Results 81 to 90 of about 75,780 (211)

Efficient transmission and characterization of creutzfeldt-jakob disease strains in bank voles. [PDF]

, 2006
Transmission of prions between species is limited by the "species barrier," which hampers a full characterization of human prion strains in the mouse model.
Bari Michele A. Di, Boyle, Aileen, Lipp Hans-Peter, Gabriele Vaccari, Maurizio Pocchiari, Cardone Franco, Sbriccoli Marco, Claudia Cartoni, Sbriccoli, Marco, Boyle Aileen, Dell'Omo, Giacomo, Nonno, Romolo, Di Bari, Michele A, Nonno Romolo, Franco Cardone, Galeno, Roberta, Marco Sbriccoli, Paola Fazzi, Vaccari Gabriele, Cartoni, Claudia, Cardone, Franco, Galeno Roberta, Loredana Ingrosso, Roberta Galeno, Fazzi, Paola, Lipp, Hans-Peter, Fazzi Paola, Michele A Di Bari, Ingrosso Loredana, Hans-Peter Lipp, Ingrosso, Loredana, Pocchiari, Maurizio, Umberto Agrimi, Pocchiari Maurizio, Vaccari, Gabriele, Agrimi, Umberto, Giacomo Dell'Omo, Moira Bruce, Aileen Boyle, Dell'Omo Giacomo, Agrimi Umberto, Bruce Moira, Bruce, Moira, Romolo Nonno, Cartoni Claudia   +44 more
core   +1 more source

Seeding and transgenic overexpression of alpha‐synuclein triggers dendritic spine pathology in the neocortex

EMBO Molecular Medicine, 2017
Although misfolded and aggregated α‐synuclein (α‐syn) is recognized in the disease progression of synucleinopathies, its role in the impairment of cortical circuitries and synaptic plasticity remains incompletely understood.
Sonja Blumenstock, Eva F Rodrigues, Finn Peters, Lidia Blazquez‐Llorca, Felix Schmidt, Armin Giese, Jochen Herms   +6 more
doaj   +1 more source

Genetic variability of the prion protein gene (PRNP) in wild ruminants from Italy and Scotland [PDF]

, 2009
The genetics of the prion protein gene (PRNP) play a crucial role in determining the relative susceptibility to transmissible spongiform encephalopathies (TSEs) in several mammalian species.
Acutis, Pier Luigi, Pier Luigi Acutis, Ezio Ferroglio, Simone Peletto, Hugh W. Reid, Perucchini, Matteo, Serena Robetto, Acin, Cristina, Bozzetta, Elena, Reid, Hugh W., Dalgleish, Mark P., Orusa, Riccardo, Elena Bozzetta, Ferroglio, Ezio, Sacchi, Paola, Paula Stewart, Daniela Meloni, Wilfred Goldmann, Meloni, Daniela, Gennero, Silvia, Riccardo Orusa, Roberto Rasero, Rasero, Roberto, Cristina Acín, Matteo Perucchini, Mark P. Dalgleish, Goldmann, Wilfred, Stewart, Paula, Maria Caramelli, Silvia Gennero, Caramelli, Maria, Robetto, Serena, Peletto, Simone, Paola Sacchi   +33 more
core   +1 more source

Yeast Prions and Their Prion-Forming Domain [PDF]

Cell, 2000
We have learned much about prion biology through the study of yeast prions and their associated PrDs, but caution must be exercised in extrapolating these findings directly to mammalian prion behavior. It must not be forgotten that mammalian PrPSc is an infectious agent that can spread from cell to cell while there is no evidence of cell-to-cell ...
openaire   +2 more sources

Prion replication in organotypic brain slice cultures is distinct from in vivo inoculation and is species dependent

Acta Neuropathologica Communications
Cultured brain slices rapidly replicate murine prions, exhibit prion pathology, and are amenable towards drug discovery, but have not been infected with human prions.
Jessy A. Slota, Lise Lamoureux, Jennifer Myskiw, Kathy L. Frost, Sarah J. Medina, Dominic M. S. Kielich, Melanie Leonhardt, Gunjan Thapar, Ben A. Bailey-Elkin, Stephanie A. Booth   +9 more
doaj   +1 more source

A Neuronal Cell Line Model for Studying Camel Prions

Pathogens
Prion diseases are fatal neurodegenerative disorders that affect humans and animals, caused by the conformational conversion of the normal cellular prion protein (PrPC) into its misfolded, infectious isoform PrPSc.
Basant Abdulrahman, Shabboo Rahimi Aqdam, Matteo Mosca, Hanaa Ahmed-Hassan, Melissa Razcon-Echeagaray, Lia Popa, Sabine Gilch, Baaissa Babelhadj, Gabriele Vaccari, Hermann M. Schätzl   +9 more
doaj   +1 more source

Glycopeptide analysis of different prion strains [PDF]

, 2020
Prion diseases or transmissible spongiform encephalopathies (TSEs) are a group of infectious neurodegenerative diseases. They are caused by a conformational change of the cellular prion protein (PrPC) to the misfolded form (PrPSc).
Nakic, Natali
core  

The 37kDa/67kDa laminin receptor as a therapeutic target in prion diseases: potency of antisense LRP RNA, siRNAs specific for LRP mRNA and a LRP decoy mutant [PDF]

, 2006
Prion diseases are a group of rare, fatal neurodegenerative diseases, also known as transmissible spongiform encephalopathies (TSEs), that affect both animals and humans and include bovine spongiform encephalopathy (BSE) in cattle, scrapie in sheep ...
Vana, Karen
core   +1 more source

A rapid dual staining procedure for the quantitative discrimination of prion amyloid from tissues reveals how interactions between amyloid and lipids in tissue homogenates may hinder the detection of prions

, 2009
Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative diseases with no cure to this day, and are often associated with the accumulation of amyloid plaques in the brain and other tissues in affected individuals. The emergence of new
Keevil, C.William, Collin, R., Hervé, R., Secker, Thomas, Pinchin, H.E.   +4 more
core   +1 more source

The presence of valine at residue 129 in human prion protein accelerates amyloid formation [PDF]

, 2005
The polymorphism at residue 129 of the human PRNP gene modulates disease susceptibility and the clinicopathological phenotypes in human transmissible spongiform encephalopathies.
Tahiri-Alaoui, Abdessamad, Gill, A, Shaw, Michael, Shaw, M, Baskakov, I, Breydo, L, James, W, Tahiri-Alaoui, A, Disterer, Petra, Gill, Andrew, Baskakov, Ilia, Breydo, Leonid, Disterer, P, James, William   +13 more
core   +1 more source