INT234091

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Context Info
Confidence 0.37
First Reported 2008
Last Reported 2008
Negated 0
Speculated 0
Reported most in Body
Documents 13
Total Number 15
Disease Relevance 0.24
Pain Relevance 0.86

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

endosome (Snap25) plasma membrane (Snap25) cytoplasm (Snap25)
Anatomy Link Frequency
plasma 2
brain 1
Snap25 (Mus musculus)
Pain Link Frequency Relevance Heat
Neurotransmitter 203 99.72 Very High Very High Very High
Calcium channel 24 99.20 Very High Very High Very High
Action potential 42 93.08 High High
GABAergic 136 89.28 High High
Pyramidal cell 45 77.20 Quite High
Hippocampus 48 74.56 Quite High
Catecholamine 11 50.56 Quite High
Thalamus 12 49.68 Quite Low
Nerve growth factor 8 41.00 Quite Low
anesthesia 12 36.24 Quite Low
Disease Link Frequency Relevance Heat
Schizophrenia 21 87.76 High High
Ganglion Cysts 64 76.16 Quite High
Sprains And Strains 9 40.40 Quite Low
Congenital Anomalies 6 34.40 Quite Low
Depression 3 14.12 Low Low
Convulsion 39 5.00 Very Low Very Low Very Low
Targeted Disruption 33 5.00 Very Low Very Low Very Low
Cognitive Disorder 24 5.00 Very Low Very Low Very Low
Cancer 17 5.00 Very Low Very Low Very Low
Attention Deficit Hyperactivity Disorder 15 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
The different stability of SNARE complexes found in neo-excised SNAP-25b deficient mutants compared to WT mice (Figure 2E) and that SNAP-25b demonstrates an increased association with plasma membrane fractions compared to SNAP-25a (see Text S1, Figure S2) suggest that SNAP-25a and SNAP-25b are differently associated with SNARE complexes close to, or immediately upstream of fusion.
SNAP-25b Binding (associated) of in plasma
1) Confidence 0.37 Published 2008 Journal PLoS Genetics Section Body Doc Link PMC2581893 Disease Relevance 0 Pain Relevance 0.08
The different stability of SNARE complexes found in neo-excised SNAP-25b deficient mutants compared to WT mice (Figure 2E) and that SNAP-25b demonstrates an increased association with plasma membrane fractions compared to SNAP-25a (see Text S1, Figure S2) suggest that SNAP-25a and SNAP-25b are differently associated with SNARE complexes close to, or immediately upstream of fusion.
SNAP-25a Binding (associated) of in plasma
2) Confidence 0.37 Published 2008 Journal PLoS Genetics Section Body Doc Link PMC2581893 Disease Relevance 0 Pain Relevance 0.08
At PN14, SNAP-25b levels were five times higher than SNAP-25a in WT mice, heterozygous neo-containing mutants had equal amounts of both SNAP-25 mRNA isoforms, while homozygous neo-containing SNAP-25b deficient mutants only expressed SNAP-25a (Figure 1C).
SNAP-25a Binding (higher) of
3) Confidence 0.37 Published 2008 Journal PLoS Genetics Section Body Doc Link PMC2581893 Disease Relevance 0 Pain Relevance 0
-actin levels could be taken as a reference to normalize SNAP-25 transcript levels between these brain regions.
SNAP-25 Binding (normalize) of in brain
4) Confidence 0.37 Published 2008 Journal BMC Neurosci Section Body Doc Link PMC2600647 Disease Relevance 0 Pain Relevance 0
Previous studies have shown that SNAP-25 is associated with N and P/Q type voltage gated calcium channels [for review, see ref. [6]], and specifically impedes calcium currents through P/Q type channels activated in response to action potential-like stimuli [7].
SNAP-25 Binding (associated) of associated with action potential and calcium channel
5) Confidence 0.36 Published 2008 Journal BMC Neurosci Section Body Doc Link PMC2600647 Disease Relevance 0 Pain Relevance 0.16
In addition to a well-documented role in membrane fusion for neuroexocytosis and neurotransmitter release, the t-SNAREs SNAP-25 and syntaxin 1 also associate with voltage-gated calcium channels (VGCCs) where they are thought to modulate steady-state inactivation of channel opening thereby regulating calcium currents in response to membrane depolarization [see ref. [6] for review].
t-SNAREs SNAP-25 Binding (associate) of associated with neurotransmitter and calcium channel
6) Confidence 0.31 Published 2008 Journal BMC Neurosci Section Body Doc Link PMC2600647 Disease Relevance 0 Pain Relevance 0.33
In addition, we did confirm that dysbindin binds to snapin (unpublished data), which is known to bind SNAP25 (Buxton et al., 2003; Ilardi et al., 1999).


SNAP25 Binding (bind) of
7) Confidence 0.26 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2396815 Disease Relevance 0.09 Pain Relevance 0.12
S5 shows the effect of the PKA-catalyzed phosphorylation of tomosyn on the oligomerization of the SNARE complex and binding of SNAP-25 to the WD-40 repeat domain of tomosyn.


SNAP-25 Binding (binding) of
8) Confidence 0.22 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2568027 Disease Relevance 0 Pain Relevance 0
Assay for the binding of syntaxin-1 or SNAP-25 to tomosyn
SNAP-25 Binding (binding) of
9) Confidence 0.22 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2568027 Disease Relevance 0 Pain Relevance 0
Indeed, SNAP-25 bound the same WD-40 repeat domain encompassing Frgs. 1 and 2 as syntaxin-1 (Fig.
SNAP-25 Binding (bound) of
10) Confidence 0.21 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2568027 Disease Relevance 0.15 Pain Relevance 0.10
Different affinities for SNAP-25 and syntaxin-1 between the N-terminal WD-40 repeat domain and the C-terminal VLD
SNAP-25 Binding (affinities) of
11) Confidence 0.21 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2568027 Disease Relevance 0 Pain Relevance 0
VAMP-2 did not affect the binding of syntaxin-1 and SNAP-25 to MBP-VLD.
SNAP-25 Binding (binding) of
12) Confidence 0.21 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2568027 Disease Relevance 0 Pain Relevance 0
Syntaxin-1 or SNAP-25 bound to MBP-tomosyn-?
SNAP-25 Binding (bound) of
13) Confidence 0.21 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2568027 Disease Relevance 0 Pain Relevance 0
Syntaxin-1 and SNAP-25 each enhanced the binding of the other to MBP-VLD by threefold, presumably reflecting the formation of a SNARE complex–like structure.
SNAP-25 Binding (binding) of
14) Confidence 0.21 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2568027 Disease Relevance 0 Pain Relevance 0
These results indicate that the tomosyn-enhanced oligomerization of the SNARE complexes is not an artifact caused by oxidative cross-linking of SNAP-25 and that the intact structure of SNAP-25 is essential for the oligomerization of the SNARE complex.


SNAP-25 Binding (linking) of
15) Confidence 0.21 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2568027 Disease Relevance 0 Pain Relevance 0

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