INT124164

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Context Info
Confidence 1.00
First Reported 2005
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 20
Total Number 21
Disease Relevance 8.58
Pain Relevance 0.44

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

Golgi apparatus (Prnp) endoplasmic reticulum (Prnp) nucleolus (Prnp)
plasma membrane (Prnp) nucleus (Prnp) cytoplasm (Prnp)
Anatomy Link Frequency
brain 3
neurons 2
cleavage 1
reticulum 1
Prnp (Mus musculus)
Pain Link Frequency Relevance Heat
anesthesia 21 94.16 High High
Inflammation 6 88.12 High High
Eae 4 80.00 Quite High
withdrawal 4 73.20 Quite High
ischemia 88 67.20 Quite High
Hippocampus 23 52.24 Quite High
imagery 54 11.52 Low Low
Thalamus 32 5.00 Very Low Very Low Very Low
medulla 16 5.00 Very Low Very Low Very Low
Central nervous system 11 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Sprains And Strains 232 99.04 Very High Very High Very High
Disease 201 98.70 Very High Very High Very High
Scrapie 259 98.44 Very High Very High Very High
Death 33 98.14 Very High Very High Very High
Injury 14 97.52 Very High Very High Very High
Stress 60 97.36 Very High Very High Very High
Creutzfeldt Jakob Disease 191 91.72 High High
Encephalitis 4 88.12 High High
Prion Diseases 89 86.92 High High
Neurodegenerative Disease 34 78.68 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
In this study we detected an increased degradation of PrPC FL to its breakdown product C1 in the area surrounding the infarct and in the contralateral hemisphere in Prnp+/+ mouse brains.
Protein_catabolism (degradation) of PrPC in brains
1) Confidence 1.00 Published 2007 Journal Brain Pathology (Zurich, Switzerland) Section Body Doc Link PMC1859984 Disease Relevance 0.59 Pain Relevance 0.05
It has been proposed that neuronal death can be triggered by accumulation of PrP in the cytosol because of impairment of proteasomal degradation of misfolded PrP molecules retrotranslocated from the endoplasmic reticulum (Ma, J., Wollmann, R., and Lindquist, S. (2002) Science 298, 1781-1785).
Protein_catabolism (degradation) of PrP in reticulum associated with death
2) Confidence 1.00 Published 2005 Journal J. Biol. Chem. Section Abstract Doc Link 15632159 Disease Relevance 0.32 Pain Relevance 0.09
Altogether, these results indirectly suggest that the observed decrease in PrPSc levels in Rab22-expressing cells is not due to increased delivery and degradation of PrPSc in LEs, but rather is due to impaired scrapie production.
Protein_catabolism (degradation) of PrPSc associated with scrapie
3) Confidence 0.98 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2673690 Disease Relevance 0.10 Pain Relevance 0
In contrast to PrPC, which is completely degraded by PK, only partial degradation of PrPSc occurs in this condition [73].
Protein_catabolism (degradation) of PrPSc
4) Confidence 0.98 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2673690 Disease Relevance 0 Pain Relevance 0
In contrast to PrPC, which is completely degraded by PK, only partial degradation of PrPSc occurs in this condition [73].
Protein_catabolism (degraded) of PrPC
5) Confidence 0.98 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2673690 Disease Relevance 0 Pain Relevance 0
Nonetheless, they do not allow us to discriminate whether the reduction in PrPSc levels is due to impaired production or to enhanced degradation of PrPSc.
Protein_catabolism (degradation) of PrPSc
6) Confidence 0.98 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2673690 Disease Relevance 0 Pain Relevance 0
It is not clear whether autophagy plays a disease promoting role or a disease defensive role since activation of autophagic vacuoles promotes degradation of PrPSc and a prolongation of incubation time [27].
Protein_catabolism (degradation) of PrPSc associated with disease
7) Confidence 0.97 Published 2010 Journal Mol Neurodegener Section Body Doc Link PMC2825502 Disease Relevance 0.56 Pain Relevance 0
On the the other hand, if the decrease of PrPSc levels by Rab22a-expression was not due to increased PrPSc degradation but rather to inhibition of PrPSc synthesis, NH4Cl treatment should not interfere and we should still observe a decrease in PrPSc levels.
Protein_catabolism (degradation) of PrPSc
8) Confidence 0.86 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2673690 Disease Relevance 0.07 Pain Relevance 0
Mangé and coworkers (20) argued that PrPC is first cleaved at the ?
Protein_catabolism (cleaved) of PrPC
9) Confidence 0.66 Published 2007 Journal Brain Pathology (Zurich, Switzerland) Section Body Doc Link PMC1859984 Disease Relevance 0.09 Pain Relevance 0
This finding is in agreement with Mangé’s postulation of increased PrPC degradation under oxidative conditions (20).
Protein_catabolism (degradation) of PrPC
10) Confidence 0.66 Published 2007 Journal Brain Pathology (Zurich, Switzerland) Section Body Doc Link PMC1859984 Disease Relevance 0.66 Pain Relevance 0.03
LSPCs injected intravenously into mice resisted serum degradation and delivered PrP siRNA throughout the brain to AchR and PrPC-expressing neurons.
Protein_catabolism (degradation) of PrPC-expressing in neurons
11) Confidence 0.66 Published 2010 Journal PLoS ONE Section Abstract Doc Link PMC2885418 Disease Relevance 0.14 Pain Relevance 0
LSPCs injected intravenously into mice resisted serum degradation and delivered PrP siRNA throughout the brain to AchR and PrPC-expressing neurons.
Protein_catabolism (degradation) of PrP in neurons
12) Confidence 0.66 Published 2010 Journal PLoS ONE Section Abstract Doc Link PMC2885418 Disease Relevance 0.14 Pain Relevance 0
Moreover, PrPSc is cleaved at its N-terminus by endogenous proteases in acidic compartments immediately after its generation [3],[16], suggesting that its conversion to a protease-resistant state occurs prior to its exposure to proteases within an endo-lysosomal compartment.
Protein_catabolism (cleaved) of PrPSc
13) Confidence 0.65 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2673690 Disease Relevance 0.19 Pain Relevance 0
In particular, it is possible that impairment of PrP recycling in GFP-Rab22a expressing cells could divert PrP towards a degradation pathway.
Protein_catabolism (degradation) of PrP
14) Confidence 0.65 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2673690 Disease Relevance 0 Pain Relevance 0
Furthermore they reported that the octapeptide repeat region of PrPC undergoes a site-specific copper- and pH-dependent cleavage, which has vast implications for further proteolysis.
Protein_catabolism (proteolysis) of PrPC in cleavage
15) Confidence 0.58 Published 2007 Journal Brain Pathology (Zurich, Switzerland) Section Body Doc Link PMC1859984 Disease Relevance 0.10 Pain Relevance 0
To further test this hypothesis and to discriminate between increased degradation and decreased production of PrPSc, we compared the levels of PrPSc in control cells and in cells transfected with GFP-Rab22a after treating them with ammonium chloride (NH4Cl), which impairs lysosomal degradation [43].
Protein_catabolism (degradation) of PrPSc
16) Confidence 0.57 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2673690 Disease Relevance 0.10 Pain Relevance 0
PrPSc is distinguished from PrPC on the basis of protease resistance: protease partly degrades PrPSc to form a protease-resistant C-terminal core fragment (PrPres), that has an unglycosylated form with a molecular weight of 19–21 kDa.
Protein_catabolism (degrades) of PrPSc
17) Confidence 0.55 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2982847 Disease Relevance 1.35 Pain Relevance 0
PrPSc is distinguished from PrPC on the basis of protease resistance: protease partly degrades PrPSc to form a protease-resistant C-terminal core fragment (PrPres), that has an unglycosylated form with a molecular weight of 19–21 kDa.
Protein_catabolism (degrades) of PrPSc
18) Confidence 0.55 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2982847 Disease Relevance 1.37 Pain Relevance 0
The biochemical characteristics of PrPSc were also different in PGP-h1, mostly in terms of the higher quantity of PrPSc accumulated in the brain and the lower relative resistance to proteolytic degradation than the other hamster strains analyzed.
Protein_catabolism (degradation) of PrPSc in brain associated with sprains and strains
19) Confidence 0.48 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2675078 Disease Relevance 1.02 Pain Relevance 0.12
The biochemical characteristics of PrPSc were also different in PGP-h1, mostly in terms of the higher quantity of PrPSc accumulated in the brain and the lower relative resistance to proteolytic degradation than the other hamster strains analyzed.
Protein_catabolism (degradation) of PrPSc in brain associated with sprains and strains
20) Confidence 0.41 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2675078 Disease Relevance 0.99 Pain Relevance 0.12

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