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Context Info
Confidence 0.05
First Reported 2004
Last Reported 2009
Negated 0
Speculated 0
Reported most in Body
Documents 3
Total Number 4
Disease Relevance 1.89
Pain Relevance 0.66

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 (CDC42EP5) cytoskeleton (CDC42EP5) cytoplasm (CDC42EP5)
CDC42EP5 (Homo sapiens)
Pain Link Frequency Relevance Heat
Kappa opioid receptor 8 95.84 Very High Very High Very High
agonist 2 93.60 High High
Chronic pancreatitis 4 91.68 High High
cINOD 1 86.48 High High
opioid receptor 1 53.40 Quite High
Opioid 1 48.76 Quite Low
Inflammation 4 5.00 Very Low Very Low Very Low
fibrosis 2 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Metastasis 46 99.12 Very High Very High Very High
Adhesions 2 93.44 High High
Pancreatitis 4 91.68 High High
Cancer 62 87.36 High High
Adenocarcinoma 102 87.08 High High
INFLAMMATION 1 86.24 High High
Clostridium Infection 2 76.44 Quite High
Stress 1 76.08 Quite High
Pancreatic Cancer 14 74.04 Quite High
Renal Cancer 2 15.96 Low Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Consistent with the activation of Rho GTPases, we found that pomalidomide enhanced F-actin formation, stabilized microtubules, and increased cell migration, all of which were blocked by selective inhibitors of ROCK1 and Rac1.
Positive_regulation (activation) of GTPases
1) Confidence 0.05 Published 2009 Journal Blood Section Abstract Doc Link 19417207 Disease Relevance 0.16 Pain Relevance 0.09
The participation of small GTPases as well as a guanine nucleotide exchange factor was also implicated because dominant-negative mutants of Rac, Cdc42, and Son-of-sevenless (Sos) attenuated the agonist-induced activation of JNK.
Positive_regulation (participation) of GTPases associated with agonist
2) Confidence 0.04 Published 2004 Journal J. Pharmacol. Exp. Ther. Section Abstract Doc Link 14996948 Disease Relevance 0.17 Pain Relevance 0.40
Due to the close homology between RhoC and RhoA (91% on the protein level), the possibility exists that both GTPases can be activated by the same RhoGEFs in vivo.
Positive_regulation (activated) of GTPases
3) Confidence 0.03 Published 2005 Journal Mol Cancer Section Body Doc Link PMC1173138 Disease Relevance 0.13 Pain Relevance 0
Similar to Ras, Rho GTPases are activated by a complex network of regulatory proteins and exists in the cell in an inactive GDP-bound and active GTP-bound state [32,33].
Positive_regulation (activated) of GTPases
4) Confidence 0.02 Published 2005 Journal Mol Cancer Section Body Doc Link PMC1173138 Disease Relevance 1.43 Pain Relevance 0.18

General Comments

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