INT253556

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Context Info
Confidence 0.44
First Reported 2007
Last Reported 2010
Negated 0
Speculated 1
Reported most in Body
Documents 6
Total Number 7
Disease Relevance 2.93
Pain Relevance 0.24

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

nucleus (Sp1) intracellular (Sp1) DNA binding (Sp1)
transcription factor binding (Sp1) cytoplasm (Sp1)
Sp1 (Mus musculus)
Pain Link Frequency Relevance Heat
metalloproteinase 31 68.72 Quite High
cytokine 68 65.52 Quite High
Inflammation 31 65.12 Quite High
IPN 5 49.08 Quite Low
Pain 6 46.12 Quite Low
Inflammatory response 17 43.44 Quite Low
Central nervous system 5 5.00 Very Low Very Low Very Low
ischemia 5 5.00 Very Low Very Low Very Low
Peripheral nervous system 4 5.00 Very Low Very Low Very Low
cINOD 3 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Cancer 163 99.06 Very High Very High Very High
Hypoxia 21 91.32 High High
Atherosclerosis 55 89.72 High High
Disease 172 72.96 Quite High
Disorder Of Lipid Metabolism 11 70.48 Quite High
INFLAMMATION 48 65.12 Quite High
Death 9 54.24 Quite High
Renal Disease 5 51.32 Quite High
Metastasis 33 50.00 Quite Low
Inflammatory Pain 5 49.08 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Transcriptional inhibition that is potentially mediated by a CK2-mediated phosphorylation of Sp1 has also been suggested for the flow-dependent suppression of endothelial Toll-like receptor 2 expression [34].
Phosphorylation (phosphorylation) of Sp1
1) Confidence 0.44 Published 2008 Journal Cell Signal Section Body Doc Link PMC2586094 Disease Relevance 0.37 Pain Relevance 0.06
Indeed, CK2-mediated phosphorylation of the carboxyl terminus of Sp1 is associated with a decrease in its DNA binding activity [35].
Phosphorylation (phosphorylation) of Sp1
2) Confidence 0.44 Published 2008 Journal Cell Signal Section Body Doc Link PMC2586094 Disease Relevance 0.41 Pain Relevance 0.05
mediated via phosphorylation of Sp1 (and possibly Sp3), which leads to decreased binding to regulatory sequences in the LPL gene.
Phosphorylation (phosphorylation) of Sp1
3) Confidence 0.44 Published 2008 Journal Cell Signal Section Body Doc Link PMC2586094 Disease Relevance 0.37 Pain Relevance 0.09
Secondly, we found that THL could inhibit, in cancer cells, the activity of ERK1/2 (Fig 2D), which phosphorylates the transcription factor Sp1 and causes the recruitment of Sp1 to the vegf-A promoter [65].
Phosphorylation (phosphorylates) of Sp1 associated with cancer
4) Confidence 0.40 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2880989 Disease Relevance 1.24 Pain Relevance 0.03
It also contains a variety of transcription factor binding sites, including those for Sp1, GATA-1, AP1, AP2, CREB, estrogen and glucocorticoid receptors, NF?
Phosphorylation (those) of Sp1
5) Confidence 0.35 Published 2007 Journal Current Genomics Section Body Doc Link PMC2647160 Disease Relevance 0.55 Pain Relevance 0
To further investigate the potential impact of CK2-mediated phosphorylation of Sp1 on DNA binding activity, experiments were carried out using purified CK2.
Spec (investigate) Phosphorylation (phosphorylation) of Sp1
6) Confidence 0.33 Published 2008 Journal Cell Signal Section Body Doc Link PMC2586094 Disease Relevance 0 Pain Relevance 0
CK2-mediated phosphorylation of Sp1 is associated with decreased DNA binding
Phosphorylation (phosphorylation) of Sp1
7) Confidence 0.33 Published 2008 Journal Cell Signal Section Body Doc Link PMC2586094 Disease Relevance 0 Pain Relevance 0

General Comments

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