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6-amidino-2-naphthyl-4-guanidinobenzoate
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Ab (2B7)
inhibits the deposition of C3b on Escherichia coli in hemolymph plasma, whereas it exhibits no inhibitory effect on the deposition of C3b on Staphylococcus aureus
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Aurin tricarboxylic acid
blocks the alternative pathway at a downstream step from C3b attachment. It prevents formation of C3 convertase at the stage where Factor B, attached to the membrane-bound properdin-C3b-Factor B (PC3bB) complex, is cleaved by the protease action of Factor D to form the active C3 convertase enzyme PC3bBb. Activity is restored by the addition of excess Factor D to the serum. But membrane attack complex formation is still blocked by ATA at the stage of C9 addition to C5b678. It has no effect on the classical pathway activation. Binding of aurin tricarboxylic acid to the QPDTIDHDLLLLQLS site blocks the ability of aurin tricarboxylic acid to bind to Factor D protein
C3b-specific antibody fragment S77
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inhibits the alternative pathway C5 convertase in human serum
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C4BP
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the inhibitor blocks both C3 and C5 conversion
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complement factor H-related protein 1
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0.005-0.16 mg/ml inhibits C5 convertase activity
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complement receptor 1
CR1, mediates decay acceleration of the C3bBb complex
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complement receptor of immunoglobulin family
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the inhibitor blocks both C3 and C5 conversion
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Cp40
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the inhibitor blocks both C3 and C5 conversion
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CRIg
phagocytic receptor, binds to the beta-chain of complement components C3b and C3c and inhibits the AP C3 and C5 convertases, structure-activity relationship of CRIg mutants indicated
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decay accelerating factor
DAF, mediates decay acceleration of the C3bBb complex
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decay-accelerating factor
DAF, CD55, major site of interaction with the larger cleavage subunit complement component factor B (Bb), interaction pathway dissected, second short consensus repeat (SCR) domain of DAF (SCR2) interacts only with fragment Bb, whereas SCR4 interacts with complement component C3b, SCR3 does not directly interact with either subunit
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Efb-C
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C-terminal region of extracellular fibrinogen binding protein. The inhibitor specifically blocks C5 conversion, while leaving C3 conversion unaffected
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extracellular complement binding protein
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the inhibitor specifically blocks C5 conversion, while leaving C3 conversion unaffected
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factor H related-protein 5
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inhibits C5 conversion in a concentration-dependent manner
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hemocyanin-depleted plasma
preincubation of hemocyanin-depleted plasma with the anti-factor C Ab (2B7) dose-dependently inhibits the proteolytic conversion of C3 to C3b in the presence of LPS
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hydroxylamine
inactivates the thioester bond on C3, dramatically decreases the deposition of C3b on microbes
Leu-Gly-Leu-Ala-Arg-sarcosine
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inhibits C5 cleavage
OmCI
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the inhibitor blocks C5 cleavage by interfering with convertase recognition far from C5a
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Ornithodoros moubata complement inhibitory protein
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the inhibitor specifically interfers with C5 conversion but not C3 conversion
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Pra1
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i. e. Candida albicans complement regulator acquiring surface protein 2 or pH-regulated Ag 1. In the direct surrounding of the pathogen, inhibitor binds to fluid-phase C3, blocks cleavage of C3 to C3a and C3b and inhibits complement activation via the alternative and classical pathways. In addition, the release of the anaphylatoxins C3a and C5a, as well as C3b/iC3b surface deposition, is reduced. By reducing C3b/iC3b levels at the yeast surface, Pra1 decreases complement-mediated adhesion, as well as uptake of Candida albicans by human macrophages
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soluble complement receptor type 1
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SSL7
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the inhibitor blocks C5 cleavage by interfering with convertase recognition far from C5a
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staphylococcal complement inhibitor
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thioredoxin 1
Trx-1, causes significant inhibition of alternative convertases, mechanism, overview. Trx-1 is capable of inhibiting all classical and alternative convertases but its effect is more pronounced in inhibition of alternative ones
TT32
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human complement receptor type 2 (CR2)/CR1 fusion protein
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eculizumab
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eculizumab
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the inhibitor specifically interfers with C5 conversion but not C3 conversion
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factor H
mediates decay acceleration of the C3bBb complex
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factor H
a well known inhibitor of the alternative complement pathway
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factor H
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the inhibitor blocks both C3 and C5 conversion
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staphylococcal complement inhibitor
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from Staphylococcus aureus, binds and blocks active convertases in solution and induced dimerization of C3bBb
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staphylococcal complement inhibitor
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TT30
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therapeutic fusion protein linking the human complement receptor type 2 C3 fragment-binding domain with the CAP inhibitory domain of human factor H. TT30 efficiently blocks ex vivo CAP-dependent accumulation of C3-fragment on activated surfaces, membrane attack complex formation and hemolysis of red blood cells, without interference of C3 activation or membrane attack complex formation
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TT30
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complement alternative pathway-selective inhibitor, fusion protein linking the first four short consensus repeats of human complement receptor type 2 with the first five short consensus repeats of human factor H
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additional information
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eculizumab does not block the activity of the APC C3 convertase
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additional information
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the anti-factor B autoantibody binds to factor B and to the alternative pathway C3 convertase and alters the kinetics of complement activation and regulation, the anti-factor B autoantibody does not influence the assembly of the C3 convertase
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additional information
addition of guinea pig serum in 40 mM EDTA initiates lysis of existing convertase complexes and excludes the possibility of de novo convertase formation
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additional information
regulatory proteins inactivate C3/C5 convertases on host surfaces to avoid collateral tissue damage
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additional information
the anticoagulogen Ab (14E7) has no effect on the conversion of C3. Abs against coagulation factor G (monoclonal) and the proclotting enzyme (polyclonal) do not inhibit the deposition of C3b on Escherichia coli
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