INT150392

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Context Info
Confidence 0.51
First Reported 2008
Last Reported 2009
Negated 2
Speculated 3
Reported most in Body
Documents 2
Total Number 40
Disease Relevance 10.49
Pain Relevance 1.44

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, PSTPIP1) cytoskeleton (MEFV, PSTPIP1) cytoplasm (MEFV, PSTPIP1)
signal transduction (PSTPIP1) oxidoreductase activity (PSTPIP1) cell adhesion (PSTPIP1)
Anatomy Link Frequency
filaments 6
SH3 5
tubules 1
MEFV (Homo sapiens)
PSTPIP1 (Homo sapiens)
PSTPIP1 - W232A (1)
Pain Link Frequency Relevance Heat
Inflammation 352 99.76 Very High Very High Very High
Arthritis 78 97.44 Very High Very High Very High
Pain 79 82.24 Quite High
Disease Link Frequency Relevance Heat
Apoptosis 3 100.00 Very High Very High Very High
Disease 390 99.92 Very High Very High Very High
INFLAMMATION 352 99.76 Very High Very High Very High
Acne 78 98.72 Very High Very High Very High
Pyoderma Gangrenosum 78 98.32 Very High Very High Very High
Fever 433 97.72 Very High Very High Very High
Arthritis 78 97.44 Very High Very High Very High
Syndrome 352 96.32 Very High Very High Very High
Pain 79 82.24 Quite High
Osteomyelitis 156 70.96 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Modeling studies support these experimental results and predict a coherent surface on the PSTPIP1 dimer that may interact with pyrin.
pyrin Binding (interact) of PSTPIP1 dimer
1) Confidence 0.51 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0.33 Pain Relevance 0.03
PSTPIP1 binds to pyrin and mutations in pyrin result in familial Mediterranean fever (FMF), a related autoinflammatory disorder.
pyrin Binding (binds) of PSTPIP1 associated with fever
2) Confidence 0.51 Published 2009 Journal PLoS ONE Section Abstract Doc Link PMC2702820 Disease Relevance 0.95 Pain Relevance 0.05
All pyrin mutants bound to PSTPIP1 and reticularized PSTPIP1 filaments in a manner similar to wildtype pyrin (Figure 6A–R).
pyrin Binding (bound) of PSTPIP1 in filaments
3) Confidence 0.51 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0.14 Pain Relevance 0
Based on these findings, it is tempting to speculate that the PSTPIP1-related protein, PSTPIP2, which lacks an SH3 domain, but also forms filaments in cells, might also interact with pyrin; PSTPIP2 has already been shown to interact with PEST phosphatases [8].
pyrin Spec (might) Binding (interact) of PSTPIP1-related in filaments
4) Confidence 0.51 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0.17 Pain Relevance 0.04
PSTPIP1, particularly the PAPA-associated mutant forms of this protein which bind pyrin with high affinity, bind to pyrin's B-box, unmasking the PyD and allowing its interaction with the PyD of ASC.
pyrin Binding (bind) of PSTPIP1
5) Confidence 0.44 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0.07 Pain Relevance 0.04
First, Shoham et al. presented a model in which PSTPIP1 binds and sequesters pyrin and showed that this interaction requires the SH3 domain of PSTPIP1 [5].
pyrin Binding (binds) of PSTPIP1 in SH3
6) Confidence 0.44 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0.09 Pain Relevance 0.05
In these latter cases, pyrin is observed either in association with both specks and PSTPIP1 filaments (Figure 9K–M) or exclusively in ASC specks (Figure 7N–P).
pyrin Binding (association) of PSTPIP1 in filaments
7) Confidence 0.44 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0 Pain Relevance 0
We show here that pyrin can not only bind to these filamentous, PSTPIP-coated membrane tubules, but can also alter their distribution.
pyrin Binding (bind) of PSTPIP in tubules
8) Confidence 0.44 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0.23 Pain Relevance 0.04
Neither of these pyrin fragments bound to PSTPIP1 filaments (Figure 5A–D).
pyrin Binding (bound) of PSTPIP1 in filaments
9) Confidence 0.44 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0 Pain Relevance 0
We also transfected cells with pyrin-myc, untagged ASC and a FLAG-tagged version of the W232A PSTPIP1 mutant that does not bind pyrin.
pyrin Neg (not) Binding (bind) of PSTPIP1 (W232A)
10) Confidence 0.44 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0.07 Pain Relevance 0
Third, and most importantly, in the presence of ASC, pyrin recruits PSTPIP1 to the ASC speck compartment, a compartment that PSTPIP1 never visits in the absence of pyrin.
pyrin Binding (recruits) of PSTPIP1
11) Confidence 0.39 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0.16 Pain Relevance 0.04
Thus, pyrin apparently recruits PSTPIP1 to the speck compartment.
pyrin Binding (recruits) of PSTPIP1
12) Confidence 0.39 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0 Pain Relevance 0
In no case does pyrin decorate PSTPIP1 filaments to the exclusion of the speck compartment.
pyrin Neg (no) Binding (decorate) of PSTPIP1 in filaments
13) Confidence 0.39 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0.05 Pain Relevance 0
Finally, we demonstrate that pyrin can recruit PSTPIP1 into aggregations (specks) of ASC, another pyrin binding protein.
pyrin Binding (aggregations) of PSTPIP1
14) Confidence 0.39 Published 2009 Journal PLoS ONE Section Abstract Doc Link PMC2702820 Disease Relevance 0.66 Pain Relevance 0.03
PSTPIP1 mutations have been shown to increase the binding affinity between PSTPIP1 and pyrin, suggesting that pyrin and PSTPIP1 are functionally linked in an unknown pathway connected to inflammation [5].
pyrin Binding (affinity) of PSTPIP1 associated with inflammation
15) Confidence 0.38 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 1.49 Pain Relevance 0.25
Thus, the SH3 domain is apparently dispensable for the interaction between pyrin and PSTPIP1.
pyrin Binding (interaction) of PSTPIP1 in SH3
16) Confidence 0.38 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0 Pain Relevance 0
PSTPIP1 mutations have been shown to increase the binding affinity between PSTPIP1 and pyrin, suggesting that pyrin and PSTPIP1 are functionally linked in an unknown pathway connected to inflammation [5].
pyrin Binding (affinity) of PSTPIP1 associated with inflammation
17) Confidence 0.38 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 1.58 Pain Relevance 0.28
To explore the effect of PAPA mutations on the PSTPIP1:pyrin interaction, we next tested whether the filaments formed by mutant forms of PSTPIP1 could be reorganized by pyrin.
pyrin Binding (interaction) of PSTPIP1 in filaments
18) Confidence 0.38 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0.15 Pain Relevance 0
The results of these analyses suggest a revised model of pyrin/PSTPIP interaction in the context of inflammatory disease.


pyrin Binding (interaction) of PSTPIP associated with inflammation and disease
19) Confidence 0.38 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0.20 Pain Relevance 0.05
The results of these analyses suggest a revised model of pyrin/PSTPIP interaction in the context of inflammatory disease.


pyrin Binding (interaction) of PSTPIP associated with inflammation and disease
20) Confidence 0.38 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0.20 Pain Relevance 0.05

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