Results 91 to 100 of about 12,786 (117)

Bactericidal Membrane Attack Complex formation initiates at the new pole ofE. coli

open access: yes
van ‘t Wout MF   +7 more
europepmc   +1 more source

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   +5 more
openaire   +3 more sources

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   +3 more
openaire   +2 more sources

Assembly and regulation of the complement amplification loop in blood: the role of C3b-C3b-IgG complexes

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
openaire   +3 more sources

Crystallization of human methylamine-treated complement C3 and C3b

Acta Crystallographica Section D Biological Crystallography, 1994
Human 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
openaire   +4 more sources

The Nature of the Receptor for Complement (C3b) in the Human Renal Glomerulus

American Journal of Clinical Pathology, 1978
The 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
openaire   +3 more sources

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