INT128755

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Context Info
Confidence 0.57
First Reported 2005
Last Reported 2011
Negated 0
Speculated 0
Reported most in Body
Documents 10
Total Number 10
Disease Relevance 4.61
Pain Relevance 0.90

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

enzyme binding (Esr1) DNA binding (Esr1) protein complex (Esr1)
cytoplasm (Esr1) lipid binding (Esr1) nucleus (Esr1)
Anatomy Link Frequency
neuronal 1
arm 1
CNS 1
Esr1 (Mus musculus)
Pain Link Frequency Relevance Heat
Central nervous system 7 97.94 Very High Very High Very High
agonist 6 97.72 Very High Very High Very High
Bioavailability 1 91.68 High High
imagery 7 86.52 High High
Inflammatory response 3 82.88 Quite High
Pain 3 80.96 Quite High
Inflammation 42 80.24 Quite High
chemokine 2 71.92 Quite High
antagonist 5 70.24 Quite High
GABAergic 29 68.40 Quite High
Disease Link Frequency Relevance Heat
Tumor Necrosis Factor Receptor-associated Periodic Syndrome 65 98.78 Very High Very High Very High
Endometriosis (extended) 1 98.24 Very High Very High Very High
Stress 68 97.74 Very High Very High Very High
Cancer 28 97.08 Very High Very High Very High
Gauchers Disease 11 96.80 Very High Very High Very High
Breast Cancer 19 93.60 High High
Sprains And Strains 1 92.56 High High
Bardet-biedl Syndrome 1 89.52 High High
Hyperglycemia 1 88.08 High High
Triple Negative Breast Cancer 15 86.32 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Fulvestrant, on the other hand, binds and degrades ER, thereby acting as a pure anti-estrogen without partial agonist activity.
Protein_catabolism (degrades) of ER associated with agonist
1) Confidence 0.57 Published 2005 Journal Anticancer Drugs Section Abstract Doc Link 16027525 Disease Relevance 0.45 Pain Relevance 0.30
Among the parameters investigated, low histologic grade, positive ER, positive PR, positive bcl-2 and low level of Ki-67 were associated with prolonged RFS in univariate analysis.
Protein_catabolism (grade) of ER
2) Confidence 0.17 Published 2007 Journal BMC Cancer Section Body Doc Link PMC2217558 Disease Relevance 0.15 Pain Relevance 0.03
The clinically most important GC mutations, such as N370S, the most common mutation associated with type I GD, and L444P, the most prevalent mutation resulting in CNS involvement, predispose GC to misfold in the endoplasmic reticulum (ER), subjecting these variants to ER-associated degradation (ERAD), reducing the normal amount of mutant GC trafficking to the lysosome.
Protein_catabolism (degradation) of ER in CNS associated with gauchers disease and central nervous system
3) Confidence 0.14 Published 2008 Journal PLoS Biology Section Body Doc Link PMC2225441 Disease Relevance 1.00 Pain Relevance 0.21
At higher levels of expression, it is probable that TRAPS-associated mutant TNFR1 exits the ER through the process of ER-associated degradation and accumulates in cytoplasmic punctate structures that colocalise with chaperone proteins termed 'aggresomes', destined for proteasome-mediated disposal [56,57].
Protein_catabolism (degradation) of ER associated with tumor necrosis factor receptor-associated periodic syndrome
4) Confidence 0.12 Published 2007 Journal Arthritis Res Ther Section Body Doc Link PMC2206363 Disease Relevance 0.80 Pain Relevance 0.03
In addition, the CNX/CRT cycle is one arm of the quality-control machinery in the ER that monitors the glycosylation status of proteins and determines whether a molecule is exported to the Golgi complex or targeted for ER-associated degradation (14,19).
Protein_catabolism (degradation) of ER in arm
5) Confidence 0.09 Published 2008 Journal Diabetes Section Body Doc Link PMC2518495 Disease Relevance 0.69 Pain Relevance 0.03
Further, Herpud1/ Herp, a membrane-associated protein which functions in ER associated degradation was upregulated 9.7-fold (Fig. 3A).
Protein_catabolism (degradation) of ER
6) Confidence 0.08 Published 2008 Journal Current Chemical Genomics Section Body Doc Link PMC2803434 Disease Relevance 0.14 Pain Relevance 0.16
This mechanism, known as ER associated degradation (ERAD), is exploited by several bacterial toxins to gain access to the cytosol.
Protein_catabolism (degradation) of ER
7) Confidence 0.08 Published 2010 Journal PLoS ONE Section Abstract Doc Link PMC2950133 Disease Relevance 0.16 Pain Relevance 0
ER associated degradation (ERAD) via the proteosome is therefore a means to regulate neuronal inhibition by GABAA receptors in response to changing neuronal activity.
Protein_catabolism (degradation) of ER in neuronal
8) Confidence 0.06 Published 2008 Journal Frontiers in Molecular Neuroscience Section Body Doc Link PMC2526003 Disease Relevance 0.09 Pain Relevance 0.11
This process, known as ER associated degradation (ERAD), is exploited by some bacterial toxins to gain access to the cytosol [2].
Protein_catabolism (degradation) of ER
9) Confidence 0.05 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2950133 Disease Relevance 0 Pain Relevance 0
The intracellular effect of P58IPK on ER stress was achieved by inhibiting PERK activation [15], suggesting that P58IPK is a key mediator of co-translocational ER protein degradation, and this process is likely to contribute to ER homeostasis in stressed cells.
Protein_catabolism (degradation) of ER associated with stress
10) Confidence 0.04 Published 2011 Journal Molecular Vision Section Body Doc Link PMC3021576 Disease Relevance 1.14 Pain Relevance 0.04

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