ArticleScience (New York, N.Y.)2013
Intrinsically disordered protein threads through the bacterial outer-membrane porin OmpF.
Article in Science (New York, N.Y.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 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
71 citing papers in PubMed, 120 citations in OpenAlex.
- In vitro reconstitution implicates multiple OMP assembly factors in CdiAThe Journal of biological chemistry · 2026Article
- Structural basis of outer membrane biogenesis and cell division by Tol/Pal nanomachinery.Science advances · 2026Article
- Bacteriocin biophysics: From protein-protein interaction models to navigators of the bacterial cell envelope.The Journal of biological chemistry · 2026Article
- Architecture and conformational dynamics of the BAM-SurA holo insertase complex.Science advances · 2025Article
- The potential of bacteriocins and bacteriophages to control bacterial disease of crops with a focus onJournal of the Royal Society of New Zealand · 2025Review
- Structural constraints of pyocin S2 import through the ferripyoverdine receptor FpvAI.PNAS nexus · 2024Article
- Tunable force transduction through theProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Envelope-Stress Sensing Mechanism of Rcs and Cpx Signaling Pathways in Gram-Negative Bacteria.Journal of microbiology (Seoul, Korea) · 2023Review
- Conformational rearrangements in the sensory RcsF/OMP complex mediate signal transduction across the bacterial cell envelope.PLoS genetics · 2023Article
- Lipids mediate supramolecular outer membrane protein assembly in bacteria.Science advances · 2022Article
- Proteolytic processing induces a conformational switch required for antibacterial toxin delivery.Nature communications · 2022Article
- The Ankyrin Repeat Protein RARP-1 Is a Periplasmic Factor That SupportsJournal of bacteriology · 2022Article
- Colicin E1 opens its hinge to plug TolC.eLife · 2022Article
- High-Throughput Native Mass Spectrometry Screening in Drug Discovery.Frontiers in molecular biosciences · 2022Review
- Porin threading drives receptor disengagement and establishes active colicin transport through Escherichia coli OmpF.The EMBO journal · 2021Article
- Deciphering Microbial Metal Toxicity Responses via Random Bar Code Transposon Site Sequencing and Activity-Based Metabolomics.Applied and environmental microbiology · 2021Article
- Entropy-driven translocation of disordered proteins through the Gram-positive bacterial cell wall.Nature microbiology · 2021Article
- Toxin import through the antibiotic efflux channel TolC.Nature communications · 2021Article
- Contact-independent killing mediated by a T6SS effector with intrinsic cell-entry properties.Nature communications · 2021Article
- Article
11 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
11 authors at 2 institutions in 1 country.
Funding
Abstract
Porins are β-barrel outer-membrane proteins through which small solutes and metabolites diffuse that are also exploited during cell death. We have studied how the bacteriocin colicin E9 (ColE9) assembles a cytotoxic translocon at the surface of Escherichia coli that incorporates the trimeric porin OmpF. Formation of the translocon involved ColE9's unstructured N-terminal domain threading in opposite directions through two OmpF subunits, capturing its target TolB on the other side of the membrane in a fixed orientation that triggers colicin import. Thus, an intrinsically disordered protein can tunnel through the narrow pores of an oligomeric porin to deliver an epitope signal to the cell to initiate cell death.
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.