ArticleNature communications2026
Near-atomic in situ architecture and membrane-coupled dynamics of the Vibrio cholerae sheathed flagellum.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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.
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.
Who cites it
1 citing paper in PubMed.
- Integrating in situ single-particle cryo-electron microscopy with cryo-electron tomography for high-resolution structural biology in native cellular contexts.Current opinion in structural biology · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors.
Funding
Abstract
The sheathed flagellum of Vibrio cholerae is a self-assembling membranous organelle that coordinates flagellar assembly, sheath biogenesis, and rapid rotation. Here, we determine in-situ near-atomic structures of the sheathed flagellar motor within intact cells. The motor anchors to the outer membrane through lipidated HL-rings without forming a membrane pore, thereby enabling flagellar assembly to drive sheath formation. Conserved LP-rings function as slide-rotary bushings, permitting high-speed rotation within the bacterial envelope while retaining the ability to constrict and seal the lumen upon flagellar ejection. We further show that stator activation depends on a specific protein-protein interaction rather than peptidoglycan engagement. Together, these findings reveal how the distinctive architecture and dynamics of the sheathed flagellum support V. cholerae motility, environmental survival, and persistent colonization of the human gut.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.