INT97955

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Context Info
Confidence 0.49
First Reported 2000
Last Reported 2010
Negated 1
Speculated 0
Reported most in Body
Documents 8
Total Number 8
Disease Relevance 2.47
Pain Relevance 1.19

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

cytosol (CDC42) plasma membrane (CDC42) cytoskeleton (CDC42)
intracellular (CDC42) GTPase activity (CDC42) cell division (CDC42)
Anatomy Link Frequency
monocytes 1
filaments 1
fibroblast 1
CDC42 (Homo sapiens)
Pain Link Frequency Relevance Heat
Kappa opioid receptor 8 99.92 Very High Very High Very High
cINOD 8 99.26 Very High Very High Very High
agonist 20 95.60 Very High Very High Very High
antagonist 6 71.56 Quite High
Inflammation 31 67.04 Quite High
opioid receptor 1 41.12 Quite Low
Opioid 1 36.48 Quite Low
imagery 45 33.12 Quite Low
COX2 1 25.00 Low Low
Kinase C 31 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Stress 10 99.08 Very High Very High Very High
Adhesions 56 99.00 Very High Very High Very High
Cancer 197 95.36 Very High Very High Very High
INFLAMMATION 28 90.40 High High
Malignant Neoplastic Disease 5 88.00 High High
Inflammatory Breast Neoplasms 114 69.08 Quite High
Adenocarcinoma 3 58.96 Quite High
Breast Cancer 40 50.00 Quite Low
Metastasis 23 50.00 Quite Low
Syndrome 5 50.00 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Further, we showed that in Swiss 3T3 cells, pomalidomide only activated RhoA, not Rac1 or Cdc42, and potently induced stress fiber formation.
Neg (not) Positive_regulation (activated) of Cdc42 associated with stress
1) Confidence 0.49 Published 2009 Journal Blood Section Abstract Doc Link 19417207 Disease Relevance 0.17 Pain Relevance 0.08
The results confirm that a growth factor-induced increase in Cdc42 activity is a direct result of EGFR activation
Positive_regulation (increase) of Cdc42
2) Confidence 0.36 Published 2009 Journal Target Oncol Section Body Doc Link PMC2778706 Disease Relevance 0 Pain Relevance 0
Using pomalidomide and primary human monocytes, we report that pomalidomide rapidly and selectively activated RhoA and Rac1, but not Cdc42 or Ras, in the absence of any costimulation.
Positive_regulation (activated) of Cdc42 in monocytes
3) Confidence 0.33 Published 2009 Journal Blood Section Abstract Doc Link 19417207 Disease Relevance 0.16 Pain Relevance 0.09
These studies demonstrate that the activation of JNK by kappa-opioid receptors is routed via Gbetagamma, Src, FAK, Sos, Rac, and Cdc42.
Positive_regulation (routed) of Cdc42 associated with kappa opioid receptor
4) Confidence 0.32 Published 2004 Journal J. Pharmacol. Exp. Ther. Section Abstract Doc Link 14996948 Disease Relevance 0.16 Pain Relevance 0.27
Here we show that inhibition of endothelial-cell COX-2 by NSAIDs suppresses alpha V beta 3-dependent activation of the small GTPases Cdc42 and Rac, resulting in inhibition of endothelial-cell spreading and migration in vitro and suppression of fibroblast growth factor-2-induced angiogenesis in vivo.
Positive_regulation (activation) of Cdc42 in fibroblast associated with cinod
5) Confidence 0.32 Published 2001 Journal Nat. Med. Section Abstract Doc Link 11533708 Disease Relevance 0.69 Pain Relevance 0.49
12 can also activate JNK via ASK1, independently of the activation of Rac1 and cdc42 [39].
Positive_regulation (activation) of cdc42
6) Confidence 0.10 Published 2010 Journal Cellular Signalling Section Body Doc Link PMC2806525 Disease Relevance 0 Pain Relevance 0.22
In addition to increased stress fiber and focal adhesion contact formation, over-expression of RhoC could activate other Rho family members (ie RhoA, rac and/or cdc42) through signaling feedback loops [39], leading to dynamic cytoskeletal reorganization and a motile/metastatic cell.
Positive_regulation (activate) of cdc42 associated with stress and adhesions
7) Confidence 0.08 Published 2000 Journal Breast Cancer Res Section Body Doc Link PMC138665 Disease Relevance 1.22 Pain Relevance 0.03
Plakophilin 1 associates with actin filaments at cell borders and has been reported to interact with a GTP exchange factor (GEF) for Rho and thereby could regulate activity of Rho GTPases similar to the closely related p120-catenin, which is known to inhibit Rho A and to activate Rac 1 and Cdc42 (Anastasiadis and Reynolds 2001; Hatzfeld 2007).
Positive_regulation (activate) of Cdc42 in filaments
8) Confidence 0.08 Published 2008 Journal Histochem Cell Biol Section Body Doc Link PMC2413110 Disease Relevance 0.07 Pain Relevance 0

General Comments

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