INT196927

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Context Info
Confidence 0.36
First Reported 2006
Last Reported 2010
Negated 0
Speculated 1
Reported most in Body
Documents 9
Total Number 9
Disease Relevance 2.31
Pain Relevance 0.36

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

cytosol (Hdac1) nucleus (Hdac1) enzyme binding (Hdac1)
DNA binding (Hdac1) protein complex (Hdac1) transcription factor binding (Hdac1)
Anatomy Link Frequency
NS20Y 1
Hdac1 (Mus musculus)
Pain Link Frequency Relevance Heat
mu opioid receptor 160 92.32 High High
depression 2 21.32 Low Low
cocaine 8 5.00 Very Low Very Low Very Low
Spinal cord 6 5.00 Very Low Very Low Very Low
opioid receptor 6 5.00 Very Low Very Low Very Low
Analgesic 6 5.00 Very Low Very Low Very Low
Morphine 6 5.00 Very Low Very Low Very Low
imagery 6 5.00 Very Low Very Low Very Low
Eae 4 5.00 Very Low Very Low Very Low
Acute pain 4 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Repression 49 99.44 Very High Very High Very High
Cancer 9 91.20 High High
Pituitary Cancer 54 87.00 High High
Hypertrophy 8 84.64 Quite High
Retinoblastoma 4 83.96 Quite High
Apoptosis 79 83.84 Quite High
Embryonic Lethality 2 73.08 Quite High
Targeted Disruption 76 72.00 Quite High
Huntington's Chorea 1 62.84 Quite High
Injury 2 59.84 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
In vitro assays have established that aa 119-208 is sufficient to interact with MEF2 and HDAC1 [4], [8].
HDAC1 Binding (interact) of
1) Confidence 0.36 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2720538 Disease Relevance 0.43 Pain Relevance 0
The global changes of acetylation in these residues of histone or specific changes in a target locus of chromatins associated with CGN5 and HDAC1 will require further investigation.
HDAC1 Binding (associated) of
2) Confidence 0.33 Published 2010 Journal Obstetrics and Gynecology International Section Body Doc Link PMC2896857 Disease Relevance 0 Pain Relevance 0
Extensive deletion analysis [4], [6], [8] coupled with in vitro assays have established that amino acids (aa) 1–660 is sufficient to interact with MEF2, Runx2, HDAC1, 14-3-3, and also for phosphorylation and nuclear export [3], [12], [13], [16]–[19].
HDAC1 Binding (interact) of
3) Confidence 0.28 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2720538 Disease Relevance 0.15 Pain Relevance 0
Interestingly, Hr also binds HDAC1[11], [37], [38] and possibly might also recruit a complex with p53 resulting in decreased stability through deacetylation.
HDAC1 Spec (might) Binding (binds) of
4) Confidence 0.24 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2944824 Disease Relevance 0.55 Pain Relevance 0
Our in vitro studies, however, revealed that Smyd2 acts as a transcriptional repressor when bound to HDAC1 and the Sin3 repression complex [20].
HDAC1 Binding (bound) of associated with repression
5) Confidence 0.23 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2840034 Disease Relevance 0.30 Pain Relevance 0
This interaction was then repeated and confirmed in vitro with recombinant proteins, finding that one of the pRB domains involved in the interaction is the A/B pocket [30], the same domain that is also involved in the interaction with E2F1, HDAC1 and viral oncoproteins such as those produced by the E1A adenovirus [39,40].
HDAC1 Binding (interaction) of
6) Confidence 0.22 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.38 Pain Relevance 0
It is an active repression that pRB exerts on E2F1-mediated transcription by recruiting class I histone deacetylase proteins (HDAC1) to the E2F1-sites.
HDAC1 Binding (recruiting) of associated with repression
7) Confidence 0.22 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.49 Pain Relevance 0
Although Sp1 mainly acts as transcriptional activator, Sp3 can repress activity of the promoter by recruiting HDAC1 or HDAC2.
HDAC1 Binding (recruiting) of
8) Confidence 0.19 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0 Pain Relevance 0.11
After cross-linking the proteins and DNAs with formaldehyde, cell lysates from NS20Y cells were subjected to immunoprecipitation with NRSF, HDAC1, HDAC2, Sp1, Sp3 and IRF-4 (as a negative control).
HDAC1 Binding (immunoprecipitation) of in NS20Y
9) Confidence 0.19 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0 Pain Relevance 0.25

General Comments

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