Prion Diseases
|
0.500 |
Biomarker
|
group |
BEFREE |
"Life, Jim, but not as we know it"? Transmissible dementias and the prion protein.
|
2054560 |
1991 |
Prion Diseases
|
0.500 |
GeneticVariation
|
group |
BEFREE |
15% of prion diseases are autosomal dominant genetic disorders associated with mutations in the gene encoding the prion protein.
|
8100163 |
1993 |
Prion Diseases
|
0.500 |
Biomarker
|
group |
BEFREE |
Transmissible spongiform encephalopathies(TSEs) or prion diseases are a closely related group of diseases, whose exact etiology is unknown, but is generally accepted to be related to protease-resistant prion protein PrP.
|
10790749 |
2000 |
Prion Diseases
|
0.500 |
Biomarker
|
group |
BEFREE |
Prion diseases such as Creutzfeldt-Jakob disease (CJD) are associated in most cases with the accumulation of an unusual isoform of prion protein (PrPSC).
|
11200684 |
2000 |
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 |
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 |
Prion diseases (also known as transmissible spongiform encephalopathies) are associated with the conversion of the normal cellular form of the prion protein (PrPC) to an abnormal scrapie-isoform (PrP(Sc).
|
12392052 |
2002 |
Prion Diseases
|
0.500 |
Biomarker
|
group |
BEFREE |
Prion diseases are characterized by the accumulation in the brain of a misfolded and protease-resistant form of the prion protein (PrP(c)).
|
12782344 |
2003 |
Prion Diseases
|
0.500 |
Biomarker
|
group |
BEFREE |
Transmissible spongiform encephalopathies (TSEs) do not go along with inflammatory infiltrates, and antibodies to the prion protein are not typically raised during the course of the disease.
|
14522856 |
2003 |
Prion Diseases
|
0.500 |
Biomarker
|
group |
BEFREE |
Prion diseases are closely associated with the conversion of the cellular prion protein (PrPC) to an abnormal conformer (PrPSc) [Prusiner, S. B.(1998) Proc.Natl.Acad.Sci.USA 95, 13363-13383].
|
15240877 |
2004 |
Prion Diseases
|
0.500 |
Biomarker
|
group |
BEFREE |
Transmissible spongiform encephalopathies are thought by some to result from changes in the conformation of a membrane glycoprotein called PrPC (prion protein) into a pathogenic form, PrPSc, which constitutes the major component of an unprecedented type of infectious particle supposedly devoid of nucleic acid.
|
15357900 |
2004 |
Prion Diseases
|
0.500 |
Biomarker
|
group |
BEFREE |
Prion diseases are transmissible fatal neurodegenerative disorders in which infectivity is associated with the accumulation of PrP(Sc), a disease-related isoform of normal cellular prion protein.
|
15542971 |
2004 |
Prion Diseases
|
0.500 |
Biomarker
|
group |
BEFREE |
Prion diseases are a group of neurodegenerative disorders associated with conversion of a normal prion protein, PrPC, into a pathogenic conformation, PrPSc.
|
15557265 |
2004 |
Prion Diseases
|
0.500 |
GeneticVariation
|
group |
BEFREE |
Prion diseases are associated with the accumulation of a misfolded, protease resistant form of the prion protein, PrPres.
|
15851854 |
2005 |
Prion Diseases
|
0.500 |
GeneticVariation
|
group |
BEFREE |
Prion diseases are neurodegenerative disorders associated in most cases with the accumulation in the central nervous system of PrPSc (conformationally altered isoform of cellular prion protein (PrPC); Sc for scrapie), a partially protease-resistant isoform of the PrPC.
|
16724107 |
2006 |
Prion Diseases
|
0.500 |
GeneticVariation
|
group |
BEFREE |
Prion diseases are caused by a unique type of infectious agent, which is thought to consist of a misfolded beta-sheeted form of the alpha-helical cellular prion protein (PrPC).
|
16911960 |
2006 |
Prion Diseases
|
0.500 |
Biomarker
|
group |
CTD_human |
Prion diseases are caused by the misfolding and aggregation of the prion protein (PrP).
|
17257012 |
2007 |
Prion Diseases
|
0.500 |
Biomarker
|
group |
BEFREE |
Prion diseases such as bovine spongiform encephalopathy in cattle and Creutzfeldt-Jakob disease in humans are associated with the misfolding and accumulation of an abnormal conformation of the host-encoded prion protein (PrP).
|
17944867 |
2007 |
Prion Diseases
|
0.500 |
GeneticVariation
|
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 PrP(Sc).
|
19075585 |
2008 |
Prion Diseases
|
0.500 |
Biomarker
|
group |
BEFREE |
Prion diseases are characterized by the conformational transition of the cellular prion protein (PrP(C)) into an aberrant protein conformer, designated scrapie-prion protein (PrP(Sc)).
|
19767654 |
2010 |
Prion Diseases
|
0.500 |
GeneticVariation
|
group |
BEFREE |
Transmissible spongiform encephalopathies (TSEs) are neurodegenerative disorders caused by PrP(Sc), or prion, an abnormally folded form of the cellular prion protein (PrP(C)).
|
20394048 |
2010 |
Prion Diseases
|
0.500 |
GeneticVariation
|
group |
BEFREE |
Prion diseases are disorders affecting the central nervous system caused by alterations in the conformation of the cellular prion protein.
|
20513552 |
2010 |
Prion Diseases
|
0.500 |
GeneticVariation
|
group |
BEFREE |
Prion diseases are associated with a conformational switch in the prion protein (PrP) from its normal cellular form (denoted PrP(C)) to a disease-associated "scrapie" form (PrP(Sc)).
|
20718410 |
2010 |
Prion Diseases
|
0.500 |
GeneticVariation
|
group |
BEFREE |
Prion diseases are fatal neurodegenerative disorders that involve the conversion of the normal cellular form of the prion protein (PrP(C)) to a misfolded pathogenic form (PrP(Sc)).
|
20949975 |
2010 |
Prion Diseases
|
0.500 |
Biomarker
|
group |
BEFREE |
Prion diseases are believed to propagate by the mechanism involving self-perpetuating conformational conversion of the normal form of the prion protein, PrP(C), to the misfolded, pathogenic state, PrP(Sc).
|
21058033 |
2011 |