ArticleOpen biology2024
The C-terminus of CFAP410 forms a tetrameric helical bundle that is essential for its localization to the basal body.
Article in Open biology, 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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Who cites it
4 citing papers in PubMed.
- Genome-Wide Analysis of DNA Methylation Profiles on Jining Grey Goat Uterus Associated with Prolificacy Using Whole-Genome Bisulfite Sequencing.Animals : an open access journal from MDPI · 2026Article
- Functional variants of CFAP410 affect the DNA damage response leading to motor neuron degeneration - Implications for ALS.iScience · 2025Article
- CFAP410 has a bimodular architecture with a conserved surface patch on its N-terminal leucine-rich repeat motif for binding interaction partners.Frontiers in cell and developmental biology · 2025Article
- Editorial: Advances in cilia and flagella research.Frontiers in cell and developmental biology · 2025Article
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10 authors.
Funding
Abstract
Cilia are antenna-like organelles protruding from the surface of many cell types in the human body. Defects in ciliary structure or function often lead to diseases that are collectively called ciliopathies. Cilia and flagella-associated protein 410 (CFAP410) localizes at the basal body of cilia/flagella and plays essential roles in ciliogenesis, neuronal development and DNA damage repair. It remains unknown how its specific basal body location is achieved. Multiple single amino acid mutations in CFAP410 have been identified in patients with various ciliopathies. One of the mutations, L224P, is located in the C-terminal domain (CTD) of human CFAP410 and causes severe spondylometaphyseal dysplasia, axial (SMDAX). However, the molecular mechanism for how the mutation causes the disorder remains unclear. Here, we report our structural studies on the CTD of CFAP410 from three distantly related organisms,
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