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Structural studies of cilia and flagella associated protein 410 (CFAP410) reveal its bimodular organization with an N-terminal LRR motif and a C-terminal tetrameric helical bundle | bioRxiv
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Emerging insights into the complex genetics and pathophysiology of amyotrophic lateral sclerosis - The Lancet Neurology
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Structural studies of cilia and flagella associated protein 410 (CFAP410) reveal its bimodular organization with an N-terminal LRR motif and a C-terminal tetrameric helical bundle | bioRxiv
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Frontiers | Pathogenicity and functional analysis of CFAP410 mutations causing cone-rod dystrophy with macular staphyloma
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FIGURE The CFAP VNTR shows promoter activity in the pGLL-B vector in... | Download Scientific Diagram
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Structural studies of cilia and flagella associated protein 410 (CFAP410) reveal its bimodular organization with an N-terminal LRR motif and a C-terminal tetrameric helical bundle | bioRxiv
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Frontiers | Pathogenicity and functional analysis of CFAP410 mutations causing cone-rod dystrophy with macular staphyloma
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Frontiers | Pathogenicity and functional analysis of CFAP410 mutations causing cone-rod dystrophy with macular staphyloma
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A polymorphic transcriptional regulatory domain in the amyotrophic lateral sclerosis risk gene CFAP410 correlates with differential isoform expression - Frontiers
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