INT183883

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Context Info
Confidence 0.46
First Reported 2005
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 8
Total Number 9
Disease Relevance 3.89
Pain Relevance 0

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

endosome (CAV1) mitochondrion (CAV1) small molecule metabolic process (CAV1)
Golgi apparatus (CAV1) endoplasmic reticulum (CAV1) intracellular (CAV1)
Anatomy Link Frequency
endothelial cells 1
HPAF-II 1
CAV1 (Homo sapiens)
Pain Link Frequency Relevance Heat
Inflammation 9 44.16 Quite Low
Chronic pancreatitis 8 18.56 Low Low
fibrosis 4 5.00 Very Low Very Low Very Low
Antihistamine 4 5.00 Very Low Very Low Very Low
potassium channel 4 5.00 Very Low Very Low Very Low
Pain 3 5.00 Very Low Very Low Very Low
peripheral neuropathy 3 5.00 Very Low Very Low Very Low
corticosteroid 2 5.00 Very Low Very Low Very Low
induced neuropathy 2 5.00 Very Low Very Low Very Low
anesthesia 2 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Prostate Cancer 198 99.96 Very High Very High Very High
Apoptosis 8 98.36 Very High Very High Very High
Hyperplasia 2 98.14 Very High Very High Very High
Adenocarcinoma 204 96.96 Very High Very High Very High
Cancer 328 93.36 High High
Metastasis 123 79.88 Quite High
Renal Cancer 4 72.92 Quite High
Skin Cancer 7 70.24 Quite High
Repression 2 69.60 Quite High
Targeted Disruption 8 65.12 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Furthermore, interaction of cav-1 and RhoC may result in decreased RhoC activation, limiting cell migration and invasion.


cav-1 Binding (interaction) of
1) Confidence 0.46 Published 2005 Journal Mol Cancer Section Body Doc Link PMC1173138 Disease Relevance 0.09 Pain Relevance 0
Numerous molecules have been identified which interact with cav-1 [14-18].
cav-1 Binding (interact) of
2) Confidence 0.46 Published 2005 Journal Mol Cancer Section Body Doc Link PMC1173138 Disease Relevance 1.56 Pain Relevance 0
Unexpectedly, the association between cav-1 and RhoC was restored in the HPAF-II/dnRhoC cell line suggesting that inhibition of RhoC activity leads to re-expression of cav-1 protein.
cav-1 Binding (association) of in HPAF-II
3) Confidence 0.36 Published 2005 Journal Mol Cancer Section Body Doc Link PMC1173138 Disease Relevance 0.14 Pain Relevance 0
Proteins that associate with cav-1 contain the canonical cav-1 binding domain, ?
cav-1 Binding (associate) of
4) Confidence 0.34 Published 2005 Journal Mol Cancer Section Body Doc Link PMC1173138 Disease Relevance 0.19 Pain Relevance 0
In prostate cancer, Cav-1 interacts with and inhibits the serine/threonine protein phosphatases PP1 and PP2A in a CSD-dependent manner.90 PP1 and PP2A are two major classes of phosphatases that act as tumor suppressors by maintaining Akt in a dephosphorylated, inactive state.
Cav-1 Binding (interacts) of associated with cancer and prostate cancer
5) Confidence 0.34 Published 2010 Journal Cancer management and research Section Body Doc Link PMC3004586 Disease Relevance 0.68 Pain Relevance 0
Caveolae modulate diverse intracellular signaling pathways involved in regulation of cellular proliferation, apoptosis, endocytosis, and cholesterol trafficking.12 This is principally achieved by the interaction of Cav-1 with a large number of molecules in either a CSD-dependent or CSD-independent manner.
Cav-1 Binding (interaction) of associated with apoptosis and hyperplasia
6) Confidence 0.34 Published 2010 Journal Cancer management and research Section Body Doc Link PMC3004586 Disease Relevance 0.63 Pain Relevance 0
When gp60 is activated, it interacts with caveolin-1 protein, leading to the formation of vesicles (caveolae) which then transport their cargo, albumin loaded with cytotoxic agent, across the endothelial cells and into the tumor interstitium where it is trapped.
caveolin Binding (interacts) of in endothelial cells associated with cancer
7) Confidence 0.03 Published 2009 Journal OncoTargets and therapy Section Body Doc Link PMC2886338 Disease Relevance 0.59 Pain Relevance 0
To establish whether interactions between maxi-K channels and caveolin affect the endogenous myometrial total outward K+ current, we used a siRNA to inhibit cav-1 gene expression in hMSMCs.
caveolin Binding (interactions) of
8) Confidence 0.03 Published 2009 Journal Reprod Biol Endocrinol Section Body Doc Link PMC2785819 Disease Relevance 0 Pain Relevance 0
The maxi-K channel fails to associate with lipid rafts when its caveolin-binding motif is disrupted
caveolin-binding Binding (motif) of
9) Confidence 0.02 Published 2009 Journal Reprod Biol Endocrinol Section Body Doc Link PMC2785819 Disease Relevance 0 Pain Relevance 0

General Comments

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