INT108333

From wiki-pain
Jump to: navigation, search
Context Info
Confidence 0.68
First Reported 2003
Last Reported 2011
Negated 0
Speculated 0
Reported most in Body
Documents 43
Total Number 46
Disease Relevance 33.77
Pain Relevance 2.45

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

lipid binding (BAD) cytosol (BAD) mitochondrion (BAD)
cytoplasm (BAD)
Anatomy Link Frequency
AsPC-1 3
colon 2
cleavage 2
bands 1
BAD (Homo sapiens)
Pain Link Frequency Relevance Heat
COX-2 inhibitor 320 98.42 Very High Very High Very High
Clonidine 6 97.00 Very High Very High Very High
cytokine 85 96.44 Very High Very High Very High
cINOD 118 95.44 Very High Very High Very High
agonist 14 86.84 High High
diclofenac 6 79.84 Quite High
Bile 6 77.96 Quite High
cerebral cortex 2 75.00 Quite High
Pain 20 68.84 Quite High
withdrawal 13 61.04 Quite High
Disease Link Frequency Relevance Heat
Apoptosis 2550 100.00 Very High Very High Very High
Colon Cancer 226 99.64 Very High Very High Very High
Death 328 99.36 Very High Very High Very High
Pancreatic Cancer 798 98.72 Very High Very High Very High
Cancer 1392 98.52 Very High Very High Very High
Hypoxia 32 98.06 Very High Very High Very High
Malignant Neoplastic Disease 54 97.56 Very High Very High Very High
Stomach Cancer 30 96.52 Very High Very High Very High
Targeted Disruption 22 96.04 Very High Very High Very High
INFLAMMATION 230 94.72 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Sulindac sulfide inhibits epidermal growth factor-induced phosphorylation of extracellular-regulated kinase 1/2 and Bad in human colon cancer cells.
Phosphorylation (phosphorylation) of Bad in colon associated with colon cancer
1) Confidence 0.68 Published 2003 Journal Cancer Res. Section Title Doc Link 12566304 Disease Relevance 1.44 Pain Relevance 0.17
EGF-stimulated phosphorylation of ERK and Bad is blocked by pretreatment with U0126, a selective MAP kinase kinase (MKK)1/2 inhibitor.
Phosphorylation (phosphorylation) of Bad
2) Confidence 0.68 Published 2003 Journal Cancer Res. Section Abstract Doc Link 12566304 Disease Relevance 1.32 Pain Relevance 0.16
Similarly, pretreatment with sulindac sulfide blocks the ability of EGF to induce ERK1/2 and Bad phosphorylation, but also down-regulates total Bad but not ERK1/2 protein levels.
Phosphorylation (phosphorylation) of Bad
3) Confidence 0.68 Published 2003 Journal Cancer Res. Section Abstract Doc Link 12566304 Disease Relevance 1.18 Pain Relevance 0.14
For instance, desphosphorylation of Bad allows it to interact with Bcl-xL and initiate cell death [43].
Phosphorylation (desphosphorylation) of Bad associated with death
4) Confidence 0.64 Published 2005 Journal BMC Cancer Section Body Doc Link PMC1198222 Disease Relevance 0.91 Pain Relevance 0
In this study we show that epidermal growth factor (EGF) strongly induces phosphorylation of ERK1/2 and Bad in HT29 colon cancer cells.
Phosphorylation (phosphorylation) of Bad in colon associated with colon cancer
5) Confidence 0.59 Published 2003 Journal Cancer Res. Section Abstract Doc Link 12566304 Disease Relevance 1.36 Pain Relevance 0.16
The phosphorylation state of anti-apoptotic (Bcl-2 and Bcl-xL) and pro-apoptotic (Bad, Bid and Bik) Bcl-2 proteins regulates their cellular activity and, therefore, cell survival and cell death.
Phosphorylation (phosphorylation) of Bad associated with apoptosis and death
6) Confidence 0.55 Published 2005 Journal BMC Cancer Section Body Doc Link PMC1198222 Disease Relevance 0.99 Pain Relevance 0
In tumor cells, activation of extracellular-regulated kinase (ERK) 1/2 results in phosphorylation of several ERK1/2 effectors, including the proapoptotic protein Bad.
Phosphorylation (phosphorylation) of Bad associated with cancer
7) Confidence 0.52 Published 2003 Journal Cancer Res. Section Abstract Doc Link 12566304 Disease Relevance 1.50 Pain Relevance 0.18
Recent studies have shown that pharmacological activation of these kinases is associated with recruitment of anti-apoptotic signaling components such as the phosphorylation and inhibition of the proapoptotic proteins Bax and Bad, the inhibition of caspase 3 activation, the phosphorylation and activation of p70S6K (which acts to inhibit Bad) and the phosphorylation and activation of the antiapoptotic protein Bcl-2 (Harada et al 2001; Hausenloy and Yellon 2007).
Phosphorylation (phosphorylation) of Bad associated with apoptosis
8) Confidence 0.36 Published 2007 Journal Vascular Health and Risk Management Section Body Doc Link PMC2291307 Disease Relevance 0.48 Pain Relevance 0.10
Recent studies have shown that pharmacological activation of these kinases is associated with recruitment of anti-apoptotic signaling components such as the phosphorylation and inhibition of the proapoptotic proteins Bax and Bad, the inhibition of caspase 3 activation, the phosphorylation and activation of p70S6K (which acts to inhibit Bad) and the phosphorylation and activation of the antiapoptotic protein Bcl-2 (Harada et al 2001; Hausenloy and Yellon 2007).
Phosphorylation (phosphorylation) of Bad associated with apoptosis
9) Confidence 0.36 Published 2007 Journal Vascular Health and Risk Management Section Body Doc Link PMC2291307 Disease Relevance 0.43 Pain Relevance 0.09
Recent studies have shown that pharmacological activation of these kinases is associated with recruitment of anti-apoptotic signaling components such as the phosphorylation and inhibition of the proapoptotic proteins Bax and Bad, the inhibition of caspase 3 activation, the phosphorylation and activation of p70S6K (which acts to inhibit Bad) and the phosphorylation and activation of the antiapoptotic protein Bcl-2 (Harada et al 2001; Hausenloy and Yellon 2007).
Phosphorylation (phosphorylation) of Bad associated with apoptosis
10) Confidence 0.35 Published 2007 Journal Vascular Health and Risk Management Section Body Doc Link PMC2291307 Disease Relevance 0.48 Pain Relevance 0.10
The antiapoptotic protein Bcl-2 and inactive phosphorylated form of Bad (Figures 1 and 2) were increased in all cancer specimens, with no differences among Duke's stages, whereas the proapototic proteins Bad and Bak were decreased (Figure 2).


Phosphorylation (form) of Bad associated with cancer
11) Confidence 0.32 Published 2009 Journal Journal of Oncology Section Body Doc Link PMC2762309 Disease Relevance 0.58 Pain Relevance 0
The antiapoptotic protein Bcl-2 and inactive phosphorylated form of Bad (Figures 1 and 2) were increased in all cancer specimens, with no differences among Duke's stages, whereas the proapototic proteins Bad and Bak were decreased (Figure 2).


Phosphorylation (phosphorylated) of Bad associated with cancer
12) Confidence 0.32 Published 2009 Journal Journal of Oncology Section Body Doc Link PMC2762309 Disease Relevance 0.58 Pain Relevance 0
Recent studies have shown that pharmacological activation of these kinases is associated with recruitment of anti-apoptotic signaling components such as the phosphorylation and inhibition of the proapoptotic proteins Bax and Bad, the inhibition of caspase 3 activation, the phosphorylation and activation of p70S6K (which acts to inhibit Bad) and the phosphorylation and activation of the antiapoptotic protein Bcl-2 (Harada et al 2001; Hausenloy and Yellon 2007).
Phosphorylation (phosphorylation) of Bad associated with apoptosis
13) Confidence 0.31 Published 2007 Journal Vascular Health and Risk Management Section Body Doc Link PMC2291307 Disease Relevance 0.38 Pain Relevance 0.06
The activation of PI3K/Akt pathway may lead to the phosphorylation of Bad, which is consequently sequestrated in the cytoplasm by 14-3-3 protein and, in this way, inhibited in its pro-apoptotic function [51].
Phosphorylation (phosphorylation) of Bad associated with apoptosis
14) Confidence 0.25 Published 2010 Journal International Journal of Cell Biology Section Body Doc Link PMC2841246 Disease Relevance 0.88 Pain Relevance 0
The PI3K pathway is negatively regulated by PTEN (phosphatase and TENsin homolog), which converts PIP3 in PIP2, preventing PKB activation and Bad phosphorylation/sequestration.
Phosphorylation (phosphorylation) of Bad
15) Confidence 0.25 Published 2010 Journal International Journal of Cell Biology Section Body Doc Link PMC2841246 Disease Relevance 1.05 Pain Relevance 0.03
Activated Akt in turn phosphorylates several proteins that regulate cell survival, including Bad and caspase 9 [30].
Phosphorylation (phosphorylates) of Bad
16) Confidence 0.25 Published 2009 Journal Lipids Health Dis Section Body Doc Link PMC2667508 Disease Relevance 0.21 Pain Relevance 0.03
The nonphosphorylated form of Bad plays a pro-apoptotic role, by binding Bcl-xL or Bcl-2 and, thus, preventing their interactions with Bak and Bax.
Phosphorylation (nonphosphorylated) of Bad associated with apoptosis
17) Confidence 0.25 Published 2010 Journal International Journal of Cell Biology Section Body Doc Link PMC2841246 Disease Relevance 0.97 Pain Relevance 0
Upon phosphorylation, Akt has been shown to phosphorylate and to block the action of several pro-apoptotic proteins such as Bad [29].
Phosphorylation (phosphorylation) of Bad associated with apoptosis
18) Confidence 0.22 Published 2004 Journal Mol Cancer Section Body Doc Link PMC394342 Disease Relevance 1.16 Pain Relevance 0.19
Upon phosphorylation, Akt has been shown to phosphorylate and to block the action of several pro-apoptotic proteins such as Bad [29].
Phosphorylation (phosphorylate) of Bad associated with apoptosis
19) Confidence 0.22 Published 2004 Journal Mol Cancer Section Body Doc Link PMC394342 Disease Relevance 1.14 Pain Relevance 0.18
Besides, PKB inhibits apoptosis, by phosphorylating the pro-apoptotic protein Bad and by inhibiting caspase-9 cleavage [51].
Phosphorylation (phosphorylating) of Bad in cleavage associated with apoptosis
20) Confidence 0.22 Published 2010 Journal International Journal of Cell Biology Section Body Doc Link PMC2841246 Disease Relevance 0.86 Pain Relevance 0.11

General Comments

This test has worked.

Personal tools
Namespaces

Variants
Actions
Navigation
Toolbox