INT87156

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Context Info
Confidence 0.40
First Reported 2000
Last Reported 2007
Negated 0
Speculated 0
Reported most in Abstract
Documents 8
Total Number 8
Disease Relevance 2.48
Pain Relevance 4.80

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

cytoskeleton (Marcks) cytoplasm (Marcks)
Anatomy Link Frequency
plasma 1
nerve 1
Marcks (Rattus norvegicus)
Pain Link Frequency Relevance Heat
Kinase C 90 99.84 Very High Very High Very High
Neuropathic pain 20 99.82 Very High Very High Very High
Inflammation 15 99.44 Very High Very High Very High
IPN 5 99.02 Very High Very High Very High
Spinal cord 15 98.76 Very High Very High Very High
Pain 15 98.58 Very High Very High Very High
antagonist 4 97.64 Very High Very High Very High
opioid receptor 4 97.16 Very High Very High Very High
Neurotransmitter 5 95.60 Very High Very High Very High
Dynorphin 9 93.92 High High
Disease Link Frequency Relevance Heat
Neuropathic Pain 20 99.82 Very High Very High Very High
INFLAMMATION 10 99.44 Very High Very High Very High
Inflammatory Pain 5 99.02 Very High Very High Very High
Pain 5 84.52 Quite High
Nash(non-alcoholic Steatohepatitis) 12 5.00 Very Low Very Low Very Low
Cognitive Disorder 1 5.00 Very Low Very Low Very Low
Aging 1 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Since the function of MARCKS is regulated by phosphorylation at multiple sites, here we examined the involvement of Rho-kinase in relation to phosphorylation of MARCKS at Ser159 in inflammatory and neuropathic pain by H-1152.
Phosphorylation (phosphorylation) of MARCKS associated with inflammation and neuropathic pain
1) Confidence 0.40 Published 2005 Journal Neuroscience Section Abstract Doc Link 15708490 Disease Relevance 0.51 Pain Relevance 0.57
Taken together, the present study demonstrates that Rho-kinase is involved in inflammatory pain and the maintenance of neuropathic pain through phosphorylation of MARCKS at Ser159.
Phosphorylation (phosphorylation) of MARCKS associated with ipn and neuropathic pain
2) Confidence 0.40 Published 2005 Journal Neuroscience Section Abstract Doc Link 15708490 Disease Relevance 0.60 Pain Relevance 0.74
A phosphorylation-site specific antibody against Ser159-phospho-MARCKS (pS159-Mar-Ab) revealed that MARCKS is phosphorylated at Ser159 by Rho-kinase and that its phosphorylation is inhibited by the Rho-kinase specific inhibitor H-1152.
Phosphorylation (phosphorylated) of MARCKS
3) Confidence 0.40 Published 2005 Journal Neuroscience Section Abstract Doc Link 15708490 Disease Relevance 0.42 Pain Relevance 0.46
Involvement of Rho-kinase in inflammatory and neuropathic pain through phosphorylation of myristoylated alanine-rich C-kinase substrate (MARCKS).
Phosphorylation (phosphorylation) of MARCKS associated with inflammation and neuropathic pain
4) Confidence 0.40 Published 2005 Journal Neuroscience Section Title Doc Link 15708490 Disease Relevance 0.47 Pain Relevance 0.78
MARCKS is normally associated with the plasma membrane and translocates to the cytoplasm on phosphorylation by PKC and/or CaM binding (Graff et al. 1989; Arbuzova et al. 2002).
Phosphorylation (phosphorylation) of MARCKS in plasma associated with kinase c
5) Confidence 0.37 Published 2007 Journal Journal of Neurochemistry Section Body Doc Link PMC2658029 Disease Relevance 0 Pain Relevance 0.38
Phosphorylation of MARCKS at Ser159 was detected in the spinal cord by pS159-Mar-Ab and the level of phosphorylation increased in the superficial layer after nerve transection.
Phosphorylation (Phosphorylation) of MARCKS in nerve associated with spinal cord
6) Confidence 0.35 Published 2005 Journal Neuroscience Section Abstract Doc Link 15708490 Disease Relevance 0.48 Pain Relevance 0.81
In PMF-exposed nuclei, nuclear protein kinase C (PKC) activity was followed by measuring the phosphorylation rate of the acrylodan-labeled MARCKS peptide.
Phosphorylation (phosphorylation) of MARCKS peptide
7) Confidence 0.15 Published 2000 Journal Cardiovasc. Res. Section Body Doc Link 10728432 Disease Relevance 0 Pain Relevance 0
Nuclei isolated from undifferentiated cells were able to phosphorylate the acrylodan-labeled MARCKS peptide, a high-affinity fluorescent PKC substrate.
Phosphorylation (phosphorylate) of MARCKS peptide associated with kinase c
8) Confidence 0.01 Published 2003 Journal Circ. Res. Section Abstract Doc Link 12623878 Disease Relevance 0 Pain Relevance 1.06

General Comments

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