INT152503

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Context Info
Confidence 0.45
First Reported 2006
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 3
Total Number 20
Disease Relevance 8.64
Pain Relevance 1.03

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

Anatomy Link Frequency
erythrocyte 3
CR1 (Homo sapiens)
Pain Link Frequency Relevance Heat
antagonist 1 99.50 Very High Very High Very High
c fibre 2 97.14 Very High Very High Very High
Adelta 4 96.98 Very High Very High Very High
dorsal root ganglion 1 93.12 High High
substantia gelatinosa 4 92.20 High High
Spinal cord 2 75.00 Quite High
Dorsal horn 1 75.00 Quite High
allodynia 1 71.04 Quite High
Thermal hyperalgesia 1 68.16 Quite High
Stimulus evoked pain 1 66.80 Quite High
Disease Link Frequency Relevance Heat
Sprains And Strains 720 99.98 Very High Very High Very High
Malaria 357 99.52 Very High Very High Very High
Ganglion Cysts 1 92.16 High High
Targeted Disruption 198 92.08 High High
Thalassemia 52 88.64 High High
Anaemia 31 85.32 High High
Necrosis 2 75.00 Quite High
Cancer 2 75.00 Quite High
Infection 8 73.40 Quite High
Neuropathic Pain 2 71.04 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
The ability of merozoites to interact with CR1 was shown by immunofluorescence microscopy and without question by the demonstration that merozoites can bind preferentially to sCR1-coated polystyrene microspheres (Figure 6).
CR1 Binding (interact) of
1) Confidence 0.45 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2887475 Disease Relevance 0.38 Pain Relevance 0
These results suggest that both sialic acid-dependent and independent strains interact with CR1 in the normal red cell during the invasion process.
CR1 Binding (interact) of associated with sprains and strains
2) Confidence 0.45 Published 2010 Journal PLoS Pathogens Section Abstract Doc Link PMC2887475 Disease Relevance 0.58 Pain Relevance 0
To further document the interaction of merozoites with CR1, we incubated enriched schizonts and late trophozoites with polystyrene microspheres coated with sCR1, BSA, glycophorin A, or fetuin.
CR1 Binding (interaction) of
3) Confidence 0.45 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2887475 Disease Relevance 0.28 Pain Relevance 0
We observed no clearly discernible difference between 7G8 and the sialic acid-dependent strain Dd2 by immunofluorescent microscopy (data not shown), suggesting that both strains can interact with CR1 or that this technique lacks sensitivity to detect differences in the way the two strains interact with CR1.
CR1 Binding (interact) of associated with sprains and strains
4) Confidence 0.45 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2887475 Disease Relevance 0.29 Pain Relevance 0
Figure 6 shows that merozoites bind to CR1-coated microspheres with greater frequency than to microspheres coated with BSA, glycophorin A, or fetuin.
CR1 Binding (bind) of
5) Confidence 0.45 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2887475 Disease Relevance 0.26 Pain Relevance 0
We observed no clearly discernible difference between 7G8 and the sialic acid-dependent strain Dd2 by immunofluorescent microscopy (data not shown), suggesting that both strains can interact with CR1 or that this technique lacks sensitivity to detect differences in the way the two strains interact with CR1.
CR1 Binding (interact) of associated with sprains and strains
6) Confidence 0.45 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2887475 Disease Relevance 0.29 Pain Relevance 0
Regardless, these results confirm that merozoites can interact directly with CR1.
CR1 Binding (interact) of
7) Confidence 0.39 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2887475 Disease Relevance 0.12 Pain Relevance 0
The ability of merozoites to interact with CR1 was shown by immunofluorescence microscopy and without question by the demonstration that merozoites can bind preferentially to sCR1-coated polystyrene microspheres (Figure 6).
sCR1 Binding (bind) of
8) Confidence 0.39 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2887475 Disease Relevance 0.35 Pain Relevance 0
Although not all merozoites were seen to interact directly with CR1, examples of this interaction were easy to find.
CR1 Binding (interact) of
9) Confidence 0.39 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2887475 Disease Relevance 0.49 Pain Relevance 0
Additional work will be needed to determine whether CR1 serves as receptor for any of the PfRh ligands.
CR1 Binding (receptor) of
10) Confidence 0.39 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2887475 Disease Relevance 0.07 Pain Relevance 0
We show that soluble CR1 (sCR1) as well as polyclonal and monoclonal antibodies against CR1 inhibit sialic acid-independent invasion in a variety of laboratory strains and wild isolates, and that merozoites interact directly with CR1 on the erythrocyte surface and with sCR1-coated microspheres.
CR1 Binding (interact) of in erythrocyte associated with sprains and strains
11) Confidence 0.35 Published 2010 Journal PLoS Pathogens Section Abstract Doc Link PMC2887475 Disease Relevance 0.57 Pain Relevance 0
Further, the binding to sCR1-coated microspheres was inhibited by chicken anti-CR1 whereas the binding to BSA-coated microspheres was not inhibited by polyclonal rabbit anti-BSA.


CR1 Binding (binding) of
12) Confidence 0.35 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2887475 Disease Relevance 0.23 Pain Relevance 0
One possible explanation for these observations is that the CR1 ligand in sialic acid-dependent strains may require interaction with both CR1 and glycophorin to mediate invasion optimally.
CR1 Binding (interaction) of associated with sprains and strains
13) Confidence 0.33 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2887475 Disease Relevance 0.43 Pain Relevance 0
Merozoites were observed interacting directly with CR1 on erythrocytes both in neuraminidase-treated and untreated control cells (Figure 5, Figure S3, and Supplementary 3D Videos S1, S2, S3, S4, S5, and S6).
CR1 Binding (interacting) of in erythrocytes
14) Confidence 0.33 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2887475 Disease Relevance 0.42 Pain Relevance 0
These experiments suggest that both sialic acid-independent and dependent strains are able to interact with CR1, but for the latter CR1-mediated invasion may rely on the presence of intact sialic acid on glycophorin.


CR1 Binding (interact) of associated with sprains and strains
15) Confidence 0.33 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2887475 Disease Relevance 0.85 Pain Relevance 0
To demonstrate direct interaction between merozoites and CR1, we performed immunofluorescent microscopy using freshly released merozoites.
CR1 Binding (interaction) of
16) Confidence 0.30 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2887475 Disease Relevance 0.54 Pain Relevance 0
We show that soluble CR1 (sCR1) as well as polyclonal and monoclonal antibodies against CR1 inhibit sialic acid-independent invasion in a variety of laboratory strains and wild isolates, and that merozoites interact directly with CR1 on the erythrocyte surface and with sCR1-coated microspheres.
sCR1 Binding (interact) of in erythrocyte associated with sprains and strains
17) Confidence 0.30 Published 2010 Journal PLoS Pathogens Section Abstract Doc Link PMC2887475 Disease Relevance 0.59 Pain Relevance 0
Further, the binding to sCR1-coated microspheres was inhibited by chicken anti-CR1 whereas the binding to BSA-coated microspheres was not inhibited by polyclonal rabbit anti-BSA.


sCR1 Binding (binding) of
18) Confidence 0.29 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2887475 Disease Relevance 0.24 Pain Relevance 0
First, they found a protective association between a promoter polymorphism of red cell CR1 and severe falciparum malaria, and second, they found an independent negative association between the expression of red cell CR1 and ?
CR1 Binding (association) of associated with malaria
19) Confidence 0.16 Published 2006 Journal PLoS Medicine Section Body Doc Link PMC1435778 Disease Relevance 1.15 Pain Relevance 0
The effects of TNF-alpha on Adelta/C fiber-evoked monosynaptic and polysynaptic or spontaneous EPSCs were significantly blocked by 5 microM TNF-alpha antagonist that inhibits TNF-alpha binding to its type 1 receptor (TNFR1).
type 1 receptor Binding (binding) of associated with c fibre, antagonist and adelta
20) Confidence 0.00 Published 2008 Journal J. Neurosci. Res. Section Abstract Doc Link 18543334 Disease Relevance 0.49 Pain Relevance 1.03

General Comments

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