INT263721

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Context Info
Confidence 0.33
First Reported 2009
Last Reported 2009
Negated 0
Speculated 1
Reported most in Body
Documents 1
Total Number 7
Disease Relevance 0
Pain Relevance 0.18

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 (Grin1, Neto1) transport (Grin1) enzyme binding (Grin1)
cytoplasm (Grin1)
Anatomy Link Frequency
tail 1
synapses 1
Grin1 (Mus musculus)
Neto1 (Mus musculus)
Pain Link Frequency Relevance Heat
Neurotransmitter 21 88.76 High High
Glutamate receptor 14 77.60 Quite High
Hippocampus 84 70.88 Quite High
long-term potentiation 182 53.84 Quite High
Glutamate 14 14.24 Low Low
nMDA receptor 63 5.00 Very Low Very Low Very Low
Pyramidal cell 28 5.00 Very Low Very Low Very Low
Central nervous system 21 5.00 Very Low Very Low Very Low
Eae 14 5.00 Very Low Very Low Very Low
tetrodotoxin 7 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Congenital Anomalies 42 29.60 Quite Low
Cognitive Disorder 56 5.00 Very Low Very Low Very Low
Convulsion 14 5.00 Very Low Very Low Very Low
Sprains And Strains 7 5.00 Very Low Very Low Very Low
Helminth Infection 7 5.00 Very Low Very Low Very Low
Influenza Virus Infection 7 5.00 Very Low Very Low Very Low
Contagious Ecthyma 7 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Removal of the cytoplasmic tail and transmembrane domain of Neto1 did not abolish the Neto1:NMDAR interaction (Figure 4B, lanes 2 and 3), suggesting that it was mediated by the ectodomain of Neto1.
NMDAR Binding (interaction) of Neto1 in tail
1) Confidence 0.33 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0
To investigate the role of Neto1 in the biology of mammalian excitatory synapses, we determined the molecular basis of the Neto1:NMDAR interaction and defined the nonredundant functions of Neto1 in synaptic plasticity, learning, and memory using Neto1 protein null mice.
NMDAR Spec (determined) Binding (interaction) of Neto1 in synapses
2) Confidence 0.31 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0.15
We next asked which NMDAR subunit mediates the Neto1:NMDAR interaction, using heterologously expressed proteins in HEK293 cells.
NMDAR Binding (interaction) of Neto1
3) Confidence 0.31 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0
These results indicate that the Neto1:NMDAR extracellular interaction is dependent on the first CUB domain of Neto1.


NMDAR Binding (interaction) of Neto1
4) Confidence 0.31 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0
Consequently, we conclude that the PSD-95-independent Neto1:NMDAR interaction is mediated through NR2 subunits, and that the first extracellular CUB domain of Neto1 is sufficient for this binding.
NMDAR Binding (interaction) of Neto1
5) Confidence 0.31 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0
These results indicate that the binding of Neto1 to PSD-95 was not required for Neto1 to interact with the NMDAR, and that Neto1 interacts with NMDARs through a PSD-95-independent mechanism.


NMDAR Binding (interact) of Neto1
6) Confidence 0.28 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0.03
Moreover, a construct expressing only the signal sequence and N-terminal CUB domain of Neto1 was sufficient to mediate the NMDAR association (Figure 4B, lane 5).
NMDAR Binding (association) of Neto1
7) Confidence 0.28 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0

General Comments

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