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C1QB expression is significantly upregulated in human masticatory mucosa during wound healing
no significant association found to either rs15940 (C1QA) or rs172378 (C1QC) when analysed in just Parkinson disease cases , just controls or combined
PepO facilitates C1q-mediated bacterial adherence, whereas its localized release consumes complement as a result of its activation following binding of C1q, thus representing an additional mechanism of human complement escape by this versatile pathogen.
Data indicate that Cna binds to C1q.
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
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.
We identified a major linear epitope of C1q that is the target of anti-C1q in systemic lupus erythematosus.
analysis of the molecular mechanisms for synchronized transcription of three complement C1q subunit genes (A, B and C) in dendritic cells and macrophages
The susceptibility for schizophrenia was particularly associated with C1QB rs291982 GG genotype.
a 2-gene signature consisting of PLEK2 and C1QB led to the best result that correctly classified 93.3% melanoma patients and 90% healthy controls
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.
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.
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.
The C-terminal globular region of the C1Q B chain may have evolved as a functionally specialized domain or module with distinct binding properties which together with the A and C chains confers versatility and flexibility to the whole C1q molecule.
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.
Complementary interacting sites on the C1q globular domain have been precisely defined. Characterization of point mutants suggests a central role for Arg114 and a complementary role for Arg129, Arg163, and His117 of C1Q B chain in the C1q-IgG interaction.
The first analysis of C1q by mass spectrometry yields evidence that the B chain moiety of the globular head is involved in the interaction with fucoidan and underscores the particular role of arginine-109 in the charge pattern recognition property of C1q.
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.
No C1q or low molecular weight C1q was detected in sera and no anti-C1q autoantibodies were found. Sequencing of the C1q genes revealed a novel missense mutation (Gly-Arg) in codon 217 of the B chain.
The mRNA levels of H2-d1 in the prefrontal cortex, hippocampus, and hypothalamus and C1qb in the hippocampus of the DBA/2 J strain were significantly down-regulated as compared to those in the C57BL/6 J strain
This gene encodes a major constituent of the human complement subcomponent C1q. C1q associates with C1r and C1s in order to yield the first component of the serum complement system. Deficiency of C1q has been associated with lupus erythematosus and glomerulonephritis. C1q is composed of 18 polypeptide chains: six A-chains, six B-chains, and six C-chains. Each chain contains a collagen-like region located near the N terminus and a C-terminal globular region. The A-, B-, and C-chains are arranged in the order A-C-B on chromosome 1. This gene encodes the B-chain polypeptide of human complement subcomponent C1q
complement C1q subcomponent subunit B
, complement component 1, q subcomponent, beta polypeptide
, complement component C1q, B chain
, complement subcomponent C1q chain B
, complement C1qB