INT238091

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Context Info
Confidence 0.00
First Reported 2008
Last Reported 2008
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 2
Disease Relevance 0
Pain Relevance 0.98

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

plasma membrane (GRIP1, Mmp24) cytosol (GRIP1) peptidase activity (Mmp24)
extracellular region (Mmp24) proteinaceous extracellular matrix (Mmp24) endoplasmic reticulum (GRIP1)
Anatomy Link Frequency
cleavage 2
GRIP1 (Homo sapiens)
Mmp24 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
metalloproteinase 34 100.00 Very High Very High Very High
nMDA receptor 84 95.64 Very High Very High Very High
Spinal cord 34 79.60 Quite High
Glutamate receptor 4 59.72 Quite High
agonist 2 5.00 Very Low Very Low Very Low
Kinase C 2 5.00 Very Low Very Low Very Low
Pain 2 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Adhesions 6 42.48 Quite Low
Death 6 5.00 Very Low Very Low Very Low
Apoptosis 4 5.00 Very Low Very Low Very Low
Immunization 2 5.00 Very Low Very Low Very Low
Pain 2 5.00 Very Low Very Low Very Low
Sprains And Strains 2 5.00 Very Low Very Low Very Low
Middle Cerebral Artery Infarction 2 5.00 Very Low Very Low Very Low
Brain Disease 2 5.00 Very Low Very Low Very Low
Disease 2 5.00 Very Low Very Low Very Low
Injury 2 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
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 (bind) of MT5-MMP in cleavage associated with metalloproteinase
1) Confidence 0.00 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2443283 Disease Relevance 0 Pain Relevance 0.49
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 (bind) of membrane-type 5 matrix metalloproteinase in cleavage associated with metalloproteinase
2) Confidence 0.00 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2443283 Disease Relevance 0 Pain Relevance 0.49

General Comments

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