ArticleNature communications2018
Mechanical architecture and folding of E. coli type 1 pilus domains.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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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.
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Who cites it
31 citing papers in PubMed, 68 citations in OpenAlex.
- Cell Adhesion and Biofilm Development via Force-Sensitive Mechanisms: A Perspective.ACS biomaterials science & engineering · 2026Review
- Protein-Protein Interactions as Promising Molecular Targets for Novel Antimicrobials Aimed at Gram-Negative Bacteria.International journal of molecular sciences · 2025Review
- Structures of the Escherichia coli type 1 pilus during pilus rod assembly and after assembly termination.Nature communications · 2025Article
- Mechanical forces and ligand binding modulateLife science alliance · 2025Article
- Biochemical characterization of theFrontiers in microbiology · 2025Article
- The strongest protein binder is surprisingly labile.Protein science : a publication of the Protein Society · 2024Article
- High-throughput virtual search of small molecules for controlling the mechanical stability of human CD4.The Journal of biological chemistry · 2024Article
- The polymer and materials science of the bacterial fimbriae Caf1.Biomaterials science · 2023Review
- Molecular mechanisms of catch bonds and their implications for platelet hemostasis.Biophysical reviews · 2023Review
- Binding site plasticity regulation of the FimH catch-bond mechanism.Biophysical journal · 2023Article
- Single-molecule mechanical studies of chaperones and their clients.Biophysics reviews · 2022Review
- Electron cryo-microscopy reveals the structure of the archaeal thread filament.Nature communications · 2022Article
- One-step asparaginyl endopeptidase (RSC chemical biology · 2022Article
- The Power of Touch: Type 4 Pili, the von Willebrand A Domain, and Surface Sensing by Pseudomonas aeruginosa.Journal of bacteriology · 2022Review
- A Single-Molecule Strategy to Capture Non-native Intramolecular and Intermolecular Protein Disulfide Bridges.Nano letters · 2022Article
- Unraveling the molecular determinants of the anti-phagocytic protein cloak of plague bacteria.PLoS pathogens · 2022Article
- Protein nanowires with tunable functionality and programmable self-assembly using sequence-controlled synthesis.Nature communications · 2022Article
- Article
- Emergence of ResistantFrontiers in microbiology · 2022Article
- DsbA is a redox-switchable mechanical chaperone.Chemical science · 2021Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
Abstract
Uropathogenic Escherichia coli attach to tissues using pili type 1. Each pilus is composed by thousands of coiled FimA domains followed by the domains of the tip fibrillum, FimF-FimG-FimH. The domains are linked by non-covalent β-strands that must resist mechanical forces during attachment. Here, we use single-molecule force spectroscopy to measure the mechanical contribution of each domain to the stability of the pilus and monitor the oxidative folding mechanism of a single Fim domain assisted by periplasmic FimC and the oxidoreductase DsbA. We demonstrate that pilus domains bear high mechanical stability following a hierarchy by which domains close to the tip are weaker than those close to or at the pilus rod. During folding, this remarkable stability is achieved by the intervention of DsbA that not only forms strategic disulfide bonds but also serves as a chaperone assisting the folding of the domains.
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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.