INT194789

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Context Info
Confidence 0.30
First Reported 2006
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 2
Total Number 4
Disease Relevance 2.61
Pain Relevance 0.08

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

cytosol (HSPB2) nucleus (HSPB2) cytoplasm (HSPB2)
HSPB2 (Homo sapiens)
Pain Link Frequency Relevance Heat
cytokine 37 83.04 Quite High
metalloproteinase 42 13.28 Low Low
Inflammation 30 5.00 Very Low Very Low Very Low
rheumatoid arthritis 4 5.00 Very Low Very Low Very Low
Pain 3 5.00 Very Low Very Low Very Low
chemokine 3 5.00 Very Low Very Low Very Low
Arthritis 3 5.00 Very Low Very Low Very Low
Central nervous system 1 5.00 Very Low Very Low Very Low
Inflammatory response 1 5.00 Very Low Very Low Very Low
headache 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Shock 5 100.00 Very High Very High Very High
Cancer 309 99.84 Very High Very High Very High
Reprotox - General 1 174 96.60 Very High Very High Very High
Stress 6 95.92 Very High Very High Very High
Metastasis 129 91.32 High High
Adhesions 114 54.16 Quite High
Congenital Anomalies 3 32.52 Quite Low
Breast Cancer 66 5.00 Very Low Very Low Very Low
Apoptosis 64 5.00 Very Low Very Low Very Low
INFLAMMATION 31 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Importantly, genistein decreased phosphorylation of both p38 MAPK and HSP27 in tumor tissue, consistent with inhibition of MEK4.
Phosphorylation (phosphorylation) of HSP27 associated with cancer
1) Confidence 0.30 Published 2010 Journal Cancer Metastasis Rev Section Body Doc Link PMC2933845 Disease Relevance 1.04 Pain Relevance 0
However, when phosphorylated, HSP27 induces increased F-actin formation [152, 153], increased cell migration [154, 155], and increased cell invasion [144].
Phosphorylation (phosphorylated) of HSP27
2) Confidence 0.30 Published 2010 Journal Cancer Metastasis Rev Section Body Doc Link PMC2933845 Disease Relevance 0.58 Pain Relevance 0
When dephosphorylated, HSP27 acts as an actin capping protein and thus inhibits actin polymerization [150, 151].
Phosphorylation (dephosphorylated) of HSP27
3) Confidence 0.30 Published 2010 Journal Cancer Metastasis Rev Section Body Doc Link PMC2933845 Disease Relevance 0.55 Pain Relevance 0
In contrast to MSK1/2, which preferentially activates transcription, MAP kinase-activated protein kinase 2 (MK2) participates in the control of gene expression at the post-transcriptional level by phosphorylating tristetraprolin (TTP) or heat shock protein 27 (hsp27) [43].


Phosphorylation (phosphorylating) of hsp27 associated with shock
4) Confidence 0.14 Published 2006 Journal Arthritis Res Ther Section Body Doc Link PMC1526596 Disease Relevance 0.45 Pain Relevance 0.08

General Comments

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