INT238088

From wiki-pain
(Difference between revisions)
Jump to: navigation, search
(Generated page)
 

Latest revision as of 03:39, 23 September 2012

Context Info
Confidence 0.04
First Reported 2008
Last Reported 2010
Negated 1
Speculated 0
Reported most in Body
Documents 6
Total Number 8
Disease Relevance 2.35
Pain Relevance 2.75

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

cytosol (GRIP1) endoplasmic reticulum (GRIP1) cytoplasmic membrane-bounded vesicle (GRIP1)
plasma membrane (GRIP1) intracellular (GRIP1)
Anatomy Link Frequency
cleavage 1
GRIP1 (Homo sapiens)
Pain Link Frequency Relevance Heat
Glutamate receptor 49 99.98 Very High Very High Very High
Kinase C 73 99.50 Very High Very High Very High
metalloproteinase 17 96.76 Very High Very High Very High
Pain 44 96.36 Very High Very High Very High
nMDA receptor 58 95.64 Very High Very High Very High
Dorsal horn neuron 24 93.68 High High
Lasting pain 24 91.32 High High
Inflammation 36 90.72 High High
Neuropathic pain 16 86.08 High High
IPN 36 85.08 High High
Disease Link Frequency Relevance Heat
Nociception 104 94.44 High High
Pain 36 91.32 High High
INFLAMMATION 36 90.72 High High
Neuropathic Pain 16 86.08 High High
Inflammatory Pain 36 85.08 High High
Hyperalgesia 20 69.12 Quite High
Motor Neuron Diseases 4 66.12 Quite High
Disease 5 65.12 Quite High
Neurodegenerative Disease 4 64.56 Quite High
Targeted Disruption 37 56.40 Quite High

[edit] Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
The phosphorylation of GluR2 subunit at Serine880 by PKC may lead to disrupt the interaction between GluR2 and GRIP and follow by GluR2 internalization.
GRIP Binding (interaction) of associated with kinase c
1) Confidence 0.04 Published 2010 Journal Mol Pain Section Body Doc Link PMC2823608 Disease Relevance 0.60 Pain Relevance 0.50
This phosphorylation of GluR2 on Serine880 may further impede the affinity of GluR2 for GRIP, release GluR2 from GRIP-GluR2 complex and finally lead to the internalization of GluR2 subunits.
GRIP Binding (complex) of
2) Confidence 0.04 Published 2010 Journal Mol Pain Section Body Doc Link PMC2823608 Disease Relevance 0.33 Pain Relevance 0.21
AMPA receptor GluR2 subunit may bind to cellular partner proteins, such as glutamate receptor interacting protein (GRIP) and this signal protein interacting with C-Kinase (PICK1), which plays an important role in the synaptic GluR2 trafficking [43,44].
GRIP Binding (interacting) of associated with glutamate receptor
3) Confidence 0.04 Published 2010 Journal Mol Pain Section Body Doc Link PMC2823608 Disease Relevance 0.32 Pain Relevance 0.56
It subsequently disrupted the binding of GluR2 subunits to synaptic anchoring protein (GRIP) and result in a switch of GluR2-containing AMPA receptors to GluR2-lacking AMPA receptors.
GRIP Binding (binding) of
4) Confidence 0.04 Published 2010 Journal Mol Pain Section Body Doc Link PMC2823608 Disease Relevance 0.95 Pain Relevance 0.67
They observed an interaction of Tmub1 and GRIP in HEK293 cells, but not in a yeast two-hybrid assay.
GRIP Neg (not) Binding (interaction) of
5) Confidence 0.03 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2889838 Disease Relevance 0.05 Pain Relevance 0.13
The authors suggested that this process may be mediated by the interaction of GRIP and Tmub1/HOPS.
GRIP Binding (interaction) of
6) Confidence 0.03 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2889838 Disease Relevance 0.06 Pain Relevance 0.14
It is possible that the interaction of Tmub1 with GluR2-GRIP is indirect and requires another mediator.
GRIP Binding (indirect) of
7) Confidence 0.02 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2889838 Disease Relevance 0.06 Pain Relevance 0.10
Interestingly, it was shown recently that two proteins (ABP and GRIP) which interact with the carboxy-terminus of AMPA receptors, bind to the membrane-type 5 matrix metalloproteinase (MT5-MMP), thereby directing MT5-MMP to growth cones and synaptic sites in neurons, where the proteolytic activity of this protein may be involved in remodelling of synapses by cleavage of cadherins and matrix proteins [10].
GRIP Binding (interact) of in cleavage associated with metalloproteinase
8) Confidence 0.02 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2443283 Disease Relevance 0 Pain Relevance 0.44

[edit] General Comments

This test has worked.

Personal tools
Namespaces

Variants
Actions
Navigation
Toolbox