INT81543

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Context Info
Confidence 0.37
First Reported 1999
Last Reported 2010
Negated 1
Speculated 1
Reported most in Abstract
Documents 7
Total Number 9
Disease Relevance 2.51
Pain Relevance 4.10

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

cytosol (Nfkbia) plasma membrane (Nfkbia) nucleus (Nfkbia)
enzyme binding (Nfkbia) protein complex (Nfkbia) cytoplasm (Nfkbia)
Anatomy Link Frequency
nucleus 2
mast cells 2
Nfkbia (Rattus norvegicus)
Pain Link Frequency Relevance Heat
aspirin 20 99.84 Very High Very High Very High
Morphine 14 99.74 Very High Very High Very High
Endep 11 99.56 Very High Very High Very High
cytokine 17 97.92 Very High Very High Very High
Inflammation 11 97.78 Very High Very High Very High
intrathecal 4 93.68 High High
dexamethasone 5 92.44 High High
Antinociceptive 2 89.72 High High
cINOD 7 78.24 Quite High
pain pelvic 1 78.16 Quite High
Disease Link Frequency Relevance Heat
INFLAMMATION 18 97.78 Very High Very High Very High
Stomach Cancer 3 94.16 High High
Endometriosis 4 83.80 Quite High
Necrosis 2 82.84 Quite High
Cancer 6 82.48 Quite High
Glioma 4 79.08 Quite High
Reprotox - General 3 2 78.80 Quite High
Pressure And Volume Under Development 2 75.44 Quite High
Disease 2 59.40 Quite High
Immune System Diseases 1 57.44 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Moreover, amitriptyline/morphine co-infusion increased IkappaBalpha phosphorylation and the translocation of NF-kappaB p65 from the cytosol to the nucleus.
Positive_regulation (increased) of Phosphorylation (phosphorylation) of IkappaBalpha in nucleus associated with endep and morphine
1) Confidence 0.37 Published 2008 Journal Neuroscience Section Abstract Doc Link 18400403 Disease Relevance 0 Pain Relevance 1.84
IL-1beta caused a rapid increase in phosphorylated IkappaB-alpha levels and subsequent transient decrease in IkappaB-alpha levels, an inhibitor of NF-kappaB, as revealed by Western blot analysis using specific antibodies for phosphorylated and nonphosphorylated IkappaB-alpha.
Positive_regulation (increase) of Phosphorylation (phosphorylated) of IkappaB-alpha
2) Confidence 0.06 Published 1999 Journal Endocrinology Section Abstract Doc Link 10218970 Disease Relevance 0.38 Pain Relevance 0.71
By transfection of TAK1 siRNA, TNFalpha-induced phosphorylation of IkappaBalpha, JNK1/2, and p38MAPK, as well as IL-6 or IL-8 expression, were repressed.
Positive_regulation (induced) of Phosphorylation (phosphorylation) of IkappaBalpha
3) Confidence 0.04 Published 2009 Journal Mol. Cell. Endocrinol. Section Abstract Doc Link 19410630 Disease Relevance 0.39 Pain Relevance 0.19
Because LPS is known to stimulate inhibitor kappaB (IkappaB) kinase (IKK)-mediated phosphorylation of IkappaB followed by its degradation, which in turn induces nuclear factor (NF)-kappaB nuclear translocation leading to transcriptional activation of COX-2 gene, the effect of gamma-mangostin on the IKK/IkappaB cascade controlling the NF-kappaB activation was examined.
Spec (examined) Positive_regulation (stimulate) of Phosphorylation (phosphorylation) of IkappaB
4) Confidence 0.01 Published 2004 Journal Mol. Pharmacol. Section Abstract Doc Link 15322259 Disease Relevance 0.15 Pain Relevance 0
Consistently gamma-mangostin was also observed to decrease the LPS-induced IkappaB degradation and phosphorylation in a concentration-dependent manner, as assayed by immunoblotting.
Positive_regulation (induced) of Phosphorylation (phosphorylation) of IkappaB
5) Confidence 0.01 Published 2004 Journal Mol. Pharmacol. Section Abstract Doc Link 15322259 Disease Relevance 0.20 Pain Relevance 0.06
We thus propose that the anti-inflammatory effects of ASA in mast cells are due to suppression of IkappaB kinase activity, thereby inhibiting subsequent phosphorylation and degradation of IkappaB-alpha, activation of NF-kappaB, and transcription of proinflammatory cytokines.
Positive_regulation (activation) of Phosphorylation (phosphorylation) of IkappaB-alpha in mast cells associated with aspirin, inflammation and cytokine
6) Confidence 0.00 Published 2005 Journal Biochem. Pharmacol. Section Abstract Doc Link 15763541 Disease Relevance 0.48 Pain Relevance 0.67
Furthermore, unlike aspirin, SC236 affected neither the phosphorylation, degradation, nor expression of IkappaB-alpha, suggesting that the effects of SC236 are independent of IKK activity and IkappaB-alpha gene transcription.
Neg (neither) Positive_regulation (affected) of Phosphorylation (phosphorylation) of IkappaB-alpha associated with aspirin
7) Confidence 0.00 Published 2003 Journal Oncogene Section Abstract Doc Link 12606945 Disease Relevance 0.38 Pain Relevance 0.26
Plumbagin also abrogated mitogen-induced phosphorylation of ERK, IKK, and degradation of IkappaB-alpha.
Positive_regulation (induced) of Phosphorylation (phosphorylation) of IkappaB-alpha
8) Confidence 0.00 Published 2010 Journal J. Cell. Biochem. Section Abstract Doc Link 20564204 Disease Relevance 0.26 Pain Relevance 0.19
Plumbagin also abrogated mitogen-induced phosphorylation of ERK, IKK, and degradation of IkappaB-alpha.
Positive_regulation (-) of Phosphorylation (phosphorylation) of IkappaB-alpha
9) Confidence 0.00 Published 2010 Journal J. Cell. Biochem. Section Abstract Doc Link 20564204 Disease Relevance 0.26 Pain Relevance 0.19

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