ArticleNature communications2016
Structure of the Neisseria meningitidis Type IV pilus.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 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
85 citing papers in PubMed, 146 citations in OpenAlex.
- The role of extracellular DNA inJournal of bacteriology · 2026Review
- Structures of the Xcp and Hxc T2SS endopili provide new insights into type IV pili subfamilies.Structure (London, England : 1993) · 2026Article
- Visualization of Type IV Pili: Linking Structural Architecture, Dynamic Function, and Translational Opportunities.Biology · 2026Review
- Ultrastructural and atomic characterization of biofilm-associated extracellular filaments in Shewanella oneidensis MR-1.Nature communications · 2026Article
- Article
- Structural insights into the secretin complex of a type IVb pilus system.Nature communications · 2025Article
- Integrative Structure and Function of thebioRxiv : the preprint server for biology · 2025Article
- Article
- The molecular basis for DNA-binding by competence T4P is distinct in a representative Gram-positive and Gram-negative species.PLoS pathogens · 2025Article
- Unusual cell surfaces, pili, and archaella of Thermoplasmatales archaea.The ISME journal · 2025Article
- Structure of the Pseudomonas aeruginosa PAO1 Type IV pilus.PLoS pathogens · 2024Article
- Functional Analysis of the Major Pilin Proteins of Type IV Pili inInternational journal of molecular sciences · 2024Article
- Tight-packing of large pilin subunits provides distinct structural and mechanical properties for theProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Cryo-EM structures of type IV pili complexed with nanobodies reveal immune escape mechanisms.Nature communications · 2024Article
- Article
- Structure and Dynamics of Type 4a Pili and Type 2 Secretion System Endopili.Sub-cellular biochemistry · 2024Review
- Tad and toxin-coregulated pilus structures reveal unexpected diversity in bacterial type IV pili.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structure of a heteropolymeric type 4 pilus from a monoderm bacterium.Nature communications · 2023Article
- Genetic variants linked to the phenotypic outcome of invasive disease and carriage ofMicrobial genomics · 2023Article
- Blocking bacterial appendage attachment to wastewater treatment membranes using anti-adhesins.Chemosphere · 2023Article
25 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 4 institutions in 3 countries.
Funding
Abstract
Neisseria meningitidis use Type IV pili (T4P) to adhere to endothelial cells and breach the blood brain barrier, causing cause fatal meningitis. T4P are multifunctional polymers of the major pilin protein, which share a conserved hydrophobic N terminus that is a curved extended α-helix, α1, in X-ray crystal structures. Here we report a 1.44 Å crystal structure of the N. meningitidis major pilin PilE and a ∼6 Å cryo-electron microscopy reconstruction of the intact pilus, from which we built an atomic model for the filament. This structure reveals the molecular arrangement of the N-terminal α-helices in the filament core, including a melted central portion of α1 and a bridge of electron density consistent with a predicted salt bridge necessary for pilus assembly. This structure has important implications for understanding pilus biology.
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.