Results 91 to 100 of about 5,869 (184)

Gene-Based Antibody Strategies for Prion Diseases

International Journal of Cell Biology, 2013
Prion diseases or transmissible spongiform encephalopathies (TSE) are a group of neurodegenerative and infectious disorders characterized by the conversion of a normal cellular protein PrPC into a pathological abnormally folded form, termed PrPSc.
Alessio Cardinale, Silvia Biocca
doaj   +1 more source

A Protein Misfolding Shaking Amplification-based method for the spontaneous generation of hundreds of bona fide prions

Nature Communications
Prion diseases are a group of rapidly progressing neurodegenerative disorders caused by the misfolding of the endogenous prion protein (PrPC) into a pathogenic form (PrPSc).
Hasier Eraña, Cristina Sampedro-Torres-Quevedo, Jorge M. Charco, Carlos M. Díaz-Domínguez, Francesca Peccati, Maitena San-Juan-Ansoleaga, Enric Vidal, Nuno Gonçalves-Anjo, Miguel A. Pérez-Castro, Ezequiel González-Miranda, Patricia Piñeiro, Leire Fernández-Veiga, Josu Galarza-Ahumada, Eva Fernández-Muñoz, Guiomar Perez de Nanclares, Glenn Telling, Mariví Geijo, Gonzalo Jiménez-Osés, Joaquín Castilla   +18 more
doaj   +1 more source

Enfermedad de creutzfeldt-jakob en el Perú: reporte de once casos

Revista Peruana de Medicina Experimental y Salud Pública
La enfermedad de Creutzfeldt-Jakob (ECJ) es una enfermedad neurológica fatal producida por la isoforma patológica de la proteína priónica humana.
Luis Torres-Ramírez, Jorge Ramírez-Quiñones, Carlos Cosentino-Esquerre, Miriam Vélez-Rojas, Martha Flores-Mendoza, Diana Rivas-Franchini, Rafael Suarez-Reyes, Yesenia Núñez-Coronado   +7 more
doaj   +2 more sources

An engineered PrPsc-like molecule from the chimera of mammalian prion protein and yeast Ure2p prion-inducing domain.

Acta biochimica et biophysica Sinica, 2004
Production of the pathogenic prion isoform PrPsc-like molecules is thought to be useful for understanding the mysterious mechanism of conformational conversion process of prion diseases and proving the "protein-only" hypothesis. In this report, an engineered PrPsc-like conformation was produced from a chimera of mammalian bovine prion protein (bPrP ...
Shao-Man, Yin, Man-Sun, Sy, Tien, Po
openaire   +1 more source

Correction: Disulfide-crosslink scanning reveals prion–induced conformational changes and prion strain–specific structures of the pathological prion protein PrPSc. [PDF]

Journal of Biological Chemistry, 2018
Yuzuru, Taguchi, Li, Lu, Cristobal, Marrero-Winkens, Hiroki, Otaki, Noriyuki, Nishida, Hermann M, Schatzl   +5 more
openaire   +2 more sources

CD and NMR studies of prion protein (PrP) helix 1. Novel implications for its role in the PrPC-->PrPSc conversion process.

The Journal of biological chemistry, 2004
The conversion of prion helix 1 from an alpha-helical into an extended conformation is generally assumed to be an essential step in the conversion of the cellular isoform PrPC of the prion protein to the pathogenic isoform PrPSc. Peptides encompassing helix 1 and flanking sequences were analyzed by nuclear magnetic resonance and circular dichroism. Our
Jan, Ziegler, Heinrich, Sticht, Ute C, Marx, Wolfgang, Müller, Paul, Rösch, Stephan, Schwarzinger   +5 more
openaire   +1 more source

Mutant knock-in mice display enhanced susceptibility to pure prion protein fibrils. [PDF]

J Gen Virol
Walsh DJ, Standke H, Kraus A, Watts JC, Supattapone S.   +4 more
europepmc   +1 more source

Consequences of prion strain mixtures: Indifference, competition, or collusion. [PDF]

PLoS Pathog
Woerman AL, Bartz JC.
europepmc   +1 more source

Prion seeding activity in DNA extractions: implications for laboratory biosafety. [PDF]

Prion
Gresch SC, Morrill T, Ellis-Cramer M, Arifin M, Frank LE, Bartz JC, Schwabenlander MD, Wolf TM, Mitchell GB, Guan J, Larsen PA.   +10 more
europepmc   +1 more source

Membrane-anchored PrPSc is the trigger for prion synaptotoxicity. [PDF]

PLoS Pathog
Gatdula JRP, Mercer RCC, Alepuz Guillen JA, Vultaggio JS, Harris DA.   +4 more
europepmc   +1 more source