INT271731

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Context Info
Confidence 0.47
First Reported 2009
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 4
Total Number 5
Disease Relevance 2.12
Pain Relevance 0.18

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

Anatomy Link Frequency
cleavage 1
20S (Mus musculus)
Pain Link Frequency Relevance Heat
spinal inflammation 1 81.84 Quite High
psoriasis 2 79.68 Quite High
ischemia 1 65.04 Quite High
Glutamate receptor 16 58.88 Quite High
cytokine 5 45.80 Quite Low
Inflammation 5 45.00 Quite Low
Central nervous system 16 31.84 Quite Low
tetrodotoxin 10 5.00 Very Low Very Low Very Low
depression 5 5.00 Very Low Very Low Very Low
Spinal cord 4 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Autoimmune Disease 5 84.08 Quite High
Neurodegenerative Disease 17 82.48 Quite High
Ankylosing Spondylitis 1 82.08 Quite High
Psoriasis 2 79.68 Quite High
Disease 40 72.56 Quite High
Motor Neuron Diseases 1 70.96 Quite High
Creutzfeldt Jakob Disease 2 68.24 Quite High
Brain Hemorrhage 1 65.04 Quite High
Aging 21 64.20 Quite High
Recurrence 1 63.08 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
This regulatory complex binds to the end of the 20S proteasome core, increasing the cleavage rate in an ATP-independent manner and affecting the quality of protein digestion [5], [8].
20S Binding (binds) of in cleavage
1) Confidence 0.47 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2823778 Disease Relevance 0.73 Pain Relevance 0.12
Intriguingly, as knockdown of Rpt2/PSMC1 expression leads to a specific impairment of 26S proteasome activity, while activity of the 20S proteasome is unaffected, neurodegeneration can be conclusively attributed to dysfunction of the 26S proteasome [31].
20S Binding (activity) of
2) Confidence 0.36 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2690827 Disease Relevance 1.08 Pain Relevance 0.03
Interestingly, the 20S proteasome complex in DM2 cells is associated with ER chaperone BiP, which is a master regulator of Unfolded Protein Response (UPR).
20S Binding (complex) of
3) Confidence 0.36 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.11 Pain Relevance 0
In the 26S proteasome, a single 20S particle may associate with one or two 19S particles to form a singly- or doubly-capped 26S proteasome.
20S Binding (associate) of
4) Confidence 0.36 Published 2010 Journal Frontiers in Molecular Neuroscience Section Body Doc Link PMC2901091 Disease Relevance 0.20 Pain Relevance 0.03
A surprising finding is that ECM29, which has been reported to stabilize the association of 19S and 20S particles (Leggett et al., 2002; Kleijnen et al., 2007), is only present in the cytosolic 26S but not the synaptic 26S.
20S Binding (association) of
5) Confidence 0.36 Published 2010 Journal Frontiers in Molecular Neuroscience Section Body Doc Link PMC2901091 Disease Relevance 0 Pain Relevance 0

General Comments

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