INT263685

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Context Info
Confidence 0.48
First Reported 2009
Last Reported 2009
Negated 1
Speculated 2
Reported most in Body
Documents 1
Total Number 11
Disease Relevance 0
Pain Relevance 0.65

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 (Neto1)
Anatomy Link Frequency
synapses 1
Neto1 (Mus musculus)
Pain Link Frequency Relevance Heat
Neurotransmitter 33 99.76 Very High Very High Very High
Pyramidal cell 44 96.52 Very High Very High Very High
long-term potentiation 286 95.40 Very High Very High Very High
Hippocampus 132 89.24 High High
Glutamate receptor 22 84.56 Quite High
Glutamate 22 61.08 Quite High
Central nervous system 33 47.12 Quite Low
antagonist 11 34.48 Quite Low
nMDA receptor 99 5.00 Very Low Very Low Very Low
Eae 22 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Congenital Anomalies 66 29.60 Quite Low
Cognitive Disorder 88 5.00 Very Low Very Low Very Low
Convulsion 22 5.00 Very Low Very Low Very Low
Sprains And Strains 11 5.00 Very Low Very Low Very Low
Helminth Infection 11 5.00 Very Low Very Low Very Low
Influenza Virus Infection 11 5.00 Very Low Very Low Very Low
Contagious Ecthyma 11 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
These results indicate that the Neto1:NMDAR extracellular interaction is dependent on the first CUB domain of Neto1.


Neto1 Binding (interaction) of
1) Confidence 0.48 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0
Despite the ability of Neto1 to bind to both NR2A and NR2B subunits in vitro, the differential effect of Neto1 on NR2A- versus NR2B-containing NMDARs in vivo, might be mediated by the extracellular, membrane or cytoplasmic domains of these NR2 subunits.
Neto1 Spec (might) Binding (bind) of
2) Confidence 0.37 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.
Neto1 Binding (interaction) of
3) Confidence 0.37 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0
Both Neto1 and SOL-1 interact with ionotropic subunits by an extracellular CUB domain.
Neto1 Binding (interact) of
4) Confidence 0.37 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0.12
Because Neto1, SOL-1, and LEV-10 are associated with neurotransmitter receptors of different classes, our work suggests that a critical interaction with a CUB domain-containing protein may be a general characteristic of ligand-gated ion channels throughout nature.
Neto1 Binding (associated) of associated with neurotransmitter
5) Confidence 0.37 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0.21
Despite the ability of Neto1 to bind to both NR2A and NR2B subunits in vitro, the differential effect of Neto1 on NR2A- versus NR2B-containing NMDARs in vivo, might be mediated by the extracellular, membrane or cytoplasmic domains of these NR2 subunits.
Neto1 Spec (might) Binding (bind) of
6) Confidence 0.37 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0
Collectively, these findings indicate that lack of Neto1 does not alter the total surface expression of NMDARs, but rather decreases the targeting or stability of NR2A-containing NMDARs at synapses.
Neto1 Neg (lack) Binding (lack) of in synapses
7) Confidence 0.37 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0.13
As predicted both by the interaction between PSD-95 and the NR2 subunits of the NMDAR [28], and by the binding of Neto1 to PSD-95 described above, we found that Neto1 was co-immunoprecipitated by anti-NR1 antibodies from lysates of cells co-expressing Neto1, PSD-95, NR1, and NR2B (Figure 4A, lane 1).
Neto1 Binding (binding) of
8) Confidence 0.37 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0.04
We next asked which NMDAR subunit mediates the Neto1:NMDAR interaction, using heterologously expressed proteins in HEK293 cells.
Neto1 Binding (interaction) of
9) Confidence 0.36 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0
Because PSD-95 is a prominent NMDAR scaffold protein [25,26], we asked whether Neto1 associates with NMDARs.
Neto1 Binding (associates) of
10) Confidence 0.36 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0
We investigated the complement C1r/C1s, Uegf, Bmp1 (CUB) domain protein neuropilin tolloid-like 1 (Neto1) [6,7], which we have discovered to be an NMDAR-associated protein [8].
protein neuropilin tolloid-like 1 Binding (complement) of
11) Confidence 0.33 Published 2009 Journal PLoS Biology Section Body Doc Link PMC2652390 Disease Relevance 0 Pain Relevance 0.16

General Comments

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