INT204382

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Context Info
Confidence 0.53
First Reported 2007
Last Reported 2008
Negated 2
Speculated 1
Reported most in Body
Documents 5
Total Number 17
Disease Relevance 0
Pain Relevance 0.14

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

transport (Napa) vesicle-mediated transport (Napa)
Anatomy Link Frequency
vesicle 6
Napa (Mus musculus)
Pain Link Frequency Relevance Heat
addiction 4 88.64 High High
Neurotransmitter 260 64.52 Quite High
Hippocampus 13 50.80 Quite High
long-term potentiation 13 48.56 Quite Low
Pyramidal cell 13 42.32 Quite Low
Action potential 53 5.00 Very Low Very Low Very Low
cerebral cortex 13 5.00 Very Low Very Low Very Low
Nerve growth factor 13 5.00 Very Low Very Low Very Low
anesthesia 13 5.00 Very Low Very Low Very Low
antagonist 13 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Ganglion Cysts 108 5.00 Very Low Very Low Very Low
Paralysis 52 5.00 Very Low Very Low Very Low
Cancer 26 5.00 Very Low Very Low Very Low
Sprains And Strains 8 5.00 Very Low Very Low Very Low
Attention Deficit Hyperactivity Disorder 8 5.00 Very Low Very Low Very Low
Coma 4 5.00 Very Low Very Low Very Low
Toxicity 4 5.00 Very Low Very Low Very Low
Stress 4 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Tomosyn enhanced the oligomerization of the SNARE complex even in the presence of 0.5 mM TCEP (Fig.
Positive_regulation (enhanced) of SNARE Binding (oligomerization) of
1) Confidence 0.53 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2568027 Disease Relevance 0 Pain Relevance 0
S2 A, available at http://www.jcb.org/cgi/content/full/jcb.200805150/DC1), suggesting that the oligomerization of the SNARE complex was not simply caused by artificial oxidation.
Neg (not) Positive_regulation (caused) of SNARE Binding (oligomerization) of
2) Confidence 0.35 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2568027 Disease Relevance 0 Pain Relevance 0
Next, we examined the ability of tomosyn to either enhance the formation of the SNARE complex or the oligomerization of the SNARE complex in a cell-free assay system using recombinant proteins.
Spec (examined) Positive_regulation (enhance) of SNARE Spec (examined) Binding (oligomerization) of
3) Confidence 0.35 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2568027 Disease Relevance 0 Pain Relevance 0
However, this competing activity of the VLD does not explain the activity of tomosyn to enhance the oligomerization of the SNARE complex.
Positive_regulation (enhance) of SNARE Binding (oligomerization) of
4) Confidence 0.35 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2568027 Disease Relevance 0 Pain Relevance 0
In contrast, tomosyn enhanced the oligomerization of the SNARE complex in a dose-dependent manner.
Positive_regulation (enhanced) of SNARE Binding (oligomerization) of
5) Confidence 0.35 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2568027 Disease Relevance 0 Pain Relevance 0
Next, we compared the activity of tomosyn to enhance the oligomerization of the SNARE complex with that of complexin.
Positive_regulation (enhance) of SNARE Binding (oligomerization) of
6) Confidence 0.35 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2568027 Disease Relevance 0 Pain Relevance 0
Consistent with a previous study (Pabst et al., 2002), complexin did not enhance the oligomerization of the SNARE complex under reducing conditions (Fig.
Neg (not) Positive_regulation (enhance) of SNARE Neg (not) Binding (oligomerization) of
7) Confidence 0.35 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2568027 Disease Relevance 0 Pain Relevance 0
Collectively, these results indicate that tomosyn has an ability to enhance oligomerization of the SNARE complex in vitro.


Positive_regulation (enhance) of SNARE Binding (oligomerization) of
8) Confidence 0.35 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.


Positive_regulation (essential) of SNARE Binding (oligomerization) of
9) Confidence 0.35 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2568027 Disease Relevance 0 Pain Relevance 0
Therefore, these results indicate that the transmembrane domains of syntaxin-1 and VAMP-2 have the ability to facilitate the oligomerization of the SNARE complexes and that the WD-40 repeat domain of tomosyn enhances the oligomerization of the SNARE complex independently of the transmembrane domains of syntaxin-1 and VAMP-2.
Positive_regulation (enhances) of SNARE Binding (oligomerization) of
10) Confidence 0.35 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2568027 Disease Relevance 0 Pain Relevance 0
These results indicate that tomosyn enhances the oligomerization of the SNARE complex.
Positive_regulation (enhances) of SNARE Binding (oligomerization) of
11) Confidence 0.35 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2568027 Disease Relevance 0 Pain Relevance 0.03
Because tomosyn was known to inhibit the formation of the SNARE complex by competing with VAMP-2 (Fujita et al., 1998; Pobbati et al., 2004), we expected that the formation of the SNARE complex would be increased in tomosyn-deficient mice.
Positive_regulation (increased) of SNARE Binding (formation) of
12) Confidence 0.35 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2568027 Disease Relevance 0 Pain Relevance 0.03
Collectively, these results suggest that tomosyn achieves the oligomerization of the SNARE complex via both facilitation of the formation of the monomeric SNARE complex and enhancement of the oligomerization of the preassembled SNARE complex.


Positive_regulation (enhancement) of SNARE Binding (oligomerization) of
13) Confidence 0.35 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2568027 Disease Relevance 0 Pain Relevance 0
Alternatively, the T254I mutation could stabilize the cis SNARE complex such that it impedes vesicle recycling and ultimately reduces exocytosis upon repetitive nerve stimulation.


Positive_regulation (stabilize) of SNARE Binding (complex) of in vesicle
14) Confidence 0.04 Published 2007 Journal PLoS Biology Section Body Doc Link PMC1808484 Disease Relevance 0 Pain Relevance 0.04
Based on this structural analysis and modeling, we predict that the T254I mutation facilitates the formation or stability of the SNARE complex by enhancing intermolecular hydrophobic interactions among the four SNARE ?
Positive_regulation (enhancing) of SNARE Binding (interactions) of
15) Confidence 0.04 Published 2007 Journal PLoS Biology Section Body Doc Link PMC1808484 Disease Relevance 0 Pain Relevance 0.04
A syntaxin 1A threonine to isoleucine mutation is found to enhance SNARE complex formation and vesicle fusion.
Positive_regulation (enhance) of SNARE Binding (formation) of in vesicle
16) Confidence 0.04 Published 2007 Journal PLoS Biology Section Abstract Doc Link PMC1808484 Disease Relevance 0 Pain Relevance 0
These results are consistent with molecular dynamics simulations of the SNARE core complex, suggesting that T254 serves as an internal brake to dampen SNARE zippering and impede vesicle fusion, whereas I254 favors fusion by enhancing intermolecular interaction within the SNARE core complex.


Positive_regulation (enhancing) of SNARE Binding (interaction) of in vesicle
17) Confidence 0.04 Published 2007 Journal PLoS Biology Section Abstract Doc Link PMC1808484 Disease Relevance 0 Pain Relevance 0

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