ArticleBiopolymers2024
The basal and major pilins in the Corynebacterium diphtheriae SpaA pilus adopt similar structures that competitively react with the pilin polymerase.
Article in Biopolymers, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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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.
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Who cites it
4 citing papers in PubMed, 7 citations in OpenAlex.
- Analysis of novel zinc-binding proteins in the cell wall ofJournal of bacteriology · 2025Article
- Intracellular invasion potential and pathogenic effects ofFrontiers in microbiology · 2025Article
- Article
- Structural and functional insights of sortases and their interactions with antivirulence compounds.Current research in structural biology · 2024Review
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10 authors at 1 institution in 1 country.
Funding
Abstract
Many species of pathogenic gram-positive bacteria display covalently crosslinked protein polymers (called pili or fimbriae) that mediate microbial adhesion to host tissues. These structures are assembled by pilus-specific sortase enzymes that join the pilin components together via lysine-isopeptide bonds. The archetypal SpaA pilus from Corynebacterium diphtheriae is built by the
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Registered trials
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