INT274584

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Context Info
Confidence 0.13
First Reported 2009
Last Reported 2009
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 7
Disease Relevance 1.34
Pain Relevance 0.22

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

cytosol (PSTPIP1, PYCARD) signal transduction (PSTPIP1, PYCARD) cytoplasm (PSTPIP1, PYCARD)
oxidoreductase activity (PSTPIP1) cell adhesion (PSTPIP1) intracellular (PYCARD)
Anatomy Link Frequency
filaments 1
PSTPIP1 (Homo sapiens)
PYCARD (Homo sapiens)
Pain Link Frequency Relevance Heat
Inflammation 63 91.92 High High
Arthritis 14 61.72 Quite High
Pain 14 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Disease 70 92.24 High High
INFLAMMATION 63 91.92 High High
Fever 77 73.04 Quite High
Syndrome 63 72.72 Quite High
Acne 14 63.00 Quite High
Pyoderma Gangrenosum 14 62.60 Quite High
Arthritis 14 61.72 Quite High
Osteomyelitis 28 5.00 Very Low Very Low Very Low
Pain 14 5.00 Very Low Very Low Very Low
Adhesions 7 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
A second difference between our findings and those of earlier studies is that we find that pyrin is not sequestered away from ASC by its interaction by PSTPIP1, and does not require PSTPIP1 to interact with ASC.
PSTPIP1 Binding (interact) of ASC
1) Confidence 0.13 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0.18 Pain Relevance 0.05
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.
Mutant PSTPIP1 Binding (recruited) of ASC
2) Confidence 0.10 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0.20 Pain Relevance 0.04
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.
PSTPIP1 Binding (recruits) of ASC
3) Confidence 0.09 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0.16 Pain Relevance 0.04
Finally, we demonstrate that pyrin can recruit PSTPIP1 into aggregations (specks) of ASC, another pyrin binding protein.
PSTPIP1 Binding (aggregations) of ASC
4) Confidence 0.09 Published 2009 Journal PLoS ONE Section Abstract Doc Link PMC2702820 Disease Relevance 0.66 Pain Relevance 0.03
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).
PSTPIP1 Binding (association) of ASC in filaments
5) Confidence 0.09 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0 Pain Relevance 0
In this model, then, PSTPIP1 is required for pyrin's functional interaction with the ASC inflammasome.
PSTPIP1 Binding (interaction) of ASC
6) Confidence 0.08 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0.06 Pain Relevance 0.03
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.
PSTPIP1 Binding (interaction) of ASC
7) Confidence 0.08 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0.07 Pain Relevance 0.04

General Comments

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