ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010
A conserved fold for fimbrial components revealed by the crystal structure of a putative fimbrial assembly protein (BT1062) from Bacteroides thetaiotaomicron at 2.2 Å resolution.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed, 9 citations in OpenAlex.
- Diversity analysis of genes encoding Mfa1 fimbrial components in Porphyromonas gingivalis strains.PloS one · 2021Article
- Genome-wide screens identify Toxoplasma gondii determinants of parasite fitness in IFNγ-activated murine macrophages.Nature communications · 2020Article
- A comprehensive guide to pilus biogenesis in Gram-negative bacteria.Nature reviews. Microbiology · 2017Review
- Article
- Molecular characterization of novel pyridoxal-5'-phosphate-dependent enzymes from the human microbiome.Protein science : a publication of the Protein Society · 2014Article
- Structure of the pilus assembly protein TadZ from Eubacterium rectale: implications for polar localization.Molecular microbiology · 2012Article
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Authors and funding
51 authors at 7 institutions in 1 country.
Funding
Abstract
BT1062 from Bacteroides thetaiotaomicron is a homolog of Mfa2 (PGN0288 or PG0179), which is a component of the minor fimbriae in Porphyromonas gingivalis. The crystal structure of BT1062 revealed a conserved fold that is widely adopted by fimbrial components.
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