structural mechanism underlying substrate specificity switching remains unclear. Here, we determined the crystal structures of the C-terminal cytoplasmic domain of FlhA(FlhA

Indexed as

AlphaFold3flagellar assemblysubstrate specificity switchingtype III secretion systemX-ray crystallography

Identifiers

PMID42840504
PMCPMC13639345

What OpenQuestion holds

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Registered trials

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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.