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Neurodegenerative Disorders
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0.100 |
GeneticVariation
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group |
BEFREE |
Here we present a unique case to demonstrate that energy migration can be a novel and sensitive readout to capture the membrane-mediated misfolding and oligomerization of the human prion protein (PrP), which is known to undergo an aberrant conformational conversion from an α-helical form into a self-propagating aggregated β-rich state causing deadly transmissible neurodegenerative diseases.
|
31740413 |
2020 |
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Neurodegenerative Disorders
|
0.100 |
GeneticVariation
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group |
BEFREE |
The structure of the infectious PrP rods, which cause lethal neurodegeneration, readily differentiates them from all other protein assemblies so far characterised in other neurodegenerative diseases.
|
30675000 |
2019 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
Misfolding and aggregation of prion protein (PrP) causes neurodegenerative diseases like Creutzfeldt-Jakob disease (CJD) and scrapie.
|
30792490 |
2019 |
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Neurodegenerative Disorders
|
0.100 |
GeneticVariation
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group |
BEFREE |
Prion diseases are fatal neurodegenerative disorders related to the conformational alteration of the prion protein (PrP C) into a pathogenic and protease-resistant isoform (PrPSc).
|
31371089 |
2019 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
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group |
BEFREE |
The abnormal assembly of tau, α-synuclein (αSyn), or prion protein into oligomers and multimers underpins the molecular pathogenesis of multiple neurodegenerative diseases.
|
30341601 |
2019 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
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group |
BEFREE |
Finally, our framework was extended as a differential diagnosis tool to identify both forms of CJD among another neurodegenerative disease.
|
31734530 |
2019 |
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Neurodegenerative Disorders
|
0.100 |
GeneticVariation
|
group |
BEFREE |
Prion diseases are fatal neurodegenerative disorders associated with the deposition of abnormal prion protein aggregates (PrP<sup>Sc</sup>) in the brain tissue.
|
30875466 |
2019 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
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group |
BEFREE |
This review highlights some important metabolic alterations detected in neurodegeneration caused by misfolded prion protein and discusses common toxicity pathways identified across different neurodegenerative diseases.
|
30539802 |
2019 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
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group |
BEFREE |
The discovery that prion protein can misfold into a pathological conformation that encodes structural information capable of both propagation and inducing severe neuropathology has revolutionized our understanding of neurodegenerative disease.
|
31736708 |
2019 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
Surveillance for variant CJD: should more children with neurodegenerative diseases have autopsies?
|
30337492 |
2019 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
This case highlights the clinical heterogeneity of sCJD presentation and the important inclusion of CJD in the differential diagnosis of atypical presentations of neurodegenerative disease.
|
30850568 |
2019 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
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group |
BEFREE |
We identified 70 additional novel and missense variants in other genes, such as MAPT, GRN, CSF1R, and PRNP, related to neurodegenerative diseases, which may represent overlapping clinical and neuropathological features with AD.
|
31182772 |
2019 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
Prions are clearly distinguishable from non-infectious recombinant PrP fibrils generated <i>in vitro</i> and from all other propagating protein structures so far described in other neurodegenerative diseases.
|
31338021 |
2019 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
Misfolded and abnormal β-sheets forms of wild-type proteins, such as cellular prion protein (PrP<sup>C</sup>) and amyloid beta (Aβ), are believed to be the vectors of neurodegenerative diseases, prion and Alzheimer's disease (AD), respectively.
|
31547531 |
2019 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
Prion diseases are a group of neurodegenerative disorders associated with the conformational conversion of the cellular prion protein (PrP<sup>C</sup>) into an abnormal misfolded form named PrP<sup>Sc</sup>.
|
31041657 |
2019 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
<b>Introduction</b>: Human prion diseases are rare fatal neurodegenerative diseases caused by the misfolding and aggregation of the prion protein in the form of infectious prions.So far, these diseases are incurable.
|
31271065 |
2019 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
In this review, we assess the prospective global dissemination of advanced cell therapies founded on transplantation or exposure to allogeneic human cells, recap lessons learned from the historical precedents of CJD transmission and review recent advances and current limits in understanding of prion and other neurodegenerative disease prion-like susceptibility and transmission.
|
30483944 |
2019 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
Human prion protein is a subject of extensive study, related in particular to the molecular basis of neurodegenerative disease development and prevention.
|
30756103 |
2019 |
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Neurodegenerative Disorders
|
0.100 |
GeneticVariation
|
group |
BEFREE |
In mammals, pathological aggregation of the prion protein causes incurable neurodegenerative disorders, while in yeast <i>Saccharomyces cerevisiae</i>, prion formation may be neutral or even beneficial.
|
30871095 |
2019 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
The cellular prion protein (PrP<sup>C</sup>), mainly known for its role in neurodegenerative diseases, is involved in several physiological processes including neuritogenesis.
|
30729399 |
2019 |
|
Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
A conformational change from normal prion protein(PrP<sup>C</sup>) to abnormal prion protein(PrP<sup>SC</sup>) induces fatal neurodegenerative diseases.
|
31848406 |
2019 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
Together with several other discoveries at the beginning of the 1990s, PrP106-126 contributed to underpin the role of amyloid in the pathogenesis of protein-misfolding neurodegenerative disorders.
|
30635947 |
2019 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
Misfolding and aggregation of the prion protein is responsible for multiple neurodegenerative diseases.
|
29789820 |
2018 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
The presence of pathology related to the deposition of amyloid-β (Aβ) has been recently reported in iatrogenic Creutzfeldt-Jakob disease (iCJD) acquired from inoculation of growth hormone (GH) extracted from human cadaveric pituitary gland or use of cadaveric dura mater (DM) grafts.To investigate this phenomenon further, a cohort of 27 iCJD cases - 21 with adequate number of histopathological sections - originating from Australia, France, Italy, and the Unites States, were examined by immunohistochemistry, amyloid staining, and Western blot analysis of the scrapie prion protein (PrP<sup>Sc</sup>), and compared with age-group matched cases of sporadic CJD (sCJD), Alzheimer disease (AD) or free of neurodegenerative diseases (non-ND).Cases of iCJD and sCJD shared similar profiles of proteinase K-resistant PrP<sup>Sc</sup> with the exception of iCJD harboring the "MMi" phenotype.
|
29310723 |
2018 |
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Neurodegenerative Disorders
|
0.100 |
Biomarker
|
group |
BEFREE |
This fatal neurodegenerative disease is caused by misfolding of the cellular prion protein to pathogenic β-rich conformers (PrPSc) that accumulate in higher order structures of the brain and other tissues.
|
30571737 |
2018 |