INT22282

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Context Info
Confidence 0.67
First Reported 1980
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 8
Total Number 9
Disease Relevance 2.82
Pain Relevance 2.12

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

mitochondrion (Chat) transferase activity, transferring acyl groups (Chat)
Anatomy Link Frequency
neurons 3
spinal cord 1
piriform cortex 1
Chat (Mus musculus)
Pain Link Frequency Relevance Heat
Spinal cord 34 99.64 Very High Very High Very High
tetrodotoxin 5 98.84 Very High Very High Very High
GABAergic 29 96.80 Very High Very High Very High
gABA 86 95.60 Very High Very High Very High
Catecholamine 7 93.20 High High
monoamine 8 91.04 High High
Hippocampus 2 85.48 High High
Glutamate 15 82.96 Quite High
amygdala 2 82.36 Quite High
Neurotransmitter 19 79.84 Quite High
Disease Link Frequency Relevance Heat
Disease 105 99.80 Very High Very High Very High
Targeted Disruption 78 99.04 Very High Very High Very High
Death 9 98.04 Very High Very High Very High
Paralysis 3 95.84 Very High Very High Very High
Amyloid Plaque 14 88.16 High High
Congenital Anomalies 10 66.08 Quite High
Ganglion Cysts 24 50.32 Quite High
Alzheimer's Dementia 28 50.00 Quite Low
Umbilical Hernia 48 41.64 Quite Low
Cleft Palate 32 41.04 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
In VAChT knockout mice the amount of the ACh-synthesizing enzyme choline acetyltransferase (ChAT) is increased at the mRNA and protein levels compared to their wild-type littermates, suggesting that the change in ChAT expression may be related to a compensatory mechanism due to the lack of ACh release [16].
Positive_regulation (increased) of choline acetyltransferase associated with targeted disruption
1) Confidence 0.67 Published 2010 Journal Mol Brain Section Body Doc Link PMC3023674 Disease Relevance 0.28 Pain Relevance 0.53
This effect, which we found to correspond to a quantitatively similar increase in the activity of choline acetyltransferase (ChAT), was completely blocked by tetrodotoxin, indicating that it was due to Na(+)-dependent depolarization.
Positive_regulation (increase) of ChAT associated with tetrodotoxin
2) Confidence 0.57 Published 1993 Journal J. Neurosci. Res. Section Abstract Doc Link 8455211 Disease Relevance 0 Pain Relevance 0.38
In association with the increase in MN number, choline acetyltransferase activity was significantly increased in both spinal cord and peripheral synaptic sites.
Positive_regulation (increased) of choline acetyltransferase in spinal cord associated with spinal cord
3) Confidence 0.57 Published 1990 Journal J. Neurobiol. Section Abstract Doc Link 2273403 Disease Relevance 0.42 Pain Relevance 0.27
ChAT+ neurons fire at lower frequencies than ChAT?
Positive_regulation (frequencies) of ChAT in neurons
4) Confidence 0.43 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2883570 Disease Relevance 0 Pain Relevance 0
Choline acetyltransferase activity rose by 64% within one week after BBX in the piriform cortex and remained elevated throughout the study.
Positive_regulation (elevated) of Choline acetyltransferase in piriform cortex
5) Confidence 0.40 Published 1980 Journal Brain Res. Section Abstract Doc Link 6250669 Disease Relevance 0 Pain Relevance 0.32
In VAChT knockout mice the amount of the ACh-synthesizing enzyme choline acetyltransferase (ChAT) is increased at the mRNA and protein levels compared to their wild-type littermates, suggesting that the change in ChAT expression may be related to a compensatory mechanism due to the lack of ACh release [16].
Positive_regulation (increased) of ChAT associated with targeted disruption
6) Confidence 0.35 Published 2010 Journal Mol Brain Section Body Doc Link PMC3023674 Disease Relevance 0.28 Pain Relevance 0.52
It is possible that the loss of IDE and neprilysin in AD brain is due to the loss of neurons that produce these two enzymes or the hypofunction of live neurons as it has been reported for choline acetyltransferase (ChAT) in AD.
Positive_regulation (reported) of choline acetyltransferase in neurons associated with disease
7) Confidence 0.16 Published 2009 Journal Mol Neurodegener Section Body Doc Link PMC2726140 Disease Relevance 0.89 Pain Relevance 0.04
It is possible that the loss of IDE and neprilysin in AD brain is due to the loss of neurons that produce these two enzymes or the hypofunction of live neurons as it has been reported for choline acetyltransferase (ChAT) in AD.
Positive_regulation (reported) of ChAT in neurons associated with disease
8) Confidence 0.16 Published 2009 Journal Mol Neurodegener Section Body Doc Link PMC2726140 Disease Relevance 0.90 Pain Relevance 0.04
At E6, CRABP-immunoreactive cells were found near the developing GCL (Fig. 4a) and a few of these cells were also immunoreactive for ChAT (Figs. 4a–c).
Positive_regulation (immunoreactive) of ChAT
9) Confidence 0.14 Published 2008 Journal BMC Dev Biol Section Body Doc Link PMC2267169 Disease Relevance 0.05 Pain Relevance 0

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