Results 171 to 180 of about 27,085 (217)
Ionic tethering contributes to the conformational stability and function of complement C3b
Molecular Immunology, 2017 C3b, the central component of the alternative pathway (AP) of the complement system, coexists as a mixture of conformations in solution. These conformational changes can affect interactions with other proteins and complement regulators. Here we combine a computational model for electrostatic interactions within C3b with molecular imaging to study the ...
Reed E S Harrison +2 more
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Structure of complement fragment C3b–factor H and implications for host protection by complement regulators [PDF]
Nature Immunology, 2009 Factor H (FH) is an abundant regulator of complement activation and protects host cells from self-attack by complement. Here we provide insight into the regulatory activity of FH by solving the crystal structure of the first four domains of FH in complex with its target, complement fragment C3b.
Daniel Ricklin +2 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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Crystallization of human complement component C3b in the presence of a staphylococcal complement-inhibitor protein (SCIN) [PDF]
Acta Crystallographica Section F: Structural Biology Communications, 2009 Staphylococcus aureus secretes a number of small proteins that effectively attenuate the human innate immune response. Among these, the staphylococcal complement-inhibitor protein (SCIN) disrupts the function of the complement component 3 (C3) convertase that is initiated through either the classical or the alternative pathway and thereby prevents ...
Brandon L Garcia +2 more
exaly +3 more sources
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.
Jelezarova E, Lutz HU
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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.
Jelezarova E, Lutz HU
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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 ...
J R, Carlo, R B, Nagle, M L, Shin
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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.
A H, Sørensen +5 more
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[Binding of activated C3b component with complement effector].
Bioorganicheskaia khimiia, 1985Various nucleophilic agents (acceptors) react with thiolester group of nascent activated fragment (C3b) of the third complement component. The C3b-acceptors binding prevents transformation of C3 convertase to C5 convertase and results in inhibition of the cell-target lysis.
L V, Kozlov +3 more
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