Results 111 to 120 of about 57,548 (261)

Tau‐targeting active immunotherapy slows progression and reduces pathology in mouse models of tauopathy

Brain Pathology, EarlyView.
The efficacy of the novel anti‐tau active immunotherapy, p5555kb, was tested using two mouse models of tau pathology. p5555kb inoculation increased the survival rate and reduced tau pathology in tau‐overexpressing P301L mice and decreased tau seeding in the brains of C57BL/6 mice injected with human‐purified Alzheimer's disease tau.
Christopher M. Brown, Jeanne K. Brooks, Louise Kelly, Madeline M. Vroom, Matthew Longo, Jean‐Cosme Dodart, Roxana Carare, Justin D. Boyd   +7 more
wiley   +1 more source

Cellular distribution of the prion protein in palatine tonsils of mule deer (Odocoileus hemionus) and Rocky Mountain elk (Cervus elaphus nelsoni) [PDF]

, 2019
Chronic wasting disease (CWD) is a transmissible spongiform encephalopathy (TSE) that affects members of the Cervidae family, including deer (Odocoileus spp.), elk (Cervus Canadensis spp.), and moose (Alces alces spp.).
Belden, E. Lee, Hille, Matthew M., Jewell, Jean E.   +2 more
core   +1 more source

Stochastic Modelling Approach to the Incubation Time of Prionic Diseases

, 2003
Transmissible spongiform encephalopathies like the bovine spongiform encephalopathy (BSE) and the Creutzfeldt-Jakob disease (CJD) in humans are neurodegenerative diseases for which prions are the attributed pathogenic agents.
A. S. Ferreira, A. L. Horwich, B. J. West, D. J. Stekel, G. C. Telling, J. C. Cressoni, J. Collinge, J. D. Murray, J. S. Griffith, M. A. A. da Silva, M. Eigen, R. G. Will, R. M. Anderson, S. B. Prusiner, S. B. Prusiner, S. B. Prusiner   +15 more
core   +1 more source

Prion protein in the cerebrospinal fluid of healthy and naturally scrapie-affected sheep [PDF]

, 2006
The aim of this study was to characterize the cerebrospinal fluid (CSF) prion protein (PrP) of healthy and naturally scrapie-affected sheep. The soluble form of CSF PrPC immunoblotted with an anti-octarepeat and an anti-C terminus mAb showed two isoforms
Andréoletti, Banks, Baron, Baylis, Bieschke, Brown, Buschmann, Catherine Viguié, Chantal Imbs, Ecroyd, Elsen, Green, Hunter, Le Dur, Mohammed Moudjou, Morel, Moudjou, Nicole Picard-Hagen, Pierre-Louis Toutain, Rezaei, Safar, Toutain, Véronique Gayrard, Weller, Wong   +24 more
core   +3 more sources

Rapid generation of prion disease models using AAV‐delivered PrP variants in knockout mice

Brain Pathology, EarlyView.
We developed a rapid AAV‐based system to generate prion disease models in weeks rather than months. Following systemic AAV9P31 delivery of modified PrP to knockout mice, we achieved brain‐wide expression and successful propagation of both classical (RML) and atypical (GSS‐A117V) prion strains.
Maitena San‐Juan‐Ansoleaga, Eva Fernández‐Muñoz, Jorge M. Charco, Enric Vidal, Diego Herrero‐Martínez, Josu Galarza‐Ahumada, Cristina Sampedro‐Torres‐Quevedo, Samanta Giler, Mariví Geijo, Gloria González‐Aseguinolaza, Hasier Eraña, Joaquín Castilla   +11 more
wiley   +1 more source

Therapeutic effect of curcumin derivative GT863 on prion-infected mice

Scientific Reports
In prion diseases, the cellular prion protein (PrPC) forms an abnormal, infectious, and disease-causing form known as PrPSc. Inhibition of prion propagation is a key approach for the treatment of these diseases.
Kenta Teruya, Ayumi Oguma, Michiaki Okuda, Sara Iwabuchi, Hiroyuki Konno, Hiroyuki Arai, Yukitsuka Kudo, Hachiro Sugimoto, Katsumi Doh-ura   +8 more
doaj   +1 more source

Prions amplify through degradation of the VPS10P sorting receptor sortilin.

PLoS Pathogens, 2017
Prion diseases are a group of fatal neurodegenerative disorders caused by prions, which consist mainly of the abnormally folded isoform of prion protein, PrPSc.
Keiji Uchiyama, Mitsuru Tomita, Masashi Yano, Junji Chida, Hideyuki Hara, Nandita Rani Das, Anders Nykjaer, Suehiro Sakaguchi   +7 more
doaj   +1 more source

Breaking the Cycle, Cholesterol Cycling, and Synapse Damage in Response to Amyloid-ß [PDF]

, 2017
Soluble amyloid-β (Aβ) oligomers, a key driver of pathogenesis in Alzheimer disease, bind to cellular prion proteins (PrPC) expressed on synaptosomes resulting in increased cholesterol concentrations, movement of cytoplasmic phospholipase A2 (cPLA2) to ...
Bate, C
core   +3 more sources

Physiology of Cellular Prion Proteins in Reproduction

Development & Reproduction
Cellular prion protein (PrPC) encoded at Prnp gene is well-known to form a misfolded isoform, termed scrapie PrP (PrPSC) that cause transmissible degenerative diseases in central nervous system. The physiological role of PrPC has been proposed by many studies, showing that PrPC interacts with various intracellular, membrane, and extracellular molecules
Željko M. Svedružić, Chongsuk Ryou, Donchan Choi, Sung-Ho Lee, Yong-Pil Cheon   +4 more
openaire   +2 more sources

The L108I polymorphism in mouse prion protein drives spontaneous disease and enhances transmission of atypical and classical prion strains

Brain Pathology, EarlyView.
A single amino acid change (L108I) combined with PrP overexpression drives spontaneous atypical prion formation in mice, enabling also efficient propagation of diverse prion strains. This model allows studying how spontaneous prion diseases arise and provides powerful tools for investigating strain emergence, transmission barriers, and mechanisms ...
Hasier Eraña, Enric Vidal, Natalia Fernández‐Borges, Jorge M. Charco, Carlos M. Díaz‐Domínguez, Cristina Sampedro‐Torres‐Quevedo, Josu Galarza‐Ahumada, Eva Fernández‐Muñoz, Maitena San‐Juan‐Ansoleaga, Miguel Ángel Pérez‐Castro, Nuno Gonçalves‐Anjo, Patricia Piñeiro, Samanta Giler, Nora González‐Martín, Nuria L. Lorenzo, Africa Manero‐Azua, Guiomar Perez de Nanclares, Mariví Geijo, Manuel A. Sánchez‐Martín, Jesús R. Requena, Joaquín Castilla   +20 more
wiley   +1 more source