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A Function for the Prion Protein?

2003
Protein function is often observed directly following protein isolation, or is deduced by loss of function following gene knockout or by analogy with proteins of known function and similar amino acid sequence. None of these is true in the case of prion proteins because aside from the association with the pathogenesis of the spongiform encaphalopathies,
D R, Brown, I M, Jones
openaire   +2 more sources

Photo-induced crosslinking of prion protein oligomers and prions

Amyloid, 2006
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). This misfolded isoform (PrPSc) tends to form insoluble amyloid-like aggregates, impeding classical structural analysis by X-ray crystallography or NMR.
Niklas, Piening   +5 more
openaire   +2 more sources

Prion Diseases and the Prion Protein

2004
Pierre Aucouturier   +3 more
openaire   +1 more source

De novo generation of prion strains

Nature Reviews Microbiology, 2011
David Colby, Stanley Prusiner
exaly  

Prion-like proteins and their computational identification in proteomes

Expert Review of Proteomics, 2017
Susanna Navarro   +2 more
exaly  

Characterization of Prion Proteins

2003
Wenquan, Zou   +3 more
openaire   +2 more sources

Overexpression of Q-rich prion-like proteins suppresses polyQ cytotoxicity and alters the polyQ interactome

Proceedings of the National Academy of Sciences of the United States of America, 2014
Roman Körner   +2 more
exaly  

Interactions of prion proteins with soil

Soil Biology and Biochemistry, 2006
Alessandro Bertoli
exaly  

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