ArticleThe Journal of biological chemistry2018
Archaic and alternative chaperones preserve pilin folding energy by providing incomplete structural information.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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.
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
8 citing papers in PubMed, 8 citations in OpenAlex.
- Should I stay or should I go? DNA damage thresholds drive stay-or-go decisions inJournal of bacteriology · 2026Review
- Antiparallel stacking of Csu pili drives Acinetobacter baumannii 3D biofilm assembly.Nature communications · 2026Article
- FimC binds to the promoter region ofFrontiers in cellular and infection microbiology · 2025Article
- Csu pili dependent biofilm formation and virulence of Acinetobacter baumannii.NPJ biofilms and microbiomes · 2023Article
- Stochastic chain termination in bacterial pilus assembly.Nature communications · 2023Article
- Urinary Tract Infections Caused by UropathogenicInternational journal of molecular sciences · 2023Review
- Article
- Classical chaperone-usher (CU) adhesive fimbriome: uropathogenic Escherichia coli (UPEC) and urinary tract infections (UTIs).Folia microbiologica · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
Adhesive pili are external component of fibrous adhesive organelles and help bacteria attach to biotic or abiotic surfaces. The biogenesis of adhesive pili via the chaperone-usher pathway (CUP) is independent of external energy sources. In the classical CUP, chaperones transport assembly-competent pilins in a folded but expanded conformation. During donor-strand exchange, pilins subsequently collapse, producing a tightly packed hydrophobic core and releasing the necessary free energy to drive fiber formation. Here, we show that pilus biogenesis in non-classical, archaic, and alternative CUPs uses a different source of conformational energy. High-resolution structures of the archaic Csu-pili system from
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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.