ArticleeLife2014
Reconstitution of bacterial autotransporter assembly using purified components.
Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 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
80 citing papers in PubMed.
- In vitro reconstitution implicates multiple OMP assembly factors in CdiAThe Journal of biological chemistry · 2026Article
- Cryo-EM structures of the SurA-BAM complex reveal conformational changes in outer membrane protein assembly.Nature communications · 2026Article
- Negative design enables cell-free expression and folding of designed transmembrane β-barrels.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Structures of folding intermediates on BAM show diverse substrates fold by a conserved mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Mechanism of phospholipid transport to the bacterial outer membrane by TAM.bioRxiv : the preprint server for biology · 2026Article
- Phospholipid composition strongly affects the assembly of β barrel proteins into purified bacterial outer membranes.Nature communications · 2026Article
- Structural basis of outer membrane biogenesis by the TamAB translocase.Nature communications · 2026Article
- Antibacterial macrocyclic peptides reveal a distinct mode of BamA inhibition.Nature communications · 2025Article
- Overproduction of β-barrel outer membrane proteins inExtracellular vesicles and circulating nucleic acids · 2025Article
- Article
- Native β-barrel substrates pass through two shared intermediates during folding on the BAM complex.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The discovery and structural basis of two distinct state-dependent inhibitors of BamA.Nature communications · 2024Article
- Outer membrane protein assembly mediated by BAM-SurA complexes.Nature communications · 2024Article
- Leptospira interrogans encodes a canonical BamA and three novel noNterm Omp85 outer membrane protein paralogs.Scientific reports · 2024Article
- The translocation assembly module (TAM) catalyzes the assembly of bacterial outer membrane proteins in vitro.Nature communications · 2024Article
- The translocation assembly module (TAM) catalyzes the assembly of bacterial outer membrane proteinsbioRxiv : the preprint server for biology · 2024Article
- Lateral gating mechanism and plasticity of the β-barrel assembly machinery complex in micelles andPNAS nexus · 2024Article
- Article
- In Vivo Disulfide-Bond Crosslinking to Study β-Barrel Membrane Protein Interactions, Dynamicity, and Folding Intermediates.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Monitoring the Interaction of the Peptidoglycan with the Bacterial β-Barrel Assembly Machinery.Methods in molecular biology (Clifton, N.J.) · 2024Article
20 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
3 authors.
Funding
Abstract
Autotransporters are a superfamily of bacterial virulence factors consisting of an N-terminal extracellular ('passenger') domain and a C-terminal β barrel ('β') domain that resides in the outer membrane (OM). The mechanism by which the passenger domain is secreted is poorly understood. Here we show that a conserved OM protein insertase (the Bam complex) and a molecular chaperone (SurA) are both necessary and sufficient to promote the complete assembly of the Escherichia coli O157:H7 autotransporter EspP in vitro. Our results indicate that the membrane integration of the β domain is the rate-limiting step in autotransporter assembly and that passenger domain translocation does not require the input of external energy. Furthermore, experiments using nanodiscs strongly suggest that autotransporter assembly is catalyzed by a single copy of the Bam complex. Finally, we describe a method to purify a highly active form of the Bam complex that should facilitate the elucidation of its function.
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.