|
Prion Diseases
|
0.200 |
Biomarker
|
group |
BEFREE |
Taken together, our study revealed a chaperon-like activity of αS against PrP amyloidogenesis, suggesting a possible involvement of αS in the pathology of TSEs.
|
31635805 |
2020 |
|
Prion Diseases
|
0.200 |
GeneticVariation
|
group |
BEFREE |
The clinical and pathological differences between synucleinopathies such as Parkinson's disease and multiple system atrophy have been postulated to stem from unique strains of α-synuclein aggregates, akin to what occurs in prion diseases.
|
31792467 |
2020 |
|
Prion Diseases
|
0.200 |
Biomarker
|
group |
BEFREE |
The confirmed transmission of α-synuclein prions to a second synucleinopathy model and the ability to propagate prions between two distinct mouse lines while retaining strain-specific properties provides compelling evidence that MSA is a prion disease.
|
30690664 |
2019 |
|
Prion Diseases
|
0.200 |
Biomarker
|
group |
BEFREE |
Quantification of CSF α-synuclein (a-syn) by an in-house ECL-based ELISA assay has been recently reported as an excellent approach for the diagnosis of sporadic Creutzfeldt-Jakob disease (sCJD), the most prevalent form of human prion disease.
|
28321768 |
2018 |
|
Prion Diseases
|
0.200 |
Biomarker
|
group |
BEFREE |
Protein misfolding diseases are usually associated with deposits of single "key" proteins that somehow drive the pathology; β-amyloid and hyperphosphorylated tau accumulate in Alzheimer's disease, α-synuclein in Parkinson's disease, or abnormal prion protein (PrPTSE) in transmissible spongiform encephalopathies (TSEs or prion diseases).
|
30427511 |
2018 |
|
Prion Diseases
|
0.200 |
Biomarker
|
group |
BEFREE |
Evidence is now emerging that α-synuclein aggregates can have different protein conformations, referred to as strains, similar to what has been shown in prion disease.
|
28213435 |
2018 |
|
Prion Diseases
|
0.200 |
Biomarker
|
group |
BEFREE |
Pre-existing α-synuclein fibrils can recruit and convert soluble non-fibrillar α-synuclein to the fibrillar form similar to what is observed in prion diseases.
|
29550546 |
2018 |
|
Prion Diseases
|
0.200 |
Biomarker
|
group |
BEFREE |
We established the clinical parameters for prion disease diagnosis for the quantification of CSF α-synuclein in patients with sporadic (n = 234) and genetic (n = 56) prion diseases, in cases with cognitive impairment/dementia or neurodegenerative disease (n = 278), and in the neurologic control group (n = 111).
|
27870938 |
2017 |
|
Prion Diseases
|
0.200 |
Biomarker
|
group |
BEFREE |
In this review, we document research progress on the molecular and mesoscopic self-assembly of amyloid-beta, alpha synuclein, human islet amyloid polypeptide and prions, the peptides and proteins associated with Alzheimer's, Parkinson's, type 2 diabetes and prion diseases.
|
28702523 |
2017 |
|
Prion Diseases
|
0.200 |
Biomarker
|
group |
BEFREE |
The expression "prion-like diseases" refers to a group of neurodegenerative diseases that share some neuropathological features with prion diseases such as the involvement of proteins (α-synuclein, amyloid β, and tau) able to precipitate producing amyloid deposits following conformational change.
|
28154522 |
2017 |
|
Prion Diseases
|
0.200 |
Biomarker
|
group |
BEFREE |
The current study demonstrates that aggregated α-synuclein is potent in cross-seeding of prion protein misfolding and aggregation in vitro, producing self-replicating states that can lead to transmissible prion diseases upon serial passaging in wild type animals.
|
28797122 |
2017 |
|
Prion Diseases
|
0.200 |
Biomarker
|
group |
BEFREE |
Recently, increasing evidence has demonstrated the existence of different structural characteristics or 'strains' of α-Syn, supporting the concept that synucleinopathies share several common features with prion diseases and possibly explaining how a single protein results in different clinical phenotypes within synucleinopathies.
|
27853185 |
2016 |
|
Prion Diseases
|
0.200 |
Biomarker
|
group |
BEFREE |
However, with the mNS prion strain there was a modest but significant acceleration in the time to terminal prion disease in mice having α-synuclein aggregates as compared with non-tg mice.
|
22460692 |
2013 |
|
Prion Diseases
|
0.200 |
GeneticVariation
|
group |
GWASDB |
Genome-wide association study in multiple human prion diseases suggests genetic risk factors additional to PRNP.
|
22210626 |
2012 |
|
Prion Diseases
|
0.200 |
GeneticVariation
|
group |
BEFREE |
Prion protein (Prion diseases), amyloid-beta (Alzheimer's disease), alpha-synuclein (Parkinson's disease), Huntingtin (Huntington's disease), serum amyloid A (AA amyloidosis) and islet amyloid polypeptide (type 2 diabetes) are some of the proteins that trigger disease when they get misfolded.
|
21571086 |
2011 |
|
Prion Diseases
|
0.200 |
Biomarker
|
group |
BEFREE |
In addition to the prion protein, deposition of tau, α-synuclein, and amyloid-β has been reported in human prion disease.
|
20593190 |
2011 |
|
Prion Diseases
|
0.200 |
Biomarker
|
group |
BEFREE |
Identification of alpha-synuclein as the first of the loci involved in Parkinson's disease and the identification of this protein in pathological deposits in other disorders has led to the suggestion that it may share pathogenic mechanisms with multiple system atrophy, Alzheimer's disease and prion disease and that these mechanisms are related to a synuclein pathway to cell death.
|
10469843 |
1999 |