INT62198

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Context Info
Confidence 0.47
First Reported 1996
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 3
Total Number 4
Disease Relevance 1.59
Pain Relevance 0.15

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

nucleus (Hsf1) DNA binding (Hsf1) protein complex (Hsf1)
response to stress (Hsf1) cytoplasm (Hsf1)
Hsf1 (Mus musculus)
Pain Link Frequency Relevance Heat
cINOD 2 78.80 Quite High
qutenza 2 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Shock 28 100.00 Very High Very High Very High
INFLAMMATION 2 78.56 Quite High
Stress 24 75.00 Quite High
Myeloid Leukemia 24 50.00 Quite Low
Chronic Myeloid Leukemia 16 50.00 Quite Low
Apoptosis 16 5.00 Very Low Very Low Very Low
Cancer 10 5.00 Very Low Very Low Very Low
Philadelphia Chromosome 4 5.00 Very Low Very Low Very Low
Death 2 5.00 Very Low Very Low Very Low
Genetic Translocation 2 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Comparison of heat shock and drug-induced forms of HSF1 has revealed that the transcriptionally inert drug-induced HSF1 is constitutively but not inducibly serine-phosphorylated, whereas heat shock-induced HSF1 is both constitutively and inducibly serine-phosphorylated.
Positive_regulation (inducibly) of Phosphorylation (serine-phosphorylated) of HSF1 associated with shock
1) Confidence 0.47 Published 1996 Journal J. Biol. Chem. Section Abstract Doc Link 8631933 Disease Relevance 0.78 Pain Relevance 0.08
Comparison of heat shock and drug-induced forms of HSF1 has revealed that the transcriptionally inert drug-induced HSF1 is constitutively but not inducibly serine-phosphorylated, whereas heat shock-induced HSF1 is both constitutively and inducibly serine-phosphorylated.
Positive_regulation (inducibly) of Phosphorylation (phosphorylated) of HSF1 associated with shock
2) Confidence 0.47 Published 1996 Journal J. Biol. Chem. Section Abstract Doc Link 8631933 Disease Relevance 0.75 Pain Relevance 0.07
Moreover it seems likely that in absence of the priming phosphorylation of HSF1 by ERK1/2, the secondary effect of the activated Gsk3?
Positive_regulation (by) of Phosphorylation (phosphorylation) of HSF1
3) Confidence 0.19 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2806839 Disease Relevance 0.06 Pain Relevance 0
can perform the secondary phosphorylation on HSF1 at ser 303 resulting in a cytoplasmic –inactive form of HSF1 [33].
Positive_regulation (resulting) of Phosphorylation (phosphorylation) of HSF1
4) Confidence 0.18 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2806839 Disease Relevance 0 Pain Relevance 0

General Comments

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