ArticleInternational journal of molecular sciences2022
Orientational Preferences of GPI-Anchored Ly6/uPAR Proteins.
Article in International journal of molecular sciences, 2022. 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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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
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- Exploring the molecular function of LYPD3 from pan-cancer to lung cancer: based on bioinformatics and cellular experiments.Mammalian genome : official journal of the International Mammalian Genome Society · 2026Article
- In Search of the Role of Three-Finger Starfish Proteins.Marine drugs · 2024Article
- Towards the Identification of New Biomarkers in Saliva and Serum for Treatment Monitoring of Equine Gastric Ulcer Syndrome: A Liquid Proteomic Approach.Animals : an open access journal from MDPI · 2024Article
- A novel anxiety-associated SNP identified inFrontiers in behavioral neuroscience · 2024Article
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
Abstract
Ly6/uPAR proteins regulate many essential functions in the nervous and immune systems and epithelium. Most of these proteins contain single β-structural LU domains with three protruding loops and are glycosylphosphatidylinositol (GPI)-anchored to a membrane. The GPI-anchor role is currently poorly studied. Here, we investigated the positional and orientational preferences of six GPI-anchored proteins in the receptor-unbound state by molecular dynamics simulations. Regardless of the linker length between the LU domain and GPI-anchor, the proteins interacted with the membrane by polypeptide parts and N-/O-glycans. Lynx1, Lynx2, Lypd6B, and Ly6H contacted the membrane by the loop regions responsible for interactions with nicotinic acetylcholine receptors, while Lypd6 and CD59 demonstrated unique orientations with accessible receptor-binding sites. Thus, GPI-anchoring does not guarantee an optimal 'pre-orientation' of the LU domain for the receptor interaction.
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Registered trials
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