INT274602

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Context Info
Confidence 0.17
First Reported 2009
Last Reported 2009
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 7
Disease Relevance 0.25
Pain Relevance 0.07

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

endoplasmic reticulum (BFAR) structural molecule activity (BFAR)
Anatomy Link Frequency
filaments 2
BFAR (Homo sapiens)
Pain Link Frequency Relevance Heat
Inflammation 63 84.24 Quite High
Pain 14 5.00 Very Low Very Low Very Low
Arthritis 14 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
INFLAMMATION 63 84.24 Quite High
Disease 70 55.44 Quite High
Syndrome 63 53.52 Quite High
Fever 77 46.56 Quite Low
Osteomyelitis 28 30.72 Quite Low
Pain 14 5.00 Very Low Very Low Very Low
Arthritis 14 5.00 Very Low Very Low Very Low
Acne 14 5.00 Very Low Very Low Very Low
Pyoderma Gangrenosum 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
In the presence of full length PSTPIP1, the protein containing only the F-BAR domain (FCH-X-CC) is able to bind to formed filaments, but the uncharacterized “Y” region between the coiled coil and the SH3 domain appears to be additionally required for the generation of filaments (Figure 2).
BAR Binding (bind) of in filaments
1) Confidence 0.17 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0.11 Pain Relevance 0.03
The F-BAR region, encompassing the FCH and the CC, was able bind to filaments formed by full-length PSTPIP1 (Figure 2B–D).
BAR Binding (bind) of in filaments
2) Confidence 0.13 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0 Pain Relevance 0
Indeed, the homologous F-BAR domain of CIP4 interacts with microtubules [14] and the related N-BAR family member, amphiphysin, interacts with a linker protein (CLIP-170) that binds to microtubules [29].
BAR Binding (binds) of
3) Confidence 0.13 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0 Pain Relevance 0
Indeed, the homologous F-BAR domain of CIP4 interacts with microtubules [14] and the related N-BAR family member, amphiphysin, interacts with a linker protein (CLIP-170) that binds to microtubules [29].
BAR Binding (binds) of
4) Confidence 0.13 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0 Pain Relevance 0
Taken together, these data confirm that PSTPIP1 shares the lipid membrane-binding properties of several other F-BAR domain-containing proteins, a property that is not affected by pyrin binding.


BAR Binding (binding) of
5) Confidence 0.13 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0.06 Pain Relevance 0
Indeed, the F-BAR domains of both PSTPIP1 and PSTPIP2 can bind to artificial liposomes containing phosphatidyl inositol (4,5) bisphosphate (PI(4,5)P2) with high affinity [19].
BAR Binding (bind) of
6) Confidence 0.12 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0 Pain Relevance 0
It will be important to determine whether PSTPIP1 binds directly to microtubules, like the related F-BAR protein, CIP4 [14], or whether the interaction is via an intermediate microtubule binding protein, as in the case of amphiphysin [29].
F-BAR protein Binding (binds) of
7) Confidence 0.11 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0.08 Pain Relevance 0.04

General Comments

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