INT102284

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Context Info
Confidence 0.27
First Reported 2002
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 5
Total Number 6
Disease Relevance 1.79
Pain Relevance 3.01

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, Grin2a) signal transduction (Grin2a) locomotion (Grin2a)
enzyme binding (Grin1) cytoplasm (Grin1)
Anatomy Link Frequency
neurons 1
Grin1 (Rattus norvegicus)
Grin2a (Rattus norvegicus)
Pain Link Frequency Relevance Heat
nMDA receptor 96 100.00 Very High Very High Very High
Hippocampus 13 98.08 Very High Very High Very High
depression 103 94.96 High High
amygdala 36 93.12 High High
long-term potentiation 148 93.04 High High
Pain 21 89.52 High High
Glutamate receptor 6 87.12 High High
antagonist 26 86.32 High High
central sensitization 1 85.84 High High
Lasting pain 2 83.84 Quite High
Disease Link Frequency Relevance Heat
Depression 103 94.96 High High
Pain 21 89.52 High High
Anaerobic Bacterial Infections 10 88.76 High High
Anxiety Disorder 47 87.72 High High
Injury 18 83.84 Quite High
Neurodegenerative Disease 2 80.00 Quite High
Cv Unclassified Under Development 30 76.88 Quite High
Hypoxia 6 75.92 Quite High
Drug Induced Neurotoxicity 2 68.40 Quite High
Arthritis 15 64.32 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Immunofluorescence with an antibody that recognized NR1 and another that recognized NR2A and NR2B showed that NR1 and NR2B colocalized in 90% of DRG neurons, including most A-fibers (identified by the presence of neurofilament 200 kDa).
NR1 Binding (recognized) of NR2A in neurons
1) Confidence 0.27 Published 2002 Journal J. Comp. Neurol. Section Abstract Doc Link 11954032 Disease Relevance 0.08 Pain Relevance 0.25
Structurally, NMDA receptors are hetero-oligomeric proteins formed by obligatory NMDA receptor 1 subunit (NR1) interacting with NMDA receptor 2A-2D subunits (NR2A-D), conferring functional variability (Monyer et al., 1992; Ishii et al., 1993).
NR1 Binding (interacting) of NR2A associated with nmda receptor
2) Confidence 0.14 Published 2010 Journal Anatomy & Cell Biology Section Body Doc Link PMC3015038 Disease Relevance 0.46 Pain Relevance 0.59
Structurally, NMDA receptors are hetero-oligomeric proteins formed by obligatory NMDA receptor 1 subunit (NR1) interacting with NMDA receptor 2A-2D subunits (NR2A-D), conferring functional variability (Monyer et al., 1992; Ishii et al., 1993).
NMDA receptor 1 subunit Binding (interacting) of NR2A associated with nmda receptor
3) Confidence 0.14 Published 2010 Journal Anatomy & Cell Biology Section Body Doc Link PMC3015038 Disease Relevance 0.46 Pain Relevance 0.60
This study is based on using NMDAR blockers with specificity for either NR2A- or NR2B-containing heteromers.
NMDAR Binding (specificity) of NR2A
4) Confidence 0.14 Published 2007 Journal BMC Neurosci Section Body Doc Link PMC1959237 Disease Relevance 0.33 Pain Relevance 0.50
Functional NMDA receptors are heteromeric assemblies of NR1 with NR2A-D or NR3A, B subunits.
NR1 Binding (assemblies) of NR2A associated with nmda receptor
5) Confidence 0.07 Published 2009 Journal Mol Pain Section Abstract Doc Link PMC2679723 Disease Relevance 0.37 Pain Relevance 0.79
Functional NMDAR has a combination of NR1 subunit and at least one of NR2 subunits (A-D).
NR1 subunit Binding (combination) of NR2
6) Confidence 0.04 Published 2008 Journal Mol Brain Section Body Doc Link PMC2570668 Disease Relevance 0.09 Pain Relevance 0.29

General Comments

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