INT155160

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Context Info
Confidence 0.47
First Reported 2004
Last Reported 2009
Negated 0
Speculated 0
Reported most in Body
Documents 20
Total Number 21
Disease Relevance 7.77
Pain Relevance 2.61

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

lipid binding (C3) extracellular space (C3) extracellular region (C3)
Anatomy Link Frequency
cleavage 2
mast cells 2
plasma 1
chondrocytes 1
cartilage 1
C3 (Mus musculus)
Pain Link Frequency Relevance Heat
Arthritis 224 97.84 Very High Very High Very High
cytokine 36 94.56 High High
Inflammation 152 91.36 High High
Potency 6 90.84 High High
tetrodotoxin 6 89.68 High High
cerebral cortex 5 87.92 High High
Hippocampus 23 76.44 Quite High
cva 38 75.68 Quite High
potassium channel 6 70.56 Quite High
chemokine 6 63.92 Quite High
Disease Link Frequency Relevance Heat
Paroxysmal Nocturnal Hemoglobinuria 275 99.84 Very High Very High Very High
Targeted Disruption 60 99.46 Very High Very High Very High
Arthritis 247 97.84 Very High Very High Very High
Amyloid Plaque 27 97.64 Very High Very High Very High
Hemolysis 73 97.56 Very High Very High Very High
Disease Progression 5 95.84 Very High Very High Very High
INFLAMMATION 176 91.36 High High
Cancer 165 89.80 High High
Synovitis 10 89.68 High High
Hematological Disease 24 87.88 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Analysis of the chemical structure showed that the relaxant activity was progressively diminished by the presence of hydroxyl group at C-3, saturation of the C-2, C-3 double bound, saturation of the C-2, C-3 double bound coupled with lack of the C-4 carbonyl and glycosylation.
C-3 Binding (bound) of
1) Confidence 0.47 Published 2008 Journal Eur. J. Pharmacol. Section Abstract Doc Link 18840426 Disease Relevance 0 Pain Relevance 0.19
Analysis of the chemical structure showed that the relaxant activity was progressively diminished by the presence of hydroxyl group at C-3, saturation of the C-2, C-3 double bound, saturation of the C-2, C-3 double bound coupled with lack of the C-4 carbonyl and glycosylation.
C-3 Binding (bound) of
2) Confidence 0.36 Published 2008 Journal Eur. J. Pharmacol. Section Abstract Doc Link 18840426 Disease Relevance 0 Pain Relevance 0.17
Analysis of the chemical structure showed that the relaxant activity was progressively diminished by the presence of hydroxyl group at C-3, saturation of the C-2, C-3 double bound, saturation of the C-2, C-3 double bound coupled with lack of the C-4 carbonyl and glycosylation.
C-3 Binding (bound) of
3) Confidence 0.36 Published 2008 Journal Eur. J. Pharmacol. Section Abstract Doc Link 18840426 Disease Relevance 0 Pain Relevance 0.17
Analysis of the chemical structure showed that the relaxant activity was progressively diminished by the presence of hydroxyl group at C-3, saturation of the C-2, C-3 double bound, saturation of the C-2, C-3 double bound coupled with lack of the C-4 carbonyl and glycosylation.
C-3 Binding (bound) of
4) Confidence 0.36 Published 2008 Journal Eur. J. Pharmacol. Section Abstract Doc Link 18840426 Disease Relevance 0 Pain Relevance 0.20
Analysis of the chemical structure showed that the relaxant activity was progressively diminished by the presence of hydroxyl group at C-3, saturation of the C-2, C-3 double bound, saturation of the C-2, C-3 double bound coupled with lack of the C-4 carbonyl and glycosylation.
C-3 Binding (saturation) of
5) Confidence 0.36 Published 2008 Journal Eur. J. Pharmacol. Section Abstract Doc Link 18840426 Disease Relevance 0 Pain Relevance 0.17
Analysis of the chemical structure showed that the relaxant activity was progressively diminished by the presence of hydroxyl group at C-3, saturation of the C-2, C-3 double bound, saturation of the C-2, C-3 double bound coupled with lack of the C-4 carbonyl and glycosylation.
C-3 Binding (saturation) of
6) Confidence 0.36 Published 2008 Journal Eur. J. Pharmacol. Section Abstract Doc Link 18840426 Disease Relevance 0 Pain Relevance 0.16
It acts via three mechanisms: preventing the formation of the C3 convertase by binding to C4b; accelerating the natural decay of the classical pathway C3 convertase; and as a cofactor for the serine proteinase factor I in the proteolytic inactivation of C4b, which prevents the formation of the C3 convertase.
C3 Binding (formation) of
7) Confidence 0.25 Published 2007 Journal Arthritis Res Ther Section Body Doc Link PMC2212569 Disease Relevance 0.53 Pain Relevance 0.07
It acts via three mechanisms: preventing the formation of the C3 convertase by binding to C4b; accelerating the natural decay of the classical pathway C3 convertase; and as a cofactor for the serine proteinase factor I in the proteolytic inactivation of C4b, which prevents the formation of the C3 convertase.
C3 Binding (formation) of
8) Confidence 0.25 Published 2007 Journal Arthritis Res Ther Section Body Doc Link PMC2212569 Disease Relevance 0.37 Pain Relevance 0.07
How the alternative pathway is activated is still a matter of speculation: one method would be the formation and stabilization of surface-bound C3b-IgG fragments on the acellular cartilage surface, leading to formation of the C3 and C5 convertase.
C3 Binding (formation) of in cartilage
9) Confidence 0.20 Published 2005 Journal Arthritis Res Ther Section Body Doc Link PMC1175042 Disease Relevance 0.84 Pain Relevance 0.19
However, progeny mice of crosses between K/B × N and knockout mice deficient for either complement factor B, C3, C5 or C5aR were found to be completely resistant to arthritis.
C3 Binding (complement) of associated with targeted disruption and arthritis
10) Confidence 0.20 Published 2005 Journal Arthritis Res Ther Section Body Doc Link PMC1175042 Disease Relevance 1.26 Pain Relevance 0.32
Because there are no complement regulatory proteins – which usually inhibit complement activation on eukaryotic cells – present on the cartilage surface and because the bound IgGs are able to bind C3b and prevent the binding of the complement regulatory plasma proteins factor I and factor H, formation of the C3 convertase is possible.
C3 Binding (formation) of in plasma
11) Confidence 0.20 Published 2005 Journal Arthritis Res Ther Section Body Doc Link PMC1175042 Disease Relevance 0.75 Pain Relevance 0.21
This would be explained by the absence of membrane-bound C3 inhibitors from chondrocytes [98].
C3 Binding (bound) of in chondrocytes
12) Confidence 0.19 Published 2005 Journal Arthritis Res Ther Section Body Doc Link PMC1064898 Disease Relevance 1.09 Pain Relevance 0.26
RANTES (Ccl5) is chemotactic for mast cells [18] and fragments generated autocatalytically from complement C3 (C3) are capable of stimulating mast cells to release TNF?
C3 Binding (complement) of in mast cells
13) Confidence 0.17 Published 2008 Journal BMC Cancer Section Body Doc Link PMC2529338 Disease Relevance 0.54 Pain Relevance 0.11
RANTES (Ccl5) is chemotactic for mast cells [18] and fragments generated autocatalytically from complement C3 (C3) are capable of stimulating mast cells to release TNF?
C3 Binding (complement) of in mast cells
14) Confidence 0.15 Published 2008 Journal BMC Cancer Section Body Doc Link PMC2529338 Disease Relevance 0.54 Pain Relevance 0.11
Its effects include binding to and subsequent inactivation of C1, inhibition of MAC assembly, and blockage of the formation of C3 convertase (Baker et al 1975; Hughes-Jones and Gardner 1978; Almeda et al 1983; Weiler 1983).
C3 Binding (formation) of
15) Confidence 0.15 Published 2008 Journal Biologics : Targets & Therapy Section Body Doc Link PMC2727911 Disease Relevance 0 Pain Relevance 0
Weisman et al developed this molecule, which comprises the entire extracellular domain of CR1, and showed that it inhibited formation of C3 and C5 convertases in vivo (Weisman et al 1990a, 1990b).
C3 Binding (formation) of
16) Confidence 0.15 Published 2008 Journal Biologics : Targets & Therapy Section Body Doc Link PMC2727911 Disease Relevance 0 Pain Relevance 0
Similarly, in the lectin pathway, cleavage of C4 and C2 allow formation of the C3 convertase.
C3 Binding (formation) of in cleavage
17) Confidence 0.15 Published 2008 Journal Biologics : Targets & Therapy Section Body Doc Link PMC2727911 Disease Relevance 0 Pain Relevance 0
Because C3b, an activation protein produced by cleavage of C3, functions as an opsonin [89], the increased C3 levels together with the reduced A?
C3 Binding (cleavage) of in cleavage
18) Confidence 0.10 Published 2004 Journal J Neuroinflammation Section Body Doc Link PMC529311 Disease Relevance 0.51 Pain Relevance 0.18
Antibody interference assays have shown that complex C1 is composed of Sp1 whereas complexes C2 and C3 consist mainly of Sp3 [9,15].
C3 Binding (complexes) of
19) Confidence 0.07 Published 2008 Journal Cell Signal Section Body Doc Link PMC2586094 Disease Relevance 0 Pain Relevance 0
This suboptimal response may be due to the complement protein C3 binding to PNH red blood cells causing an increase in extravascular hemolysis.63 Co-existent bone marrow failure is also likely to be contributory.
C3 Binding (binding) of in bone marrow associated with hemolysis and paroxysmal nocturnal hemoglobinuria
20) Confidence 0.06 Published 2009 Journal Therapeutics and Clinical Risk Management Section Body Doc Link PMC2789686 Disease Relevance 0.62 Pain Relevance 0

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