INT309493

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Context Info
Confidence 0.37
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 15
Disease Relevance 3.00
Pain Relevance 0.20

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

lyase activity (Xrcc6) nucleolus (Xrcc6) chromosome (Xrcc6)
nucleus (Xrcc6) helicase activity (Xrcc6) DNA binding (Xrcc6)
Anatomy Link Frequency
neuronal 1
HeLa 1
Xrcc6 (Mus musculus)
Pain Link Frequency Relevance Heat
cerebral cortex 90 94.64 High High
imagery 30 5.00 Very Low Very Low Very Low
anesthesia 15 5.00 Very Low Very Low Very Low
Hippocampus 15 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Apoptosis 90 99.92 Very High Very High Very High
Death 120 99.88 Very High Very High Very High
Targeted Disruption 495 97.20 Very High Very High Very High
Disease 750 95.68 Very High Very High Very High
Stress 75 95.68 Very High Very High Very High
Infection 75 83.72 Quite High
Dyskinesias 15 81.12 Quite High
Dna Damage 60 71.92 Quite High
Ataxia 15 56.72 Quite High
Lifespan 75 42.88 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
We found that an expression level of mutant Htt almost equivalent to the expression level of endogenous Htt was sufficient for interaction with Ku70 (Fig. 3 D, bottom).
Ku70 Binding (interaction) of
1) Confidence 0.37 Published 2010 Journal The Journal of Cell Biology Section Body Doc Link PMC2867301 Disease Relevance 0 Pain Relevance 0
The decrease of Ku70 was blocked by the protease inhibitor MG132 (Fig. 6 D), indicating that one part of the Ku70 and mutant Htt complex was degraded by the proteasome system, whereas another part forms intracellular aggregates.
Ku70 Binding (complex) of
2) Confidence 0.28 Published 2010 Journal The Journal of Cell Biology Section Body Doc Link PMC2867301 Disease Relevance 0.08 Pain Relevance 0
Our experiments show that impairment of DNA repair through the interaction between Ku70 and mutant Htt accelerates accumulation of DSBs and causes neuronal dysfunction from an early stage of the HD pathology.
Ku70 Binding (interaction) of in neuronal associated with disease
3) Confidence 0.28 Published 2010 Journal The Journal of Cell Biology Section Body Doc Link PMC2867301 Disease Relevance 0.79 Pain Relevance 0
Furthermore, we titrated the amount of mutant Htt necessary for the interaction with Ku70 by using stable T-Rex–HeLa cells in which expression levels of mutant Htt can be controlled by the concentration of tetracyclin in the culture medium.
Ku70 Binding (interaction) of in HeLa
4) Confidence 0.28 Published 2010 Journal The Journal of Cell Biology Section Body Doc Link PMC2867301 Disease Relevance 0 Pain Relevance 0
S2 shows interaction between Ku70 and full-length mutant Htt protein.
Ku70 Binding (interaction) of
5) Confidence 0.27 Published 2010 Journal The Journal of Cell Biology Section Body Doc Link PMC2867301 Disease Relevance 0.25 Pain Relevance 0
Ku70–Ku80 interaction
Ku70 Binding (interaction) of
6) Confidence 0.27 Published 2010 Journal The Journal of Cell Biology Section Body Doc Link PMC2867301 Disease Relevance 0.09 Pain Relevance 0.08
Functions of the N-terminal domain are not known in detail, whereas its deletion profoundly impairs DNA–PK activity, DNA repair after ionizing radiation, and DNA end binding of Ku70 (Jin and Weaver, 1997).
Ku70 Binding (binding) of
7) Confidence 0.27 Published 2010 Journal The Journal of Cell Biology Section Body Doc Link PMC2867301 Disease Relevance 0 Pain Relevance 0
Especially soluble, rather than insoluble, mutant Htt impairs DNA–PK activity through the binding to Ku70 (Fig. 5 A).
Ku70 Binding (binding) of
8) Confidence 0.27 Published 2010 Journal The Journal of Cell Biology Section Body Doc Link PMC2867301 Disease Relevance 0.43 Pain Relevance 0
Ku70 interacts with mutant Htt
Ku70 Binding (interacts) of
9) Confidence 0.27 Published 2010 Journal The Journal of Cell Biology Section Body Doc Link PMC2867301 Disease Relevance 0.51 Pain Relevance 0
Binding (co-IP) of the firefly-V5–tagged fusion proteins to the PA-Renilla–tagged Ku70 was quantified by measuring the firefly luciferase activity in a luminescence plate reader (TECAN Infinite M200) using the Dual-Glo Luciferase Assay system (Promega).
Ku70 Binding (Binding) of
10) Confidence 0.27 Published 2010 Journal The Journal of Cell Biology Section Body Doc Link PMC2867301 Disease Relevance 0.13 Pain Relevance 0
Ku70 binding to DNA and Ku70–Ku80 interaction is also impaired by mutant Htt (Fig. 5, B and C).
Ku70 Binding (binding) of
11) Confidence 0.27 Published 2010 Journal The Journal of Cell Biology Section Body Doc Link PMC2867301 Disease Relevance 0.46 Pain Relevance 0
Acetylation of Ku70 seems to inhibit the interaction with Bax and promote apoptosis (Cohen et al., 2004).
Ku70 Binding (Acetylation) of associated with apoptosis
12) Confidence 0.25 Published 2010 Journal The Journal of Cell Biology Section Body Doc Link PMC2867301 Disease Relevance 0.25 Pain Relevance 0
Ku70–DNA-binding activity
Ku70 Binding (binding) of
13) Confidence 0.25 Published 2010 Journal The Journal of Cell Biology Section Body Doc Link PMC2867301 Disease Relevance 0 Pain Relevance 0.04
Ku70–DNA-binding activity
Ku70 Binding (activity) of
14) Confidence 0.25 Published 2010 Journal The Journal of Cell Biology Section Body Doc Link PMC2867301 Disease Relevance 0 Pain Relevance 0.04
The Ku70–DNA-binding activity was analyzed by Ku70–Ku86 DNA repair kit (Active Motif) according to the manufacturer’s instructions.
Ku70 Binding (binding) of
15) Confidence 0.24 Published 2010 Journal The Journal of Cell Biology Section Body Doc Link PMC2867301 Disease Relevance 0 Pain Relevance 0.04

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