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Clinical implications and mechanism of complement C1q in polymyositis
Applied Biochemistry and Biotechnology, 2023Polymyositis (PM) is the most common autoimmune disease in neurology and among muscle disorders; it is of great significance to thoroughly understand the mechanism of PM to find new diagnosis and treatment methods. This research intends to elucidate the clinical implications and mechanisms of complement C1q in polymyositis (PM).
Di Wu +6 more
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Binding of complement component C1q by spectrin
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986125I-labelled human C1q was found to bind to human spectrin. Scatchard plots for the binding process were non-linear, indicating the possible presence of multiple classes of binding sites for C1q on spectrin. The binding was ionic-strength-dependent; the extent of binding decreased with increasing ionic strength.
A, Comis, S B, Easterbrook-Smith
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Heme Interacts with C1q and Inhibits the Classical Complement Pathway [PDF]
Journal of Biological Chemistry, 2011 C1q is the recognition subunit of the first component of the classical complement pathway. It participates in clearance of immune complexes and apoptotic cells as well as in defense against pathogens. Inappropriate activation of the complement contributes to cellular and tissue damage in different pathologies, urging the need for the development of ...
Lubka T Roumenina +2 more
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Complement and C1q Binding Substances in Otitis Media
Annals of Otology, Rhinology & Laryngology, 1980Complement activation, as shown by increased amounts of complexes composed of Clr-Cls-Cl IA, and abnormal complexes of Clr-Cls were demonstrated in serum from patients with acute pneumococcal and chronic otitis media, serous or mucoid respectively. C1q binding substances were shown in middle ear effusions and in sera from patients with chronic serous ...
K, Prellner +3 more
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Complement activation by phospholipids: the interplay of factor H and C1q [PDF]
Protein and Cell, 2010 Complement proteins in blood recognize charged particles. The anionic phospholipid (aPL) cardiolipin binds both complement proteins C1q and factor H. C1q is an activator of the complement classical pathway, while factor H is an inhibitor of the alternative pathway.
R B Sim, Uday Kishore
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Regulation of the alternative pathway of human complement by C1q
Molecular Immunology, 1987The interaction of C1q with C3b and its effect on C3b activities in the alternative pathway of complement (APC) have been studied. Purified C1q markedly inhibited C3b deposition on and lysis of rabbit erythrocytes by the isolated cytolytic APC. It also blocked formation of the C3 convertase, C3b, Bb as well as binding of Factors B and H to sheep ...
Z, Fishelson, H J, Müller-Eberhard
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C1q component of complement binds to fibrinogen and fibrin
Biochemistry, 1988The interaction of complement component C1q with fibrinogen and fibrin was studied by using a solid-phase direct binding assay. Scatchard analysis of radioiodinated fibrinogen binding to C1q indicated at least two high-affinity binding constants (Kd) calculated as 8.5 and 120 nM. In contrast, binding of radioiodinated fibrin to C1q showed only a single
R A, Entwistle, L T, Furcht
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Detection of complement C1q receptors on human spermatozoa
Journal of Reproductive Immunology, 1998Clq, the first component of the classical complement pathway, is known to play roles in promoting phagocytic events, in addition to its role in activation of complement. Although the molecular events in fertilization leading to the entrance of the spermatozoan into the egg are not well understood, ultrastructural observations suggest that the process ...
R, Bronson +4 more
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