INT238585

From wiki-pain
Jump to: navigation, search
Context Info
Confidence 0.47
First Reported 2008
Last Reported 2008
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 6
Disease Relevance 0.06
Pain Relevance 0.31

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

Golgi apparatus (EPB41) plasma membrane (EPB41) nucleus (EPB41)
protein complex (EPB41) cytoplasm (EPB41)
Anatomy Link Frequency
spine 2
SH3 1
EPB41 (Homo sapiens)
Pain Link Frequency Relevance Heat
tetrodotoxin 60 87.80 High High
Calcium channel 12 78.48 Quite High
Neurotransmitter 6 20.56 Low Low
GABAergic 6 11.20 Low Low
cerebral cortex 18 5.00 Very Low Very Low Very Low
Glutamate receptor 18 5.00 Very Low Very Low Very Low
midbrain 12 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Adhesions 36 60.52 Quite High
Targeted Disruption 36 38.16 Quite Low
Cleft Palate 12 5.00 Very Low Very Low Very Low
Myelodysplastic Syndromes 6 5.00 Very Low Very Low Very Low
Aids-related Complex 6 5.00 Very Low Very Low Very Low
Apoptosis 6 5.00 Very Low Very Low Very Low
Stroke 6 5.00 Very Low Very Low Very Low
Cytomegalovirus Infection 6 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
From the N terminus to the C terminus, the CASK protein consists of calcium/calmodulin-dependent protein kinase (CaMK)–like, L27A, L27B, PDZ, SH3, protein 4.1–binding, and guanylate kinase–like domains.
protein 4.1 Binding (binding) of in SH3
1) Confidence 0.47 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0.06 Pain Relevance 0
Because SUMOylation of CASK regulates the interaction between CASK and protein 4.1 and because the interaction with protein 4.1 is required for CASK function in spinogenesis, we then investigated whether CASK SUMOylation modulates spine formation.
protein 4.1 Binding (interaction) of in spine
2) Confidence 0.36 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0 Pain Relevance 0.24
We then wondered whether the CASK protein 4.1–binding site is also required for spinogenesis.
protein 4.1 Binding (binding) of
3) Confidence 0.36 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0 Pain Relevance 0
Interactions via the PDZ domain and protein 4.1–binding site are involved in CASK function in spine formation
protein 4.1 Binding (Interactions) of in spine
4) Confidence 0.36 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0 Pain Relevance 0
Because SUMOylation usually modifies target protein–protein interaction, distribution, or activity, we wondered whether CASK is SUMOylated and whether CASK SUMOylation affects the interaction between CASK and protein 4.1 and thus regulates the function of CASK in spinogenesis.
protein 4.1 Binding (interaction) of
5) Confidence 0.36 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0 Pain Relevance 0
We also identified SUMOylation as a posttranslational modification of CASK that regulates the interaction between CASK and protein 4.1 and, thus, modulates spinogenesis.
protein 4.1 Binding (interaction) of
6) Confidence 0.35 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2447900 Disease Relevance 0 Pain Relevance 0.07

General Comments

This test has worked.

Personal tools
Namespaces

Variants
Actions
Navigation
Toolbox