Results 151 to 160 of about 792,617 (213)

Characterization of the human complement (c3b) receptor with a fluid phase C3b dimer.

The Journal of Immunology, 1981
Abstract 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, J, Melamed, B F, Tack, H R, Colten   +3 more
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The structure of complement C3b provides insights into complement activation and regulation

Nature, 2006
The 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, K, Gunasekaran, John E, Volanakis, Sthanam V L, Narayana, Girish J, Kotwal, H M Krishna, Murthy   +5 more
openaire   +3 more sources

Complement C3b interactions studied with surface plasmon resonance technique

International Immunopharmacology, 2001
The surface plasmon resonance (SPR) phenomenon is utilized in a number of new real time biosensors. In this study, we have used this technique to study interactions between the central complement component C3b and its multiple ligands by using the Biacore equipment.
T S, Jokiranta, J, Westin, U R, Nilsson, B, Nilsson, J, Hellwage, S, Löfås, D L, Gordon, K N, Ekdahl, S, Meri   +8 more
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Epithelial Deposition of Immunoglobulin G1 and Activated Complement (C3b and Terminal Complement Complex) in Ulcerative Colitis

Gastroenterology, 1990
The epithelial destruction seen in ulcerative colitis remains unexplained. Complement activation has been proposed to be involved, but no definite evidence has been available to this end. In the present study, we examined immunohistochemically ulcerative colitis lesions with monoclonal antibodies to activation neoepitopes in the complement component ...
T S, Halstensen, T E, Mollnes, P, Garred, O, Fausa, P, Brandtzaeg   +4 more
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Associated complement C3b. Towards an understanding of its intracellular modifications

Molecular Immunology, 1993
Covalent Superose microspheres-bound C3b was used as a model system to simplify the analysis of antigen-bound C3b modifications during antigen processing. The model was set up using purified C3 and Superose-bound trypsin. C3b was covalently bound to Superose through an ester link, as indicated by lability to hydroxylamine treatment at alkaline pH.
C A, Rey-Millet, S, Chesne, M G, Colomb
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