INT69570

From wiki-pain
Jump to: navigation, search
Context Info
Confidence 0.48
First Reported 1997
Last Reported 2010
Negated 6
Speculated 3
Reported most in Body
Documents 75
Total Number 80
Disease Relevance 44.26
Pain Relevance 4.37

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 9
plaques 4
postsynaptic membrane 3
neurons 2
thalamus 2
Prnp (Mus musculus)
Pain Link Frequency Relevance Heat
long-term potentiation 120 99.72 Very High Very High Very High
Thalamus 229 99.12 Very High Very High Very High
Peripheral nervous system 14 99.04 Very High Very High Very High
Inflammation 63 98.84 Very High Very High Very High
cerebral cortex 22 98.72 Very High Very High Very High
Central nervous system 47 94.96 High High
adenocard 8 93.60 High High
medulla 80 91.76 High High
anesthesia 291 90.32 High High
Spinal cord 14 88.52 High High
Disease Link Frequency Relevance Heat
Creutzfeldt Jakob Disease 1784 100.00 Very High Very High Very High
Scrapie 1050 100.00 Very High Very High Very High
Infection 497 100.00 Very High Very High Very High
Alzheimer's Dementia 426 100.00 Very High Very High Very High
Disease 1536 99.98 Very High Very High Very High
Prion Diseases 370 99.98 Very High Very High Very High
Chronic Wasting Disease 83 99.96 Very High Very High Very High
Neuroblastoma 45 99.56 Very High Very High Very High
Proteostasis Deficiencies 5 99.40 Very High Very High Very High
Neurodegenerative Disease 107 99.32 Very High Very High Very High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
For example, the myc-tagged prion inoculum may allow for investigating the fate of inoculated prions in vivo, since PrPmyc can be detected and traced by tag-specific antibodies which do not recognize endogenous PrP.
PrP Neg (not) Binding (recognize) of
1) Confidence 0.48 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2635968 Disease Relevance 0.37 Pain Relevance 0
In many paradigms, expression of heterologous PrP molecules which differ from the endogenous PrP by as little as one amino acid can profoundly interfere with the overall accumulation of PrPSc [30], [31], suggesting that precise homotypic interactions between PrP molecules are important for PrPSc accumulation [31], [32].
PrP Binding (interactions) of
2) Confidence 0.48 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2635968 Disease Relevance 0.57 Pain Relevance 0
We have exploited this method for identifying several candidate proteins which appear to interact with PrPC in vivo.
PrPC Binding (interact) of
3) Confidence 0.48 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2635968 Disease Relevance 0.26 Pain Relevance 0
Furthermore, PrP association with specific lipid domains in different cellular contexts may influence its cellular transport and thereby determine the differential cellular susceptibility to prion infection.
PrP Binding (association) of associated with infection
4) Confidence 0.47 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2673690 Disease Relevance 0.33 Pain Relevance 0
In addition, GA was unable to inhibit the in vitro transconversion of PrPC in PrPSc in a Protein Misfolded Cyclic Amplification assay (PMCA) and did not directly interact with PrP (Tribouillard-Tanvier et al. submitted), further confirming that this drug is probably not acting in cis on PrP.


PrP Neg (not) Binding (interact) of
5) Confidence 0.47 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2291559 Disease Relevance 0 Pain Relevance 0
Mammalian prions have been most closely associated with PrP that resists protease digestion [4],[5],[6],[7].
PrP Binding (associated) of
6) Confidence 0.47 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2809756 Disease Relevance 0.78 Pain Relevance 0
These changes were not dependent on PrPSc formation, since the protein accumulated in the brain to the same levels as in the untreated mice.
PrPSc Neg (not) Binding (formation) of in brain
7) Confidence 0.41 Published 2010 Journal PLoS Pathogens Section Abstract Doc Link PMC2951383 Disease Relevance 0.72 Pain Relevance 0
In our experiments this interaction could not be initiated by PrP lacking the octapeptide and flanking amino acids (PrP?
PrP Binding (initiated) of
8) Confidence 0.37 Published 2007 Journal Brain Pathology (Zurich, Switzerland) Section Body Doc Link PMC1859984 Disease Relevance 0.66 Pain Relevance 0.12
Since most prion strains are both neurotropic and lymphotropic [47], [48], and inflammatory conditions specify the tropism of prions [49], [50], the interactome of PrPC and PrPSc in lymphoid organs will also be of interest.
PrPSc Binding (interactome) of associated with inflammation and sprains and strains
9) Confidence 0.37 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2635968 Disease Relevance 0.55 Pain Relevance 0.05
Since most prion strains are both neurotropic and lymphotropic [47], [48], and inflammatory conditions specify the tropism of prions [49], [50], the interactome of PrPC and PrPSc in lymphoid organs will also be of interest.
PrPC Binding (interactome) of associated with inflammation and sprains and strains
10) Confidence 0.37 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2635968 Disease Relevance 0.54 Pain Relevance 0.05
We found PrPmyc to be fully functional and substitute dosage-dependently for endogenous PrP in rescuing the neurodegenerative phenotype induced by PrP?
PrP Binding (endogenous) of associated with neurodegenerative disease
11) Confidence 0.37 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2635968 Disease Relevance 0.45 Pain Relevance 0
As the minimal myc epitope tag consists of only 10 amino acids, we reasoned that it might not interfere with the geometry and proper folding of PrPC, and with its function.
PrPC Neg (not) Spec (might) Binding (interfere) of
12) Confidence 0.37 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2635968 Disease Relevance 0.36 Pain Relevance 0
Most of the above processes may require interactions with proteins other than PrP, yet the nature of such interaction partners is largely unknown.
PrP Binding (interactions) of
13) Confidence 0.37 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2635968 Disease Relevance 0.40 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.
PrP Binding (recycling) of
14) Confidence 0.37 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2673690 Disease Relevance 0 Pain Relevance 0
PrP sorting to the endosomal recycling compartment is required for PrPSc production
PrP Binding (sorting) of
15) Confidence 0.37 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2673690 Disease Relevance 0.19 Pain Relevance 0
Immunohistochemistry showed that uni- and multicentric PrP plaques in BSE mice were associated with substantial amounts of granular PrP deposits in the same areas, while diffuse PrP immunoreactivity was weak (Figure 1E and 1F).
PrP Binding (associated) of in plaques associated with creutzfeldt jakob disease
16) Confidence 0.37 Published 2007 Journal PLoS Pathogens Section Body Doc Link PMC1817656 Disease Relevance 1.31 Pain Relevance 0.26
Indeed, recent results showed that depleting PrPC from neurons of prion-infected mice in which the Prnp gene (encoding PrP protein) can be turned off, not only prevented progression of clinical disease, but also reversed spongiosis and early cognitive deficits and neurophysiological dysfunction [2], [3].
Prnp Binding (depleting) of in neurons associated with cognitive disorder and disease
17) Confidence 0.36 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2291559 Disease Relevance 0.89 Pain Relevance 0
PrPres is often equated with PrPSc, and PrPsen with PrPC.
PrPSc Binding (equated) of
18) Confidence 0.36 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2809756 Disease Relevance 0.42 Pain Relevance 0
In the thalamus, where disease was initiated by unilateral inoculation of PrPSc, the conversion of PrPC to rPrPSc (PrP27-30) began unilaterally and then spread bilaterally.
PrPSc Binding (inoculation) of in thalamus associated with thalamus and disease
19) Confidence 0.36 Published 2010 Journal Mol Neurodegener Section Body Doc Link PMC2825502 Disease Relevance 0.18 Pain Relevance 0.21
Once it traverses the synaptic cleft, it can bind to PrPC on the postsynaptic membrane and convert it to rPrPSc, possibly in endosomes by endocytosis of PrPC-PrPSc complex.


PrPC Binding (complex) of in postsynaptic membrane
20) Confidence 0.36 Published 2010 Journal Mol Neurodegener Section Body Doc Link PMC2825502 Disease Relevance 0.31 Pain Relevance 0.12

General Comments

This test has worked.

Personal tools
Namespaces

Variants
Actions
Navigation
Toolbox