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mSphere of Influence: Complement activity beyond systemic circulation-implications in the context of infections. [PDF]
Desai JV.
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Chronic kidney disease enhances alternative pathway activity: a new paradigm. [PDF]
Jalal DI, Thurman JM, Smith RJ.
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Bactericidal Membrane Attack Complex formation initiates at the new pole ofE. coli
van ‘t Wout MF+7 more
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The structure of complement C3b provides insights into complement activation and regulation
Nature, 2006The human complement system is an important component of innate immunity. Complement-derived products mediate functions contributing to pathogen killing and elimination. However, inappropriate activation of the system contributes to the pathogenesis of immunological and inflammatory diseases.
A, Abdul Ajees+5 more
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Characterization of the human complement (c3b) receptor with a fluid phase C3b dimer.
The Journal of Immunology, 1981Abstract The interaction of C3b receptor with C3b, the major cleavage product of C3, elicits important biologic functions, such as enhanced phagocytosis and release of cellular enzymes. We determined the binding kinetics and binding isotherm of C3b-receptor interaction by using human cells and fluid phase C3b generated by trypsin ...
M A, Arnaout+3 more
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Molecular Immunology, 1999
Amplification of complement activation in blood and serum starts on multi-protein complexes that act as precursors of an alternative C3 convertase. Among these covalently linked C4b-, C3b-, and IgG-containing complexes C3b-C3b-IgG complexes represent the major species containing C3b and IgG.
Emiliana Jelezarova, Hans U. Lutz
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Amplification of complement activation in blood and serum starts on multi-protein complexes that act as precursors of an alternative C3 convertase. Among these covalently linked C4b-, C3b-, and IgG-containing complexes C3b-C3b-IgG complexes represent the major species containing C3b and IgG.
Emiliana Jelezarova, Hans U. Lutz
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Crystallization of human methylamine-treated complement C3 and C3b
Acta Crystallographica Section D Biological Crystallography, 1994Human methylamine-treated complement C3 (C3-MA) and C3b (C3b-MA) have been crystallized using ammonium sulfate as precipitant. The crystals of the two compounds are morphologically indistinguishable though they belong to different space groups. We show that only minor alterations in packing are responsible for the change in space group.
Søren Thirup+5 more
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The Nature of the Receptor for Complement (C3b) in the Human Renal Glomerulus
American Journal of Clinical Pathology, 1978The physicochemical nature of the human glomerular complement receptor was studied. Receptor activity was measured by determining the avidity of glomeruli of normal human renal tissue for fluorescein-labeled bacteria (S.typhi) coated with C3b. Maximal binding of C3b-coated bacteria to normal human glomeruli took place in phosphate-saline buffers of pH ...
Moon L. Shin+2 more
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