INT249383

From wiki-pain
Jump to: navigation, search
Context Info
Confidence 0.23
First Reported 2008
Last Reported 2010
Negated 1
Speculated 0
Reported most in Body
Documents 5
Total Number 8
Disease Relevance 0.33
Pain Relevance 1.03

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

vesicle-mediated transport (Vamp2) plasma membrane (Vamp2) protein complex assembly (Vamp2)
Anatomy Link Frequency
cleavage 2
neurons 1
Vamp2 (Mus musculus)
Pain Link Frequency Relevance Heat
Spinal cord 184 97.60 Very High Very High Very High
tetrodotoxin 56 90.96 High High
Action potential 24 89.52 High High
Neurotransmitter 96 50.00 Quite Low
Calcium channel 4 24.40 Low Low
imagery 4 6.32 Low Low
Central nervous system 24 5.00 Very Low Very Low Very Low
antagonist 16 5.00 Very Low Very Low Very Low
cerebral cortex 4 5.00 Very Low Very Low Very Low
long-term potentiation 4 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Cancer 8 88.00 High High
Toxicity 4 67.12 Quite High
Disease 24 64.64 Quite High
Anaerobic Bacterial Infections 88 50.00 Quite Low
Ganglion Cysts 32 23.12 Low Low
Paralysis 28 5.00 Very Low Very Low Very Low
Targeted Disruption 24 5.00 Very Low Very Low Very Low
Infection 16 5.00 Very Low Very Low Very Low
Poisoning 8 5.00 Very Low Very Low Very Low
Injury 8 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
We previously reported that tomosyn is phosphorylated by PKA, leading to a decrease in its binding activity for VAMP-2 (Baba et al., 2005).
VAMP-2 Binding (activity) of
1) Confidence 0.23 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2568027 Disease Relevance 0 Pain Relevance 0
We previously reported that tomosyn is phosphorylated by PKA, leading to a decrease in its binding activity for VAMP-2 (Baba et al., 2005).
VAMP-2 Binding (activity) of
2) Confidence 0.18 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2568027 Disease Relevance 0 Pain Relevance 0
A structural study of tomosyn indicated that the C-terminal VAMP-like domain (VLD) of tomosyn acts as a SNARE domain that competes with VAMP-2, leading to inhibition of the formation of the SNARE complex (Pobbati et al., 2004).
VAMP-2 Binding (competes) of
3) Confidence 0.18 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2568027 Disease Relevance 0.09 Pain Relevance 0
VAMP-2 did not bind to MBP-VLD.
VAMP-2 Neg (not) Binding (bind) of
4) Confidence 0.17 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2568027 Disease Relevance 0 Pain Relevance 0
Hence, we first pre-treated spinal cord neurons with BoNT/A to cleave SNAP-25 and inhibit exocytosis [1], and then we subsequently assayed for entry of TeNT by monitoring cleavage of syb II.
syb II Binding (cleavage) of in cleavage associated with spinal cord
5) Confidence 0.12 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2991259 Disease Relevance 0.07 Pain Relevance 0.07
As BoNT/A and BoNT/E cleave SNAP-25 instead of syb II, we were able to inhibit exocytosis in neurons while still monitor the entry of TeNT through cleavage of syb II.
syb II Binding (cleavage) of in cleavage
6) Confidence 0.12 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2991259 Disease Relevance 0.05 Pain Relevance 0.13
To test this idea, we determined whether the ability of TeNT holotoxin to enter neurons and cleave syb II also depended on SV recycling.
syb II Binding (enter) of in neurons
7) Confidence 0.12 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2991259 Disease Relevance 0.06 Pain Relevance 0.39
We employed a monoclonal antibody raised against syb II (Cl. 69.1) that cannot recognize the enzymatically cleaved form of the protein.
syb II Binding (recognize) of
8) Confidence 0.12 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2991259 Disease Relevance 0.06 Pain Relevance 0.44

General Comments

This test has worked.

Personal tools
Namespaces

Variants
Actions
Navigation
Toolbox