INT102745

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Context Info
Confidence 0.61
First Reported 2002
Last Reported 2010
Negated 1
Speculated 2
Reported most in Body
Documents 17
Total Number 19
Disease Relevance 12.41
Pain Relevance 0.78

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
muscle 7
neuronal 2
liver 1
satellite cells 1
neurons 1
Hmbs (Mus musculus)
Pain Link Frequency Relevance Heat
Inflammation 96 98.68 Very High Very High Very High
Glutamate receptor 3 83.16 Quite High
palliative 6 79.64 Quite High
abdominal pain 3 75.36 Quite High
cytokine 33 71.92 Quite High
Dopamine 33 67.92 Quite High
Glutamate 6 49.44 Quite Low
Pain 8 43.92 Quite Low
tetrodotoxin 4 27.84 Quite Low
fibrosis 8 21.52 Low Low
Disease Link Frequency Relevance Heat
Disease 342 99.82 Very High Very High Very High
Chronic Renal Failure 225 99.80 Very High Very High Very High
Frailty 172 99.80 Very High Very High Very High
Porphyria 15 99.68 Very High Very High Very High
Muscular Atrophy 45 99.66 Very High Very High Very High
Acid Base Imbalance 48 99.36 Very High Very High Very High
INFLAMMATION 120 98.68 Very High Very High Very High
Parkinson's Disease 147 98.46 Very High Very High Very High
Insulin Resistance 72 98.40 Very High Very High Very High
Acidosis 48 98.00 Very High Very High Very High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Further addition of DNA increased the PBGD activity up to threefold the normal value.
Positive_regulation (increased) of PBGD
1) Confidence 0.61 Published 2002 Journal Scand. J. Clin. Lab. Invest. Section Abstract Doc Link 12004925 Disease Relevance 0.34 Pain Relevance 0.12
When these vectors were used to deliver the PBGD gene into the AIP mouse model no enhancement of the endogenous PBGD activity in liver was detectable, despite the presence of the PBGD-plasmids as verified by PCR.
Neg (no) Positive_regulation (enhancement) of PBGD in liver associated with porphyria
2) Confidence 0.60 Published 2004 Journal Mol. Genet. Metab. Section Abstract Doc Link 15110317 Disease Relevance 0.55 Pain Relevance 0.11
Thus, the PBGD activity was increased 3-10 times in NIH 3T3 cells and 95-240 times in HeLa cells.
Positive_regulation (increased) of PBGD in HeLa
3) Confidence 0.41 Published 2002 Journal Scand. J. Clin. Lab. Invest. Section Abstract Doc Link 12004925 Disease Relevance 0.54 Pain Relevance 0.15
Thus, parkin over-expression may be a therapeutic strategy for PD, due to increased UPS activity and misfolded proteins clearance, avoiding aggregates-induced cell death.
Positive_regulation (increased) of UPS associated with disease and death
4) Confidence 0.20 Published 2010 Journal Frontiers in Aging Neuroscience Section Body Doc Link PMC2890153 Disease Relevance 0.49 Pain Relevance 0
Excessive ROS/RNS formation by these two processes may induce UPS impairment and/or misfolding of molecular chaperons, thus resulting in protein aggregation and neuronal damage (Nakamura and Lipton, 2009).
Spec (may) Positive_regulation (induce) of UPS in neuronal
5) Confidence 0.14 Published 2010 Journal Frontiers in Aging Neuroscience Section Body Doc Link PMC2890153 Disease Relevance 0.71 Pain Relevance 0.10
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.
Spec (may) Positive_regulation (indicate) of UPS associated with parkinson's disease and disease
6) Confidence 0.14 Published 2010 Journal Frontiers in Aging Neuroscience Section Body Doc Link PMC2890153 Disease Relevance 0.65 Pain Relevance 0
Patients with different clinical conditions associated with muscle atrophy exhibit similar increases in mRNAs encoding components of the UPS (e.g. an increase in mRNAs encoding Ub and proteasome subunits) [11, 29–31].
Positive_regulation (increases) of UPS in muscle associated with muscular atrophy
7) Confidence 0.12 Published 2007 Journal Pediatr Nephrol Section Body Doc Link PMC2259254 Disease Relevance 0.98 Pain Relevance 0
The finding that various diseases with muscle wasting are caused by activation of the UPS, plus the fact that coordinated changes in the expression of genes in muscle occur in different catabolic states, suggest that catabolic states activate a common cellular signaling pathway [28].
Positive_regulation (activation) of UPS in muscle associated with frailty and disease
8) Confidence 0.12 Published 2007 Journal Pediatr Nephrol Section Body Doc Link PMC2259254 Disease Relevance 1.56 Pain Relevance 0.03
The principal mechanism causing muscle atrophy in CKD involves activation of the UPS.
Positive_regulation (activation) of UPS in muscle associated with chronic renal failure and muscular atrophy
9) Confidence 0.12 Published 2007 Journal Pediatr Nephrol Section Body Doc Link PMC2259254 Disease Relevance 0.96 Pain Relevance 0
The activation of atrogin-1, and hence the UPS, involves another mechanism: changes in activity of the fork-head transcription factors (FoxO 1, 3 and 4).
Positive_regulation (activation) of UPS in head
10) Confidence 0.12 Published 2007 Journal Pediatr Nephrol Section Body Doc Link PMC2259254 Disease Relevance 0.42 Pain Relevance 0.13
The mechanism by which metabolic acidosis causes muscle wasting involves activation of the UPS and caspase-3 [40, 43].
Positive_regulation (activation) of UPS in muscle associated with frailty and acid base imbalance
11) Confidence 0.10 Published 2007 Journal Pediatr Nephrol Section Body Doc Link PMC2259254 Disease Relevance 1.44 Pain Relevance 0.05
Interestingly, angiotensin II/AT1R signaling proved to cause the activation of the UPS, leading to synaptophysin degradation in neuronal cells (Fig. 4G–I).
Positive_regulation (activation) of UPS in neuronal
12) Confidence 0.10 Published 2008 Journal Diabetes Section Body Doc Link PMC2494692 Disease Relevance 0.14 Pain Relevance 0
ERK activation results in: 1) hyperexpression of the muscle-specific ubiquitin ligase atrogin-1, suggesting that an upregulation of UPS activity eventually supports protein hypercatabolism; 2) downregulation of the myogenic process, characterized by accumulation of activated satellite cells not competent to proceed into the differentiative program.
Positive_regulation (upregulation) of UPS in satellite cells
13) Confidence 0.09 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2965098 Disease Relevance 0.56 Pain Relevance 0
It is now known that complications of these various disorders, including acidosis, insulin resistance, inflammation, and increased glucocorticoid and angiotensin II production, all activate the ubiquitin–proteasome system (UPS) to degrade muscle proteins.
Positive_regulation (activate) of UPS in muscle associated with acidosis, inflammation and insulin resistance
14) Confidence 0.08 Published 2007 Journal Pediatr Nephrol Section Abstract Doc Link PMC2259254 Disease Relevance 1.13 Pain Relevance 0.05
Patients with different clinical conditions associated with muscle atrophy exhibit similar increases in mRNAs encoding components of the UPS (e.g. an increase in mRNAs encoding Ub and proteasome subunits) [11, 29–31].
Positive_regulation (increase) of UPS in muscle associated with muscular atrophy
15) Confidence 0.08 Published 2007 Journal Pediatr Nephrol Section Body Doc Link PMC2259254 Disease Relevance 0.97 Pain Relevance 0
Third, the increase in muscle protein degradation in uremia and most other catabolic disease states is mostly due to programmed activation of the ubiquitin–proteasome system (UPS) [5, 11].
Positive_regulation (activation) of UPS in muscle associated with chronic renal failure and disease
16) Confidence 0.08 Published 2007 Journal Pediatr Nephrol Section Body Doc Link PMC2259254 Disease Relevance 0.80 Pain Relevance 0.04
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.
Positive_regulation (mediated) of UPS
17) Confidence 0.07 Published 2008 Journal Diabetes Section Body Doc Link PMC2494692 Disease Relevance 0.05 Pain Relevance 0
Although the UPS was recently shown to play a role in the degradation of several synaptic proteins (25–27), the present data are the first to reveal the RAS-mediated UPS activation for synaptic protein degradation in neurons.
Positive_regulation (activation) of UPS in neurons
18) Confidence 0.07 Published 2008 Journal Diabetes Section Body Doc Link PMC2494692 Disease Relevance 0.12 Pain Relevance 0
This is supported by several recent studies showing that the activation of the ERK pathway promoted the UPS-mediated degradation of the cell cycle protein Cdc25 (40,41) and the cell survival factor Bim (42).
Positive_regulation (promoted) of UPS
19) Confidence 0.07 Published 2008 Journal Diabetes Section Body Doc Link PMC2494692 Disease Relevance 0 Pain Relevance 0

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