INT105888

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Context Info
Confidence 0.80
First Reported 2002
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 9
Total Number 9
Disease Relevance 4.78
Pain Relevance 0.40

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 (BAX) cytosol (BAX) mitochondrion (BAX)
endoplasmic reticulum (BAX) nucleus (BAX) cytoplasm (BAX)
BAX (Homo sapiens)
Pain Link Frequency Relevance Heat
vincristine 1 80.88 Quite High
cINOD 1 79.52 Quite High
Pain 6 68.84 Quite High
ischemia 66 53.84 Quite High
Potency 1 31.84 Quite Low
imagery 1 9.68 Low Low
Angina 24 5.00 Very Low Very Low Very Low
adenocard 18 5.00 Very Low Very Low Very Low
Kinase C 9 5.00 Very Low Very Low Very Low
bradykinin 9 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Apoptosis 353 99.92 Very High Very High Very High
Cancer 92 95.84 Very High Very High Very High
Chronic Lymphoid Leukemia 9 93.96 High High
Colon Cancer 1 89.08 High High
Myeloproliferative Disorder 45 86.40 High High
Stress 4 84.76 Quite High
Pancreatic Cancer 144 83.92 Quite High
Death 51 75.60 Quite High
Myeloid Leukemia 25 71.00 Quite High
Pain 6 68.84 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
G(2)-M arrest was associated with phosphorylation of Bcl2 (but not BAD, Bax, or Bcl-XL): both of these end points were abrogated by treatment with a calcium chelator.
Phosphorylation (phosphorylation) of Bax
1) Confidence 0.80 Published 2002 Journal Cancer Res. Section Abstract Doc Link 12384529 Disease Relevance 0.80 Pain Relevance 0.12
Immunofluorescence staining of Bax
Phosphorylation (staining) of Bax
2) Confidence 0.75 Published 2010 Journal Cancer Cell Int Section Body Doc Link PMC2873331 Disease Relevance 0.37 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 Bax associated with apoptosis
3) Confidence 0.35 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 Bax associated with apoptosis
4) Confidence 0.34 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 Bax associated with apoptosis
5) Confidence 0.34 Published 2007 Journal Vascular Health and Risk Management Section Body Doc Link PMC2291307 Disease Relevance 0.43 Pain Relevance 0.09
Deacetylation of p53 by HDAC1–3 or SIRT1 inhibits its transcriptional activity, and subsequently, the activation of its downstream molecules, Bax and p21 [93–95].
Phosphorylation (Deacetylation) of Bax
6) Confidence 0.15 Published 2010 Journal Invest New Drugs Section Body Doc Link PMC3003795 Disease Relevance 0.81 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 Bax
7) 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 Bax
8) 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 Bax
9) Confidence 0.08 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.39 Pain Relevance 0

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