ArticleNature communications2023
Assembly mechanism of a Tad secretion system secretin-pilotin complex.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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
15 citing papers in PubMed, 24 citations in OpenAlex.
- Article
- Structural insights into the assembly and evolution of a complex bacterial flagellar motor.Nature microbiology · 2026Article
- Article
- Unveiling the genetic landscape and motility-associated functions of Type IV pili in theMicrobiome research reports · 2026Article
- Recombinant TadZ from the type IVc pilus system induces protective immunity against virulentFrontiers in immunology · 2026Article
- Transcriptional profiling ofFrontiers in microbiology · 2026Article
- Article
- Electron Cryo-Tomography Reveals thebioRxiv : the preprint server for biology · 2025Article
- Structural insights into the secretin complex of a type IVb pilus system.Nature communications · 2025Article
- The structure of the Tad pilus alignment complex reveals a periplasmic conduit for pilus extension.Nature communications · 2025Article
- Conformational changes in the motor ATPase CpaF facilitate a rotary mechanism of Tad pilus assembly.Nature communications · 2025Article
- PilY1 regulates the dynamic architecture of the type IV pilus machine in Pseudomonas aeruginosa.Nature communications · 2024Article
- Bidirectional pilus processing in the Tad pilus system motor CpaF.Nature communications · 2024Article
- Article
- Membrane platform protein PulF of themBio · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
Abstract
The bacterial Tight adherence Secretion System (TadSS) assembles surface pili that drive cell adherence, biofilm formation and bacterial predation. The structure and mechanism of the TadSS is mostly unknown. This includes characterisation of the outer membrane secretin through which the pilus is channelled and recruitment of its pilotin. Here we investigate RcpA and TadD lipoprotein from Pseudomonas aeruginosa. Light microscopy reveals RcpA colocalising with TadD in P. aeruginosa and when heterologously expressed in Escherichia coli. We use cryogenic electron microscopy to determine how RcpA and TadD assemble a secretin channel with C13 and C14 symmetries. Despite low sequence homology, we show that TadD shares a similar fold to the type 4 pilus system pilotin PilF. We establish that the C-terminal four residues of RcpA bind TadD - an interaction essential for secretin formation. The binding mechanism between RcpA and TadD appears distinct from known secretin-pilotin pairings in other secretion systems.
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.