INT207630

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Context Info
Confidence 0.06
First Reported 2007
Last Reported 2007
Negated 2
Speculated 0
Reported most in Body
Documents 1
Total Number 13
Disease Relevance 1.03
Pain Relevance 1.82

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

cell cycle (Calm3) cytoplasm (Nrgn)
Anatomy Link Frequency
neurons 3
brain 2
Calm3 (Mus musculus)
Nrgn (Mus musculus)
Pain Link Frequency Relevance Heat
Kinase C 273 97.96 Very High Very High Very High
Hippocampus 65 85.20 High High
cytokine 26 82.92 Quite High
depression 13 37.40 Quite Low
long-term potentiation 39 31.08 Quite Low
tolerance 39 5.00 Very Low Very Low Very Low
Spinal cord 13 5.00 Very Low Very Low Very Low
Neuritis 13 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Apoptosis 65 86.12 High High
Aging 13 81.00 Quite High
Neuroblastoma 39 75.00 Quite High
Targeted Disruption 39 67.48 Quite High
Congenital Anomalies 13 45.40 Quite Low
Depression 13 37.40 Quite Low
Cognitive Disorder 13 31.84 Quite Low
Reprotox - General 1 26 5.00 Very Low Very Low Very Low
Starvation 26 5.00 Very Low Very Low Very Low
Neuritis 13 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
On the other hand, it is noteworthy that I33Q mutant that completely inhibited the Ng's interaction with CaM, showed similar ERK activity as Ng wild type, implying that Ng/CaM interaction played little role in ERK activation.
CaM Binding (interaction) of Ng
1) Confidence 0.06 Published 2007 Journal International Journal of Biological Sciences Section Body Doc Link PMC1865092 Disease Relevance 0.07 Pain Relevance 0.25
Previous attempt to identify the proteins interacting with Ng using yeast-two-hybrid technology has demonstrated that CaM is the only major protein that interacted with Ng in vivo 13.
CaM Binding (interacted) of Ng
2) Confidence 0.06 Published 2007 Journal International Journal of Biological Sciences Section Body Doc Link PMC1865092 Disease Relevance 0.37 Pain Relevance 0.07
Because of the special properties of Ng to bind CaM in a Ca2+-sensitive way and CaM is the only protein identified to interact with Ng yeast-hybrid experiment, many studies have been focused on the roles of Ng in regulating Ca2+/CaM signaling in neurons.
CaM Binding (interact) of Ng in neurons
3) Confidence 0.06 Published 2007 Journal International Journal of Biological Sciences Section Body Doc Link PMC1865092 Disease Relevance 0 Pain Relevance 0.07
It has been known the S36A has a slightly stronger interaction with CaM than native Ng, thus it also increased the intracellular free Ca2+ concentration.
CaM Binding (interaction) of Ng
4) Confidence 0.06 Published 2007 Journal International Journal of Biological Sciences Section Body Doc Link PMC1865092 Disease Relevance 0.06 Pain Relevance 0.27
On the other hand, it is noteworthy that I33Q mutant that completely inhibited the Ng's interaction with CaM, showed similar ERK activity as Ng wild type, implying that Ng/CaM interaction played little role in ERK activation.
CaM Binding (interaction) of Ng
5) Confidence 0.05 Published 2007 Journal International Journal of Biological Sciences Section Body Doc Link PMC1865092 Disease Relevance 0.13 Pain Relevance 0.25
It has been reported that the mutation of S36A totally abolished the phosphorylation of Ng and I33Q mutation completely inhibited the interaction between Ng and CaM 13.
CaM Binding (interaction) of Ng
6) Confidence 0.05 Published 2007 Journal International Journal of Biological Sciences Section Body Doc Link PMC1865092 Disease Relevance 0 Pain Relevance 0.22
On the other hand, it is noteworthy that I33Q mutant that completely inhibited the Ng's interaction with CaM, showed similar ERK activity as Ng wild type, implying that Ng/CaM interaction played little role in ERK activation.
CaM Binding (interaction) of Ng
7) Confidence 0.05 Published 2007 Journal International Journal of Biological Sciences Section Body Doc Link PMC1865092 Disease Relevance 0.13 Pain Relevance 0.25
Neurogranin (Ng) is among the most abundant proteins known to bind calmodulin (CaM) in a Ca2+-sensitive way in the brain 1.
CaM Binding (bind) of Ng in brain
8) Confidence 0.05 Published 2007 Journal International Journal of Biological Sciences Section Body Doc Link PMC1865092 Disease Relevance 0 Pain Relevance 0.11
The mutation of Ng at S36A caused sustained increase of ERK1/2 activity, whereas the ERK1/2 activity in mutation at I33Q showed no difference compared to wild type Ng, suggesting the phosphorylation of Ng but not the CaM /Ng interaction plays an important role in ERK activation.
CaM Neg (not) Binding (interaction) of Ng
9) Confidence 0.05 Published 2007 Journal International Journal of Biological Sciences Section Abstract Doc Link PMC1865092 Disease Relevance 0.13 Pain Relevance 0.04
The mutation of Ng at S36A caused sustained increase of ERK1/2 activity, whereas the ERK1/2 activity in mutation at I33Q showed no difference compared to wild type Ng, suggesting the phosphorylation of Ng but not the CaM /Ng interaction plays an important role in ERK activation.
CaM Neg (not) Binding (interaction) of Ng
10) Confidence 0.05 Published 2007 Journal International Journal of Biological Sciences Section Abstract Doc Link PMC1865092 Disease Relevance 0.13 Pain Relevance 0.04
Neurogranin (Ng) is among the most abundant proteins known to bind calmodulin (CaM) in a Ca2+-sensitive way in the brain 1.
CaM Binding (bind) of Neurogranin in brain
11) Confidence 0.05 Published 2007 Journal International Journal of Biological Sciences Section Body Doc Link PMC1865092 Disease Relevance 0 Pain Relevance 0.11
Because of the special properties of Ng to bind CaM in a Ca2+-sensitive way and CaM is the only protein identified to interact with Ng yeast-hybrid experiment, many studies have been focused on the roles of Ng in regulating Ca2+/CaM signaling in neurons.
CaM Binding (bind) of Ng in neurons
12) Confidence 0.05 Published 2007 Journal International Journal of Biological Sciences Section Body Doc Link PMC1865092 Disease Relevance 0 Pain Relevance 0.07
Because of the special properties of Ng to bind CaM in a Ca2+-sensitive way and CaM is the only protein identified to interact with Ng yeast-hybrid experiment, many studies have been focused on the roles of Ng in regulating Ca2+/CaM signaling in neurons.
CaM Binding (interact) of Ng in neurons
13) Confidence 0.05 Published 2007 Journal International Journal of Biological Sciences Section Body Doc Link PMC1865092 Disease Relevance 0 Pain Relevance 0.07

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