INT92117

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Context Info
Confidence 0.80
First Reported 2000
Last Reported 2011
Negated 0
Speculated 2
Reported most in Body
Documents 26
Total Number 28
Disease Relevance 9.93
Pain Relevance 0.86

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

mitochondrion (BCL2) cell morphogenesis (BCL2) endoplasmic reticulum (BCL2)
intracellular (BCL2) cytoplasm (BCL2) cytosol (BCL2)
Anatomy Link Frequency
OGE 1
BCL2 (Homo sapiens)
Pain Link Frequency Relevance Heat
cINOD 8 98.04 Very High Very High Very High
withdrawal 1 95.36 Very High Very High Very High
Spinal cord 1 86.88 High High
Kinase C 14 84.80 Quite High
antagonist 39 83.76 Quite High
COX-2 inhibitor 7 77.24 Quite High
Inflammation 28 68.16 Quite High
Pain 10 64.16 Quite High
aspirin 1 58.36 Quite High
Neuropeptide 7 52.68 Quite High
Disease Link Frequency Relevance Heat
Apoptosis 406 100.00 Very High Very High Very High
Breast Cancer 69 99.84 Very High Very High Very High
Prostate Cancer 14 99.48 Very High Very High Very High
Cancer 372 97.88 Very High Very High Very High
Death 100 96.68 Very High Very High Very High
Starvation 225 96.52 Very High Very High Very High
Stress 273 95.44 Very High Very High Very High
Colon Cancer 30 95.24 Very High Very High Very High
Carcinoma 10 94.24 High High
Reprotox - General 1 32 93.60 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
COS-7 cells were treated as shown for 24 h and blotted for phosphorylated Bcl-2 (PBcl-2) before stripping and reprobing for total Bcl-2 (TBcl-2).
Phosphorylation (phosphorylated) of Bcl-2
1) Confidence 0.80 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2916709 Disease Relevance 0 Pain Relevance 0
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 Bcl-2 associated with apoptosis and death
2) Confidence 0.73 Published 2005 Journal BMC Cancer Section Body Doc Link PMC1198222 Disease Relevance 0.98 Pain Relevance 0
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 Bcl-2 associated with apoptosis and death
3) Confidence 0.72 Published 2005 Journal BMC Cancer Section Body Doc Link PMC1198222 Disease Relevance 1.00 Pain Relevance 0
This data suggests that alterations in expression and phosphorylation of Bcl-2 family proteins may underlie the increase in NPC viability induced by PACAP.
Phosphorylation (phosphorylation) of Bcl-2
4) Confidence 0.61 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2885411 Disease Relevance 0.09 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 Bcl-2 associated with apoptosis
5) Confidence 0.52 Published 2007 Journal Vascular Health and Risk Management Section Body Doc Link PMC2291307 Disease Relevance 0.39 Pain Relevance 0.06
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 Bcl-2 associated with apoptosis
6) Confidence 0.52 Published 2007 Journal Vascular Health and Risk Management Section Body Doc Link PMC2291307 Disease Relevance 0.39 Pain Relevance 0.06
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 Bcl-2 associated with cancer
7) Confidence 0.32 Published 2009 Journal Journal of Oncology Section Body Doc Link PMC2762309 Disease Relevance 0.58 Pain Relevance 0
This effect may due to induction of apoptosis through uncoupling of oxidative phosphorylation and down-regulation of Bcl-2, as has been demonstrated for some nonselective NSAIDs, for instance, flurbiprofen.
Phosphorylation (phosphorylation) of Bcl-2 associated with cinod and apoptosis
8) Confidence 0.29 Published 2000 Journal Crit Rev Clin Lab Sci Section Abstract Doc Link 11078056 Disease Relevance 0.80 Pain Relevance 0.48
This effect is associated with reduced expression level of p21 in prostate cancer cell PC3 33 or increased Bcl-2 phosphorylation in breast cancer cells 34, and multidrug resistance-associated protein 1 35, respectively.
Phosphorylation (phosphorylation) of Bcl-2 associated with breast cancer and prostate cancer
9) Confidence 0.18 Published 2010 Journal Journal of Cancer Section Body Doc Link PMC2938072 Disease Relevance 1.22 Pain Relevance 0
Additionally, OGE pretreatment significantly upregulated Bcl-2 expression and Akt phosphorylation, and slightly affected the phosphorylation of mitogen-activated protein kinases including p38 MAPK and JNK.
Phosphorylation (phosphorylation) of Bcl-2 in OGE
10) Confidence 0.14 Published 2011 Journal Evidence-based Complementary and Alternative Medicine : eCAM Section Abstract Doc Link PMC2952314 Disease Relevance 0.49 Pain Relevance 0.03
Paclitaxel-induced apoptosis resulted in the phosphorylation of Bcl-2 that was suppressed by the addition of ET-1.
Phosphorylation (phosphorylation) of Bcl-2 associated with apoptosis
11) Confidence 0.10 Published 2004 Journal J Transl Med Section Body Doc Link PMC436068 Disease Relevance 0.89 Pain Relevance 0.12
LN also caused an increase in the expression of survivin and the phosphorylation of Bad at Ser136 but did not affect Bax, Bcl-2 or Bad expression or Bad phosphorylation at Ser112 in AsPC-1cells (Fig. 10D).
Phosphorylation (phosphorylation) of Bcl-2
12) Confidence 0.08 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.39 Pain Relevance 0
Compared with parental cells and vector cells, clone 2 and pool 1 cells transfected with pcDNA3.1-FRNK showed a decrease in survivin expression and Bad phosphorylation at Ser136 but did not affect Bax, Bcl-2 or Bad expression or Bad phosphorylation at Ser112 (Fig. 5E).
Phosphorylation (phosphorylation) of Bcl-2
13) Confidence 0.08 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.63 Pain Relevance 0
LN also caused an increase in the expression of survivin and the phosphorylation of Bad at Ser136 but did not affect Bax, Bcl-2 or Bad expression or Bad phosphorylation at Ser112 in AsPC-1cells (Fig. 10D).
Phosphorylation (phosphorylation) of Bcl-2
14) Confidence 0.08 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.39 Pain Relevance 0
Menadione had the opposite effect of thiol antioxidants by enhancing JNK and Bcl-2 phosphorylation, but had no effect on mTOR activity or Beclin-1 expression (Fig. 6F).
Phosphorylation (phosphorylation) of Bcl-2
15) Confidence 0.07 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2916709 Disease Relevance 0.12 Pain Relevance 0
NAC and glutathione inhibited the activation of JNK and decreased the phosphorylation of Bcl-2 (Fig. 6C and D).
Phosphorylation (phosphorylation) of Bcl-2
16) Confidence 0.07 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2916709 Disease Relevance 0.17 Pain Relevance 0
Thiol ROS scavengers such as NAC inhibit mTOR (which would be expected to induce autophagy) but decrease the phosphorylation of JNK and Bcl-2 which will inhibit autophagy, while the superoxide-generating agent menadione increases levels of LC3-II and the phosphorylation of JNK and Bcl-2.


Phosphorylation (phosphorylation) of Bcl-2
17) Confidence 0.07 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2916709 Disease Relevance 0.29 Pain Relevance 0
Given the central role of superoxide in autophagy and our observation that menadione has opposite effects on the phosphorylation of JNK and Bcl-2 to NAC, it is possible that NAC exerts its effects by acting downstream of superoxide.
Phosphorylation (phosphorylation) of Bcl-2
18) Confidence 0.07 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2916709 Disease Relevance 0.24 Pain Relevance 0
(D) Thiol antioxidants decrease Bcl-2 phosphorylation.
Phosphorylation (phosphorylation) of Bcl-2
19) Confidence 0.07 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2916709 Disease Relevance 0 Pain Relevance 0
Thiol ROS scavengers such as NAC inhibit mTOR (which would be expected to induce autophagy) but decrease the phosphorylation of JNK and Bcl-2 which will inhibit autophagy, while the superoxide-generating agent menadione increases levels of LC3-II and the phosphorylation of JNK and Bcl-2.


Phosphorylation (phosphorylation) of Bcl-2
20) Confidence 0.07 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2916709 Disease Relevance 0.26 Pain Relevance 0

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