INT63923

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Context Info
Confidence 0.47
First Reported 1996
Last Reported 2010
Negated 2
Speculated 0
Reported most in Body
Documents 4
Total Number 10
Disease Relevance 6.28
Pain Relevance 1.19

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 (Mapt) cytoskeleton (Mapt) nucleus (Mapt)
enzyme binding (Mapt) cytoplasm (Mapt)
Anatomy Link Frequency
neurons 1
adrenal glands 1
neuropil 1
Mapt (Mus musculus)
Pain Link Frequency Relevance Heat
Endogenous opioid 1 98.82 Very High Very High Very High
Inflammation 29 97.84 Very High Very High Very High
narcan 2 97.68 Very High Very High Very High
Antinociceptive 3 96.98 Very High Very High Very High
qutenza 2 93.12 High High
antinociception 2 87.96 High High
Analgesic 2 78.24 Quite High
antagonist 2 73.80 Quite High
Hippocampus 32 73.60 Quite High
Morphine 1 67.80 Quite High
Disease Link Frequency Relevance Heat
Targeted Disruption 111 99.74 Very High Very High Very High
Tauopathy 182 99.56 Very High Very High Very High
Death 85 98.76 Very High Very High Very High
Stress 34 98.52 Very High Very High Very High
Alzheimer's Dementia 230 98.20 Very High Very High Very High
INFLAMMATION 36 97.84 Very High Very High Very High
Nociception 3 91.36 High High
Cognitive Disorder 65 89.20 High High
Disease 288 86.80 High High
Sclerosis 14 81.72 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
This confirms our observations in transgenic mice that show aggregation of Tau leading to Tauopathy in somata and neuropil, but not accompanied by marked neurodegeneration [25, 26, 36].
Tau Neg (not) Binding (aggregation) of in neuropil associated with targeted disruption and tauopathy
1) Confidence 0.47 Published 2010 Journal International Journal of Alzheimer's Disease Section Body Doc Link PMC2938448 Disease Relevance 0.52 Pain Relevance 0
Tau binds to and stabilizes microtubules and promotes microtubule assembly.
Tau Binding (binds) of
2) Confidence 0.47 Published 2006 Journal Orphanet J Rare Dis Section Body Doc Link PMC1563447 Disease Relevance 0.17 Pain Relevance 0.03
Tau stabilizes microtubules through binding and is essential to the integrity of axonal transport [48].
Tau Binding (binding) of
3) Confidence 0.47 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2866668 Disease Relevance 0.29 Pain Relevance 0.07
Clearly, the viral models comply with the transgenic models that aggregation of Tau and neurodegeneration are not closely linked.
Tau Binding (aggregation) of associated with targeted disruption
4) Confidence 0.47 Published 2010 Journal International Journal of Alzheimer's Disease Section Body Doc Link PMC2938448 Disease Relevance 0.73 Pain Relevance 0
The inherent conclusion must be that microtubule binding of protein Tau is essentially involved in the neurotoxic degenerative mechanism.
Tau Binding (microtubule binding of protein) of
5) Confidence 0.36 Published 2010 Journal International Journal of Alzheimer's Disease Section Body Doc Link PMC2938448 Disease Relevance 0.20 Pain Relevance 0.03
Its antinociceptive effect was insensitive to naloxone, suggesting the lack of involvement of endogenous opioid, was not modulated by adrenal glands and does not involve interaction with the L-arginine-nitric oxide pathway, activation of alpha-1 adrenoceptors or tau-aminobutyric acidB receptors, but requires, at least in part, the serotoninergic pathway.
tau Neg (not) Binding (interaction) of in adrenal glands associated with endogenous opioid, narcan and antinociceptive
6) Confidence 0.36 Published 1996 Journal J. Pharmacol. Exp. Ther. Section Abstract Doc Link 8764364 Disease Relevance 0.25 Pain Relevance 1.01
We proposed that neurons affected by Tauopathy can either engage in aggregation of Tau and thereby try to decrease the toxic species and hope to survive, or to enter the “path to death” by failing to aggregate protein Tau [11].
Tau Binding (aggregation) of in neurons associated with tauopathy and death
7) Confidence 0.35 Published 2010 Journal International Journal of Alzheimer's Disease Section Body Doc Link PMC2938448 Disease Relevance 0.66 Pain Relevance 0
These pathways obligatory involve kinases such as GSK3 [25, 26] that contribute, directly or indirectly to the phosphorylation of Tau at residues that affect its binding to microtubuli.
Tau Binding (binding) of
8) Confidence 0.35 Published 2010 Journal International Journal of Alzheimer's Disease Section Body Doc Link PMC2938448 Disease Relevance 1.14 Pain Relevance 0
In this concept, the aggregation of Tau acts as the “escape from cell death pathway”.
Tau Binding (aggregation) of associated with death
9) Confidence 0.35 Published 2010 Journal International Journal of Alzheimer's Disease Section Body Doc Link PMC2938448 Disease Relevance 0.72 Pain Relevance 0.05
The genetic data imply that deranged Tau-microtubule interactions, caused either directly by the mutation, by phosphorylation, by increased absolute or by disturbed relative concentrations of Tau, all can contribute or even be sufficient to cause neurodegeneration in primary Tauopathies, that is, in the absence of amyloid pathology.
Tau-microtubule Binding (interactions) of associated with tauopathy and alzheimer's dementia
10) Confidence 0.12 Published 2010 Journal International Journal of Alzheimer's Disease Section Body Doc Link PMC2938448 Disease Relevance 1.61 Pain Relevance 0

General Comments

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