ArticleThe Journal of biological chemistry2019
Alternative folding to a monomer or homopolymer is a common feature of the type 1 pilus subunit FimA from enteroinvasive bacteria.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Water, water, every where-the advent of hydrated pili structure.The FEBS journal · 2026Article
- Biological and structural characterization of the Type 3 fimbrial subunit MrkA from Klebsiella pneumoniae.Protein science : a publication of the Protein Society · 2025Article
- Article
- The assembly platform FimD is required to obtain the most stable quaternary structure of type 1 pili.Nature communications · 2024Article
- Zingerone inhibits biofilm formation and enhances antibiotic efficacy against Salmonella biofilm.World journal of microbiology & biotechnology · 2023Article
- Prophylaxis and Treatment againstInternational journal of molecular sciences · 2021Review
- Phosphorylation of Extracellular Proteins inFrontiers in microbiology · 2021Article
- Donor strand sequence, rather than donor strand orientation, determines the stability and non-equilibrium folding of the type 1 pilus subunit FimA.The Journal of biological chemistry · 2020Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Adhesive type 1 pili from enteroinvasive, Gram-negative bacteria mediate attachment to host cells. Up to 3000 copies of the main pilus subunit, FimA, assemble into the filamentous, helical quaternary structure of the pilus rod via a mechanism termed donor-strand complementation, in which the N-terminal extension of each subunit, the donor strand, is inserted into the incomplete immunoglobulin-like fold of the preceding FimA subunit. For FimA from
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Registered trials
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