INT159248

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Context Info
Confidence 0.46
First Reported 2009
Last Reported 2009
Negated 3
Speculated 1
Reported most in Body
Documents 2
Total Number 8
Disease Relevance 2.54
Pain Relevance 0.20

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

cytosol (MEFV) cytoskeleton (MEFV) nucleus (MEFV)
intracellular (MEFV) cytoplasm (MEFV)
Anatomy Link Frequency
filaments 4
SH3 4
MEFV (Homo sapiens)
Pain Link Frequency Relevance Heat
abdominal pain 1 96.48 Very High Very High Very High
Arthritis 14 90.44 High High
Inflammation 63 72.64 Quite High
Pain 14 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Fever 85 100.00 Very High Very High Very High
Congenital Anomalies 1 100.00 Very High Very High Very High
Sacroiliitis 1 99.76 Very High Very High Very High
Syndrome 63 99.72 Very High Very High Very High
Disease 71 99.34 Very High Very High Very High
Abdominal Pain 1 96.48 Very High Very High Very High
Serositis 1 92.96 High High
Acne 14 91.72 High High
Pyoderma Gangrenosum 14 91.32 High High
Arthritis 14 90.44 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
We therefore examined the effect of the W232A mutation and the requirement for the SH3 domain on pyrin's recruitment to and reticularization of PSTPIP1 filaments.
Spec (examined) Positive_regulation (requirement) of pyrin Spec (examined) Binding (recruitment) of in SH3
1) Confidence 0.46 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0 Pain Relevance 0
Mutant PSTPIP1, by virtue of its increased binding affinity for pyrin, may be somewhat more readily recruited to ASC specks than is wild type PSTPIP1, placing mutant PSTPIP1 more frequently in the inflammasome compartment.
Positive_regulation (increased) of pyrin Binding (affinity) of
2) Confidence 0.46 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0.15 Pain Relevance 0.04
In contrast, the W232A mutation in PSTPIP1 abolished pyrin binding; consequently, PSTPIP1 filaments were primarily straight, not extensively branched (Figure 4I–K), confirming that the reticularization of PSTPIP1 filaments is a direct consequence of pyrin binding.
Positive_regulation (consequence) of pyrin Binding (binding) of in filaments
3) Confidence 0.46 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0 Pain Relevance 0
Patients with FMF are considered to have an increased risk of sacroiliitis, while the association of such abnormalities with FMF has not been accepted uniformly.
Neg (not) Positive_regulation (accepted) of FMF Binding (association) of associated with sacroiliitis, congenital anomalies and fever
4) Confidence 0.44 Published 2009 Journal Singapore Med J Section Abstract Doc Link 19352557 Disease Relevance 1.12 Pain Relevance 0.10
Since disease-associated mutations in PSTPIP1 enhance pyrin binding, PAPA syndrome and FMF are thought to share a common pathoetiology.
Positive_regulation (enhance) of pyrin Binding (binding) of associated with syndrome, fever and disease
5) Confidence 0.43 Published 2009 Journal PLoS ONE Section Abstract Doc Link PMC2702820 Disease Relevance 0.95 Pain Relevance 0.05
We also examine the pyrin/PSTPIP1 interaction and show that contrary to earlier predictions [5], the PSTPIP1 SH3 domain is not required for its interaction with pyrin.
Neg (not) Positive_regulation (required) of pyrin Binding (interaction) of in SH3
6) Confidence 0.40 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0.27 Pain Relevance 0
This region might also be a PEST phosphatase interaction surface, since pyrin and PEST phosphatase are thought to bind to the same region of PSTPIP1 and the PAPA mutations increase affinity for pyrin while decreasing affinity for PEST phophatases [5].
Positive_regulation (increase) of pyrin Binding (affinity) of
7) Confidence 0.40 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0 Pain Relevance 0
First, our studies show clearly that the SH3 domain of PSTPIP1 is not required for pyrin binding nor is it necessary for pyrin-mediated reticularization of PSTPIP1 filaments.
Neg (not) Positive_regulation (required) of pyrin Binding (binding) of in filaments
8) Confidence 0.40 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0.05 Pain Relevance 0.03

General Comments

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