ArticleFrontiers in immunology2020
Complement C1q Interacts With LRP1 Clusters II and IV Through a Site Close but Different From the Binding Site of Its C1r and C1s-Associated Proteases.
Article in Frontiers in immunology, 2020. 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, 10 citations in OpenAlex.
- Integrated Transcriptomic Analysis Suggests a C1Q-Related Macrophage-Fibroblast Signaling Axis in Keloids.International journal of molecular sciences · 2026Article
- Genomic and Structural Insights into Chandipura Virus: A Comparative in Silico Analysis of Indian and West African Strains and Potential Host Receptor Interactions.Current microbiology · 2025Article
- Article
- Reactive Microglia and Astrocytes as Therapeutic Targets in Prion Diseases.Sub-cellular biochemistry · 2025Review
- Insights into the ligand binding specificity of SREC-II (scavenger receptor expressed by endothelial cells).FEBS open bio · 2021Article
- Molecular Basis of Complement C1q Collagen-Like Region Interaction with the Immunoglobulin-Like Receptor LAIR-1.International journal of molecular sciences · 2021Article
Corrections and comments
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Authors and funding
11 authors at 7 institutions in 2 countries.
Funding
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Abstract
LRP1 is a large endocytic modular receptor that plays a crucial role in the scavenging of apoptotic material through binding to pattern-recognition molecules. It is a membrane anchored receptor of the LDL receptor family with 4 extracellular clusters of ligand binding modules called cysteine rich complement-type repeats that are involved in the interaction of LRP1 with its numerous ligands. Complement C1q was shown to interact with LRP1 and to be implicated in the phagocytosis of apoptotic cells. The present work aimed at exploring how these two large molecules interact at the molecular level using a dissection strategy. For that purpose, recombinant LRP1 clusters II, III and IV were produced in mammalian HEK293F cells and their binding properties were investigated. Clusters II and IV were found to interact specifically and efficiently with C1q with K
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