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期刊名:Prion

缩写:PRION

ISSN:1933-6896

e-ISSN:1933-690X

IF/分区:1.7/Q4

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共收录本刊相关文章索引737
Clinical Trial Case Reports Meta-Analysis RCT Review Systematic Review
Classical Article Case Reports Clinical Study Clinical Trial Clinical Trial Protocol Comment Comparative Study Editorial Guideline Letter Meta-Analysis Multicenter Study Observational Study Randomized Controlled Trial Review Systematic Review
Isaac H Solomon,Emiliano Biasini,David A Harris Isaac H Solomon
Prion diseases comprise a group of rapidly progressive and invariably fatal neurodegenerative disorders for which there are no effective treatments. While conversion of the cellular prion protein (PrP(C)) to a β-sheet rich isoform (PrP(Sc)...
Giuseppe Legname Giuseppe Legname
The conversion to a disease-associated conformer (PrP(Sc)) of the cellular prion protein (PrP(C)) is the central event in prion diseases. Wild-type PrPC converts to PrP(Sc) in the sporadic forms of the disorders through an unknown mechanism...
Giuseppe Legname Giuseppe Legname
The conversion to a disease-associated conformer (PrP(Sc)) of the cellular prion protein (PrP(C)) is the central event in prion diseases. Wild-type PrPC converts to PrP(Sc) in the sporadic forms of the disorders through an unknown mechanism...
Ralph Andre,Sarah J Tabrizi Ralph Andre
Prion diseases comprise a family of fatal neurodegenerative disorders caused by the conformational re-arrangement of a normal host-encoded protein, PrP (C) , to an abnormal infectious isoform termed PrP (Sc) . Currently, the precise cellula...
Ralph Andre,Sarah J Tabrizi Ralph Andre
Prion diseases comprise a family of fatal neurodegenerative disorders caused by the conformational re-arrangement of a normal host-encoded protein, PrP (C) , to an abnormal infectious isoform termed PrP (Sc) . Currently, the precise cellula...
Shahar Sukenik,Daniel Harries Shahar Sukenik
It is widely recognized that amyloid formation sensitively responds to conditions set by myriad cellular solutes. These cosolutes include two important classes: macromolecular crowders and compatible osmolytes. We have recently found that a...
Shahar Sukenik,Daniel Harries Shahar Sukenik
It is widely recognized that amyloid formation sensitively responds to conditions set by myriad cellular solutes. These cosolutes include two important classes: macromolecular crowders and compatible osmolytes. We have recently found that a...
Frédéric Checler Frédéric Checler
Cellular prion (PrP(c)) undergoes a regulated α-secretase-like cleavage by the disintegrin ADAM17 similar to the one taking place on β-amyloid precursor protein (βAPP). Because these cleavages give rise to biologically active fragments, ...
Frédéric Checler Frédéric Checler
Cellular prion (PrP(c)) undergoes a regulated α-secretase-like cleavage by the disintegrin ADAM17 similar to the one taking place on β-amyloid precursor protein (βAPP). Because these cleavages give rise to biologically active fragments, ...
Martin L Daus,Michael Beekes Martin L Daus
Transmissible spongiform encephalopathies (prion diseases) in animals may be associated with a zoonotic risk potential for humans as shown by the occurrence of variant Creutzfeldt-Jakob disease in the wake of the bovine spongiform encephalo...