INT226176

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Context Info
Confidence 0.61
First Reported 2007
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 15
Total Number 21
Disease Relevance 13.17
Pain Relevance 0.56

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

nucleus (Hmbs) cytoplasm (Hmbs)
Anatomy Link Frequency
myofibril 2
muscle 2
muscle cells 1
neurons 1
brains 1
Hmbs (Mus musculus)
Pain Link Frequency Relevance Heat
Inflammation 105 94.08 High High
ischemia 4 82.60 Quite High
Central nervous system 43 81.20 Quite High
Dopamine 77 77.52 Quite High
cytokine 35 67.88 Quite High
midbrain 20 57.92 Quite High
fibrosis 7 56.80 Quite High
Pain 7 55.28 Quite High
Neuritis 9 48.60 Quite Low
Glutamate receptor 7 41.12 Quite Low
Disease Link Frequency Relevance Heat
Disease 791 99.64 Very High Very High Very High
Death 105 99.52 Very High Very High Very High
Apoptosis 68 99.08 Very High Very High Very High
Toxocariasis 90 97.68 Very High Very High Very High
Parkinson's Disease 345 97.06 Very High Very High Very High
Chronic Renal Failure 196 96.08 Very High Very High Very High
Neurodegenerative Disease 66 95.52 Very High Very High Very High
Cancer 46 94.40 High High
INFLAMMATION 126 94.08 High High
Autoimmune Disease 2 93.36 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Covalent linkage of ubiquitin regulates the function and, ultimately, the degradation of many proteins by the ubiquitin-proteasome system (UPS).
Protein_catabolism (degradation) of UPS
1) Confidence 0.61 Published 2009 Journal PLoS ONE Section Abstract Doc Link PMC2690827 Disease Relevance 0.22 Pain Relevance 0
In addition to degrading regulatory proteins, the UPS also degrades misfolded and damaged proteins, thus collectively implicating the UPS in a wide range of conditions, including neurodegenerative diseases, cancer, inflammation, and autoimmunity [2], [3].
Protein_catabolism (degrades) of UPS associated with autoimmune disease, inflammation, cancer and neurodegenerative disease
2) Confidence 0.46 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2690827 Disease Relevance 0.55 Pain Relevance 0.05
In addition to the existence of EOPD forms caused by mutations in genes that codify proteins of UPS pathway, such as parkin and UCHL1, as previously referred, the colocalization of proteasome subunits in LBs (Ii et al., 1997) and also the presence of ubiquitinated proteins in LB may indicate UPS failure in PD, since ubiquitin is the signal protein for degradation by UPS.
Protein_catabolism (degradation) of UPS associated with parkinson's disease and disease
3) Confidence 0.29 Published 2010 Journal Frontiers in Aging Neuroscience Section Body Doc Link PMC2890153 Disease Relevance 0.58 Pain Relevance 0
Protein degradation by the UPS consists in a tightly regulated process, starting with target-protein tagging with a polyubiquitine chain by ubiquitin ligases E3 in an ATP dependent manner and ending with degradation by the 26S proteasome, which also requires ATP to assemble 19S and 20S subunits (Goldberg, 2003).
Protein_catabolism (degradation) of UPS
4) Confidence 0.29 Published 2010 Journal Frontiers in Aging Neuroscience Section Body Doc Link PMC2890153 Disease Relevance 0.95 Pain Relevance 0.06
PINK1 and parkin also form a functional E3 ligase complex with DJ-1, which promotes degradation of misfolded parkin substrates by UPS, including parkin itself and synphilin-1.
Protein_catabolism (degradation) of UPS
5) Confidence 0.25 Published 2010 Journal Frontiers in Aging Neuroscience Section Body Doc Link PMC2890153 Disease Relevance 0.67 Pain Relevance 0
Despite the overall rarity of the familiar forms of PD, the identification of single genes linked to the disease has yielded crucial insights into possible mechanisms of the PD pathogenesis, giving strong evidences of the involvement of organelles like mitochondria and intracellular degradation pathways as UPS and autophagy in the pathophysiology of PD (revised in Arduino et al., 2010).
Protein_catabolism (degradation) of UPS associated with disease
6) Confidence 0.25 Published 2010 Journal Frontiers in Aging Neuroscience Section Body Doc Link PMC2890153 Disease Relevance 0.56 Pain Relevance 0
Evidences exists that UPS is the primary mechanism for its degradation (Rideout et al., 2001), but it can be inhibited by alpha-synuclein protofibrils (Zhang et al., 2008).
Protein_catabolism (degradation) of UPS
7) Confidence 0.19 Published 2010 Journal Frontiers in Aging Neuroscience Section Body Doc Link PMC2890153 Disease Relevance 1.07 Pain Relevance 0.04
PINK1 also interacts with Parkin which is responsible for PINK1 homeostasis by ubiquitination and posterior degradation via UPS (Deas et al., 2009).
Protein_catabolism (degradation) of UPS in posterior
8) Confidence 0.19 Published 2010 Journal Frontiers in Aging Neuroscience Section Body Doc Link PMC2890153 Disease Relevance 0.61 Pain Relevance 0
Regarding UPS dysfunction is significant, since proteasome is a major protein degradation cell complex and protein aggregation appears as a main event in PD pathology.
Protein_catabolism (degradation) of UPS associated with disease
9) Confidence 0.19 Published 2010 Journal Frontiers in Aging Neuroscience Section Body Doc Link PMC2890153 Disease Relevance 0.80 Pain Relevance 0
Caspase-3 is required because the UPS minimally degrades the myofibril but rapidly degrades its component proteins.
Protein_catabolism (degrades) of UPS in myofibril
10) Confidence 0.17 Published 2007 Journal Pediatr Nephrol Section Abstract Doc Link PMC2259254 Disease Relevance 1.04 Pain Relevance 0.04
The UPS degrades a specific protein depending on which E3 ubiquitin ligase is activated.
Protein_catabolism (degrades) of UPS
11) Confidence 0.17 Published 2007 Journal Pediatr Nephrol Section Body Doc Link PMC2259254 Disease Relevance 0.97 Pain Relevance 0.07
The UPS readily degrades the main proteins in myofibrils (i.e. actin, myosin, troponin, or tropomyosin), but it does not readily break up the myofibril into its main component proteins [39].
Protein_catabolism (degrades) of UPS in myofibril
12) Confidence 0.17 Published 2007 Journal Pediatr Nephrol Section Body Doc Link PMC2259254 Disease Relevance 0.53 Pain Relevance 0.04
The UPS degrades muscle proteins to provide amino acids that can be converted to glucose (i.e. gluconeogenesis).
Protein_catabolism (degrades) of UPS in muscle
13) Confidence 0.17 Published 2007 Journal Pediatr Nephrol Section Body Doc Link PMC2259254 Disease Relevance 0.27 Pain Relevance 0.03
When we activated caspase-3 in cultured muscle cells, we found that UPS rapidly degraded myofibrillar component proteins, and again, the 14kD C-terminal fragment of actin was left in the muscle cells [40].
Protein_catabolism (degraded) of UPS in muscle cells
14) Confidence 0.15 Published 2007 Journal Pediatr Nephrol Section Body Doc Link PMC2259254 Disease Relevance 0.71 Pain Relevance 0.10
Thousands of proteins have been recognized as being degraded by the UPS, and novel cellular functions are now known to be regulated by Ub conjugation.
Protein_catabolism (degraded) of UPS
15) Confidence 0.15 Published 2007 Journal Pediatr Nephrol Section Body Doc Link PMC2259254 Disease Relevance 0 Pain Relevance 0
Out of several signaling molecules in the downstream of AT1R, the phosphorylation of ERK, but not Akt or STAT3, was required for synaptophysin degradation (Fig. 5), suggesting that the UPS-dependent synaptophysin degradation is mediated by ERK activation.
Protein_catabolism (degradation) of UPS
16) Confidence 0.14 Published 2008 Journal Diabetes Section Body Doc Link PMC2494692 Disease Relevance 0.05 Pain Relevance 0
The ubiquitin-proteasome system (UPS) functions in cellular quality control by degrading misfolded, unassembled, or damaged proteins that could otherwise form potentially toxic aggregates.
Protein_catabolism (degrading) of UPS
17) Confidence 0.12 Published 2008 Journal BMC Infect Dis Section Body Doc Link PMC2442079 Disease Relevance 0.78 Pain Relevance 0.08
We explored the possibility that some protein degradation systems, e.g., the UPS, were disabled or impaired in brains of the experimental CT mice between 4 and 8 wpi.
Protein_catabolism (degradation) of UPS in brains associated with toxocariasis
18) Confidence 0.12 Published 2008 Journal BMC Infect Dis Section Body Doc Link PMC2442079 Disease Relevance 1.30 Pain Relevance 0
Additional evidence linking the UPS to protein degradation in catabolism is the finding that the increase in protein degradation in the muscle of rats with CKD (and other muscle-wasting conditions) can be blocked by inhibitors of the proteasome [5, 6, 33].
Protein_catabolism (degradation) of UPS in muscle associated with chronic renal failure
19) Confidence 0.12 Published 2007 Journal Pediatr Nephrol Section Body Doc Link PMC2259254 Disease Relevance 1.14 Pain Relevance 0.05
Due to the size of the narrow barrel of the proteasome and the specificity of the process, many proteins are unable to be degraded by the UPS, including oligomers or proteins in organelles [1].
Protein_catabolism (degraded) of UPS
20) Confidence 0.11 Published 2008 Journal Biochim Biophys Acta Section Body Doc Link PMC2597715 Disease Relevance 0.25 Pain Relevance 0

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