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Neuromyelitis optica patients had higher levels of C3a and anti-C1q antibodies than healthy controls.
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C1q deficiency due to a Gly164Ser mutation may have a role in Rothmund-Thomson syndrome and glomerulonephritis [case report]
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Data indicate that Cna binds to C1q.
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Analysis of its interaction properties by surface plasmon resonance shows that rC1q retains the ability of serum C1q to associate with the C1s-C1r-C1r-C1s tetramer, to recognize physiological C1q ligands such as IgG and pentraxin 3
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Single nucleotide polymorphisms in and around the C1q genes, C1qA, C1qB and C1qC, correlated with C1q serum levels and may be a risk for the development of rheumatoid arthritis.
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We identified a major linear epitope of C1q that is the target of anti-C1q in systemic lupus erythematosus.
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C1q and C1q receptor interaction may be responsible for the C1q-mediated migration of mesenchymal stromal cells.
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analysis of the molecular mechanisms for synchronized transcription of three complement C1q subunit genes (A, B and C) in dendritic cells and macrophages
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Three single nucleotide polymorphisms (STAT6 rs703817, C1qG rs17433222, and MBP rs3794845) were found to be significantly associated with childhood leukemia risk in Koreans.
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These results suggest a novel pathway in which C1q and MBL influence removal and metabolism of atherogenic forms of LDL in the early stages of atherosclerosis.
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prevents monocyte-derived dendritic cell differentiation
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In a large family-based association study of C1Q gene cluster polymorphisms no evidence for a genetic role of C1Q locus SNP in systemic lupus erythematosus risk predisposition was obtained in patients of European ancestry.
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Data show that C1q, C4, C3, and C9 bind to thrombin receptor-activating peptide-activated platelets in lepirudin-anticoagulated platelet-rich plasma (PRP) and whole blood.
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Experiments with recombinant globular head domains of human C1q A, B, and C chains indicated that C1q interacts with PTX3 via its globular head region. Binding of C1q to immobilized PTX3 induced activation of the classical complement pathway.
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The C-terminal globular region of the C1Q C chain may have evolved as a functionally specialized domain or module with distinct binding properties which together with the A and B chains confers versatility and flexibility to the whole C1q molecule.
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The structure refined to 1.9 A of resolution of C1q reveals the conformation of subunits A, B, and C and their compact, almost spherical heterotrimeric assembly held together mainly by non-polar interactions, with a Ca2+ ion bound at the top.
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Complementary interacting sites on the C1q globular domain have been precisely defined. Characterization of point mutants suggests a complementary role for Arg156 of C1Q C chain in the C1q-IgG interaction.
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results suggest that charged residues belonging to the apex of the gC1q heterotrimer (with participation of all three chains) as well as the side of the ghB are crucial for C1q binding to ligands, IgG1, C-reactive protein, and pentraxin 3
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C1q polymorphisms are associated with SLE, serum C1q and CH50 levels in a stable founder population of patients with SLE.
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The peripheral globular region of the C1q molecule displays a lectin-like activity, which contributes to DNA binding through interaction with its deoxy-d-ribose moiety and may participate in apoptotic cell recognition.
