Results 121 to 130 of about 82,850 (254)

Targeting of the prion protein to the cytosol: mechanisms and consequences

, 2010
Prion diseases are characterized by the conformational transition of the cellular prion protein (PrPC) into an aberrant protein conformer, designated scrapie-prion protein (PrPSc).
Miesbauer, M., Rambold, A., Tatzelt, J., Winkelhofer, K.   +3 more
core  

Prions and Prion Diseases [PDF]

Laboratory Medicine, 1999
Prion diseases (transmissible encephalopathies) are progressive neurodegenerative diseases of animals and humans caused by a unique agent, the prion. These diseases have recently been in the news because of the emergence of bovine spongiform encephalopathy (BSE; mad cow disease) and variant Creutzfeldt-Jakob disease (vCJD) in the United Kingdom.
openaire   +1 more source

Epilepsia partialis continua as the presenting manifestation of Creutzfeldt–Jakob disease: A video‐polygraphic clinical vignette

Epileptic Disorders, EarlyView.
Roberta Cutellè, Angelo Pascarella, Ada Santoro, Vittoria Cianci, Anna Mammì, Giovanbattista Gaspare Tripodi, Caterina Prestandrea, Sara Gasparini, Edoardo Ferlazzo   +8 more
wiley   +1 more source

Infection control in the brain and the eye

Acta Ophthalmologica, EarlyView.
Abstract The Central Nervous System (CNS), comprising the brain and the eye, is considered to have a ‘privileged’ mechanism for dealing with immunological challenge (immune privilege, IP). CNS IP has been revealed through experiments using foreign protein antigens and cell and tissue alloantigens (grafts), but evidence for a role for IP in modulating ...
John V. Forrester, Paul G. McMenamin, Samantha J. Dando   +2 more
wiley   +1 more source

Red blood cell membrane proteome as a reporter of disease severity, transfusion impact and genetic background in transfusion‐dependent β‐thalassaemia

British Journal of Haematology, EarlyView.
Summary Omics technologies have transformed research in haemoglobinopathies, yet the proteome of RBCs remains largely unexplored in transfusion‐dependent thalassaemia (TDT). In this proteomic analysis, Red blood cell (RBC) membranes from 48 adults with TDT were compared with healthy controls.
Konstantina Theocharaki, Sophia Delicou, Aikaterini Ntzoura‐Kani, Nikolaos Simantiris, Marianna Politou, Veroniki Komninaka, Martina Samiotaki, Jerome Zoidakis, Marianna H. Antonelou   +8 more
wiley   +1 more source

Transcriptional profile of Glaesserella parasuis in swine serosal and joint fluids

Frontiers in Veterinary Science
Glaesserella parasuis is the causative agent of Glässer's disease and contributes to significant post-weaning mortality in the swine industry. Glässer's disease is characterized by meningitis, polyserositis, and polyarthritis.
Daniel W. Nielsen, Kaitlyn M. Sarlo Davila, Susan L. Brockmeier, Samantha J. Hau   +3 more
doaj   +1 more source

Assignment of the Human and Mouse Prion Protein Genes to Homologous Chromosomes [PDF]

, 1986
Purified preparations of scrapie prions contain one major macromolecule, designated prion protein (PrP). Genes encoding PrP are found in normal animals and humans but not within the infectious particles.
Blatt, Cila, Cohn, Vivian H., DeArmond, Stephen J., Fournier, R. E. K., Heinzmann, Camilla, Klisak, Ivana, Lem, Janice, Lucero, Michael, Mohandas, T., Pruisner, Stanley B., Simon, Melvin, Sparkes, Robert S., Weiner, Leslie P., Westaway, David   +13 more
core  

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

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

Human prion diseases

Annals of Medicine, 2000
The term 'prion diseases' refers to a group of neurodegenerative disorders thought to be caused by prions, pathogenic agents with novel modes of replication and transmission. Prion diseases are characterized by long incubation periods ranging from months to years and are invariably fatal once clinical symptoms have appeared.
openaire   +2 more sources