|
Prion Diseases
|
0.500 |
GeneticVariation
|
group |
BEFREE |
Here we introduce several PRNP gene mutations (such as, PrP-KDEL, PrP-3AV, PrP-A117V, PrP-G114V, PrP-P102L and PrP-E200K) into the cultured cells in order to explore the pathogenic mechanism of familial prion disease.
|
21298055 |
2011 |
|
Prion Diseases
|
0.500 |
GeneticVariation
|
group |
BEFREE |
Compared to ND, t-PrP concentrations were significantly decreased in sCJD, iCJD and in genetic prion diseases associated with the three most common mutations E200K, V210I (associated with genetic CJD) and D178N-129M (associated with fatal familial insomnia).
|
30062673 |
2019 |
|
Prion Diseases
|
0.500 |
Biomarker
|
group |
BEFREE |
The main cause for the development of transmissible spongiform encephalopathies (TSE) is the conformational change of prion protein from the normal cellular isoform (PrP(C)) into the abnormal isoform, named prion (PrP(Sc)).
|
17884181 |
2007 |
|
Prion Diseases
|
0.500 |
Biomarker
|
group |
BEFREE |
The development of transmissible spongiform encephalopathies (TSEs) is associated with the conversion of the cellular prion protein (PrP(C)) into a misfolded, pathogenic isoform (PrP(Sc)).
|
21839748 |
2011 |
|
Prion Diseases
|
0.500 |
Biomarker
|
group |
BEFREE |
Cellular prion protein (PrP<sup>C</sup> ) is infamous for its role in prion diseases.
|
31736091 |
2020 |
|
Prion Diseases
|
0.500 |
Biomarker
|
group |
BEFREE |
The presence of PrP-immunoreactive patches with unique morphology in the molecular layer of the cerebellum is a hallmark of certain prion encephalopathies with insertional mutations and is useful in the diagnosis of this subtype of human prion disease.
|
9222181 |
1997 |
|
Prion Diseases
|
0.500 |
Biomarker
|
group |
BEFREE |
The PrP or prion protein plays a key role in the pathogenesis of the transmissible spongiform encephalopathies.
|
8137132 |
1993 |
|
Prion Diseases
|
0.500 |
GeneticVariation
|
group |
BEFREE |
Valine-to-isoleucine substitution at codon 180 of the prion protein gene is only observed in patients with Creutzfeldt-Jakob disease and accounts for approximately half of all cases of genetic prion disease in Japan.
|
29382530 |
2018 |
|
Prion Diseases
|
0.500 |
Biomarker
|
group |
BEFREE |
Transmissible spongiform encephalopathies are associated with the conversion of cellular prion protein, PrP(C), into a misfolded oligomeric form, PrP(Sc).
|
12356762 |
2002 |
|
Prion Diseases
|
0.500 |
GeneticVariation
|
group |
BEFREE |
A total of 10-15% of human transmissible spongiform encephalopathies (TSEs) or prion diseases are characterised by disease-specific mutations in the prion protein gene (PRNP).
|
16187142 |
2005 |
|
Prion Diseases
|
0.500 |
Biomarker
|
group |
BEFREE |
Recently, testing of CSF with a new in vitro abnormal prion protein amplification technology, designated real-time quaking-induced conversion (RT-QUIC), has shown considerable promise as a highly specific diagnostic test for human prion disease.
|
28861798 |
2017 |
|
Prion Diseases
|
0.500 |
Biomarker
|
group |
BEFREE |
Transmissible spongiform encephalopathies - also known as prion-related diseases - are a group of fatal neurodegenerative disorders associated with the misfolding of prion protein.
|
11286781 |
2001 |
|
Prion Diseases
|
0.500 |
GeneticVariation
|
group |
BEFREE |
Prion diseases are a group of rare, fatal neurodegenerative disorders associated with a conformational transformation of the cellular prion protein (PrP(C)) into a self-replicating and proteinase K-resistant conformer, termed scrapie PrP (PrP(Sc)).
|
22362783 |
2012 |
|
Prion Diseases
|
0.500 |
GeneticVariation
|
group |
BEFREE |
Mutations and polymorphisms in the sequence of the coding region of the prion protein gene (PRNP) have been established as an important factor in all of these three types of prion diseases.
|
10987652 |
1999 |
|
Prion Diseases
|
0.500 |
GeneticVariation
|
group |
BEFREE |
Among the dozen known mutations in the PrP gene which segregate with the inherited prion diseases, only 2 mutations have been described in Israel so far: the codon 200 mutation in Creutzfeldt-Jakob disease (CJD) affected Libyan Jews, and the codon 102 mutation in 1 Jewish Gerstmann-Straussler-Scheinker (GSS) affected pedigree of German origin.
|
9531435 |
1998 |
|
Prion Diseases
|
0.500 |
GeneticVariation
|
group |
BEFREE |
We describe the neuropsychological profiles of 10 cases and compare these data with cross sectional data obtained from patients with histologically confirmed sporadic CJD and cases with inherited prion disease with confirmed mutations in the prion protein gene.
|
15716521 |
2005 |
|
Prion Diseases
|
0.500 |
GeneticVariation
|
group |
BEFREE |
Prominent psychiatric features and early onset in an inherited prion disease with a new insertional mutation in the prion protein gene.
|
10581230 |
1999 |
|
Prion Diseases
|
0.500 |
GeneticVariation
|
group |
BEFREE |
Mutations in the coding region of the prion protein (PRNP) gene are linked to inherited forms of TSEs whereas aetiology of sporadic CJD (sCJD) remains obscure.
|
22505365 |
2012 |
|
Prion Diseases
|
0.500 |
Biomarker
|
group |
BEFREE |
The cases illustrate the histological variability that can occur in familial prion diseases despite similarity in PrP staining.
|
12662318 |
2003 |
|
Prion Diseases
|
0.500 |
Biomarker
|
group |
BEFREE |
Protein amplification techniques exploit the ability of PrP<sup>TSE</sup> to induce a conformational change in prion protein (PrP) in a continuous fashion, so that the small amount of PrP<sup>TSE</sup> found in tissues and biologic fluids in prion diseases can be amplified to a point where they are detectable by conventional laboratory techniques.
|
29887145 |
2018 |
|
Prion Diseases
|
0.500 |
Biomarker
|
group |
BEFREE |
Prion diseases are associated with the misfolding of the prion protein (PrP) from its normal cellular form (PrP<sup>C</sup> ) to its infectious scrapie form (PrP<sup>S</sup><sup>c</sup> ).
|
28407243 |
2017 |
|
Prion Diseases
|
0.500 |
Biomarker
|
group |
BEFREE |
Association of prion protein genotype and scrapie prion protein type with cellular prion protein charge isoform profiles in cerebrospinal fluid of humans with sporadic or familial prion diseases.
|
24360565 |
2014 |
|
Prion Diseases
|
0.500 |
GeneticVariation
|
group |
BEFREE |
These diseases, known as prion diseases, are thought to involve a self-perpetuating change in the conformation of the prion protein (PrP) from a soluble form to one reflecting amyloid structure.
|
15126688 |
2004 |
|
Prion Diseases
|
0.500 |
Biomarker
|
group |
BEFREE |
While loss of function of PrP does not elicit apparent phenotypes, generation of misfolded forms of the protein or its aberrant metabolic isoforms has been implicated in a number of neurodegenerative disorders such as scrapie, kuru, Creutzfeldt-Jakob disease, fatal familial insomnia, Gerstmann-Sträussler-Scheinker and bovine spongiform encephalopathy.
|
28421536 |
2018 |
|
Prion Diseases
|
0.500 |
Biomarker
|
group |
BEFREE |
Cellular prion protein (PrP<sup>C</sup>), the infective agent of transmissible spongiform encephalopathies, is thought to be related to several cellular physiological and physiopathological processes.
|
29069734 |
2017 |