INT187587

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Context Info
Confidence 0.35
First Reported 2005
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 11
Total Number 11
Disease Relevance 2.37
Pain Relevance 0.34

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

nucleus (Ep300) transferase activity, transferring acyl groups (Ep300) DNA binding (Ep300)
transcription factor binding (Ep300) cytoplasm (Ep300)
Anatomy Link Frequency
nucleus 1
Ep300 (Mus musculus)
Pain Link Frequency Relevance Heat
ischemia 17 97.14 Very High Very High Very High
Inflammation 68 83.04 Quite High
cytokine 12 81.48 Quite High
Inflammatory response 6 53.72 Quite High
chemokine 2 26.80 Quite Low
cINOD 4 24.48 Low Low
Paracetamol 12 8.36 Low Low
agonist 17 5.00 Very Low Very Low Very Low
cva 4 5.00 Very Low Very Low Very Low
withdrawal 4 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Cv Unclassified Under Development 25 97.14 Very High Very High Very High
Cancer 51 87.28 High High
Adhesions 16 85.76 High High
Apoptosis 115 83.76 Quite High
Necrosis 8 83.32 Quite High
INFLAMMATION 59 83.04 Quite High
Hypoxia 15 74.60 Quite High
Targeted Disruption 160 74.24 Quite High
Hemorrhagic Shock 46 72.68 Quite High
Lung Cancer 6 72.36 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Two coactivators that have histone acetyltransferase activity, steroid receptor coactivator-1 (SRC-1) and CREB binding protein/p300 (CBP), can bind to PPARs in a ligand-dependent manner.
p300 Binding (bind) of
1) Confidence 0.35 Published 2005 Journal Reprod Biol Endocrinol Section Body Doc Link PMC1266036 Disease Relevance 0.11 Pain Relevance 0
Thus, some of the described isoforms lack the C-terminal STL region which interacts with CBP/p300, DRIP130 and DNA-PKc, while retaining the interaction domain for NIF-1, PIMT and CoAA.
p300 Binding (interacts) of
2) Confidence 0.16 Published 2008 Journal Nuclear Receptor Signaling Section Body Doc Link PMC2254332 Disease Relevance 0 Pain Relevance 0
PIMT does not appear to methylate histones, but binds CBP/p300 and PBP(DRIP205/TRAP220) [Misra et al., 2002].
p300 Binding (binds) of
3) Confidence 0.16 Published 2008 Journal Nuclear Receptor Signaling Section Body Doc Link PMC2254332 Disease Relevance 0.10 Pain Relevance 0
In this regard, many of the factors described above have been shown to interact with CBP/p300, suggesting that NCoA6 may function to enhance the activity of such factors through its interaction with CBP/p300, which occurs in vivo.
p300 Binding (interaction) of
4) Confidence 0.16 Published 2008 Journal Nuclear Receptor Signaling Section Body Doc Link PMC2254332 Disease Relevance 0.20 Pain Relevance 0.04
In this regard, many of the factors described above have been shown to interact with CBP/p300, suggesting that NCoA6 may function to enhance the activity of such factors through its interaction with CBP/p300, which occurs in vivo.
p300 Binding (interact) of
5) Confidence 0.16 Published 2008 Journal Nuclear Receptor Signaling Section Body Doc Link PMC2254332 Disease Relevance 0.20 Pain Relevance 0.04
is recruited to the ROR-bound promoter, it could recruit p300 and GCN5 histone acetyltransferase to modify local chromatin structure to be permissive to transcriptional machinery [43].
p300 Binding (recruit) of
6) Confidence 0.15 Published 2010 Journal PPAR Research Section Body Doc Link PMC2943104 Disease Relevance 0.17 Pain Relevance 0
C-terminal activation domain from interacting with the transcriptional co-activating protein p300 [16], in turn limiting the transcriptional activity of HIF-1 in a normoxic environment [19].
p300 Binding (interacting) of
7) Confidence 0.15 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2908132 Disease Relevance 0.34 Pain Relevance 0
CBP/p300 was identified as a coactivator for NRs [Chakravarti et al., 1996] and is considered a transcriptional integrator which is recruited to the NRs and other transcription factors through their association with other coactivators (e.g., the SRCs and NCoA6(NRC)) [Chan and La Thangue, 2001; Chen et al., 1997; Goodman and Smolik, 2000; Mahajan and Samuels, 2000; Tian et al., 2006; Torchia et al., 1997].
p300 Binding (integrator) of
8) Confidence 0.12 Published 2008 Journal Nuclear Receptor Signaling Section Body Doc Link PMC2254332 Disease Relevance 0 Pain Relevance 0
The potential role of NCoA6 as a co-integrator is suggested by its ability to enhance transcriptional activation of a wide variety of transcription factors and from its in vivo association with a number of known cofactors including CBP/p300.
p300 Binding (association) of
9) Confidence 0.12 Published 2008 Journal Nuclear Receptor Signaling Section Abstract Doc Link PMC2254332 Disease Relevance 0.15 Pain Relevance 0
Once in the nucleus, the p65 subunit is phosphorylated at serine 276, which enhances its ability to recruit CBP and p300 and subsequently bind to DNA.36,37 Here, HSPTX-resuscitated animals displayed a marked reduction in nuclear phosphorylated NF-?
p300 Binding (recruit) of in nucleus
10) Confidence 0.07 Published 2010 Journal Clinics (Sao Paulo) Section Body Doc Link PMC2898548 Disease Relevance 0.36 Pain Relevance 0.11
Stimulus-induced activation of CREB can occur secondary to a variety of cellular stressors, including ischemia-reperfusion, and is mediated by phosphorylation of CREB at serine residue 133.10 The coactivator CREB-binding protein (CBP) and its paralogue p300 regulate transcription through selective interaction with individual transcription factors.
p300 Binding (interaction) of associated with ischemia
11) Confidence 0.07 Published 2010 Journal Clinics (Sao Paulo) Section Body Doc Link PMC2898548 Disease Relevance 0.74 Pain Relevance 0.15

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