ArticleNature structural & molecular biology2011
Common architecture of the flagellar type III protein export apparatus and F- and V-type ATPases.
Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 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
95 citing papers in PubMed.
- Review
- Article
- Uncoupling substrate delivery from export gate activation reveals distinct roles of the flagellar ATPase complex.Frontiers in microbiology · 2026Article
- Continuous exchange of an inner-membrane ring component is required for assembly and function of the type III secretion system.Nature communications · 2025Article
- Dimeric assembly of FScience advances · 2025Article
- Viscosity-dependent determinants ofmBio · 2024Article
- Structure, Assembly, and Function of Flagella Responsible for Bacterial Locomotion.EcoSal Plus · 2023Review
- Parallel genetic adaptation ofMicrobial genomics · 2023Article
- Virulence-associated type III secretion systems in Gram-negative bacteria.Microbiology (Reading, England) · 2023Review
- Orf1B controls secretion of T3SS proteins and contributes to Edwardsiella piscicida adhesion to epithelial cells.Veterinary research · 2022Article
- Insight Into Distinct Functional Roles of the Flagellar ATPase Complex for Flagellar Assembly inFrontiers in microbiology · 2022Review
- Activation mechanism of the bacterial flagellar dual-fuel protein export engine.Biophysics and physicobiology · 2022Article
- Structural and Functional Analysis of SsaV Cytoplasmic Domain and Variable Linker States in the Context of the InvA-SsaV Chimeric Protein.Microbiology spectrum · 2021Article
- Bacterial Flagellar Filament: A Supramolecular Multifunctional Nanostructure.International journal of molecular sciences · 2021Review
- Membrane voltage-dependent activation mechanism of the bacterial flagellar protein export apparatus.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The holobiont transcriptome of teneral tsetse fly species of varying vector competence.BMC genomics · 2021Article
- A positive charge region of Salmonella FliI is required for ATPase formation and efficient flagellar protein export.Communications biology · 2021Article
- Protein Export via the Type III Secretion System of the Bacterial Flagellum.Biomolecules · 2021Review
- Architecture and Assembly of the Bacterial Flagellar Motor Complex.Sub-cellular biochemistry · 2021Review
- The PopN Gate-keeper Complex Acts on the ATPase PscN to Regulate the T3SS Secretion Switch from Early to Middle Substrates in Pseudomonas aeruginosa.Journal of molecular biology · 2020Article
35 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.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The proteins that form the bacterial flagellum are translocated to its distal end through the central channel of the growing flagellum by the flagellar-specific protein export apparatus, a family of the type III protein secretion system. FliI and FliJ are soluble components of this apparatus. FliI is an ATPase that has extensive structural similarity to the α and β subunits of F(o)F(1)-ATP synthase. FliJ is essential for export, but its function remains obscure. Here we show that the structure of FliJ derived from Salmonella enterica serovar Typhimurium is remarkably similar to that of the two-stranded α-helical coiled-coil part of the γ subunit of F(o)F(1)-ATP synthase and that FliJ promotes the formation of FliI hexamer rings by binding to the center of the ring. These results suggest that the type III protein export system and F- and V-type ATPases share a similar mechanism and an evolutionary relationship.
Indexed as
Identifiers
21278755What 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.