Results 31 to 40 of about 73,750 (253)

A New Cell Model for Investigating Prion Strain Selection and Adaptation

Viruses, 2019
Prion diseases are fatal neurodegenerative diseases that affect humans and animals. Prion strains, conformational variants of misfolded prion proteins, are associated with distinct clinical and pathological phenotypes.
Alexandra Philiastides, Juan Manuel Ribes, Daniel Chun-Mun Yip, Christian Schmidt, Iryna Benilova, Peter-Christian Klöhn   +5 more
doaj   +1 more source

Combination of structure-based virtual screening, molecular docking and molecular dynamics approaches for the discovery of anti-prion fibril flavonoids

Frontiers in Molecular Biosciences, 2023
Prion diseases are a group of rare neurodegenerative diseases caused by the structural conversion of cellular prion into Scrapie prion resulting aggregated fibrils. Therapy of prion diseases has been developed for several decades, especially drug designs
Cheng-Ping Jheng, Cheng-I Lee, Cheng-I Lee, Cheng-I Lee   +3 more
doaj   +1 more source

The most problematic symptoms of prion disease - an analysis of carer experiences [PDF]

, 2019
Objectives: Prion diseases are rare dementias that most commonly occur sporadically, but can be inherited or acquired, and for which there is no cure.
Collinge, John, Ford, Liz, Gorham, Michele, Mead, Simon, Robinson, Kathy, Rudge, Peter   +5 more
core   +2 more sources

A cationic tetrapyrrole inhibits toxic activities of the cellular prion protein [PDF]

, 2016
Prion diseases are rare neurodegenerative conditions associated with the conformational conversion of the cellular prion protein (PrPC) into PrPSc, a self-replicating isoform (prion) that accumulates in the central nervous system of affected individuals.
Biasini, Emiliano, Borsello, Tiziana, Castilla, Joaqu\uedn, Cerovic, Milica, Cimini, Sara, Elezgarai, Saioa R., Gobbi, Marco, Massignan, Tania, Moreno, Jorge, Negro, Alessandro, Nonno, Romolo, Restelli, Elena, Riccardi, Geraldina, Sangiovanni, Valeria, Stincardini, Claudia, Stravalaci, Matteo, Vanni, Ilaria   +16 more
core   +2 more sources

Genome-wide association study of behavioural and psychiatric features in human prion disease. [PDF]

, 2015
Prion diseases are rare neurodegenerative conditions causing highly variable clinical syndromes, which often include prominent neuropsychiatric symptoms.
Carswell, C, Collinge, J, Lowe, J, Lukic, A, MacKay, A, Mead, S, Porter, MC, Rudge, P, Thompson, AG, Uphill, J   +9 more
core   +1 more source

Gerstmann-Sträussler-Scheinker disease revisited: accumulation of covalently-linked multimers of internal prion protein fragments [PDF]

, 2019
Despite their phenotypic heterogeneity, most human prion diseases belong to two broadly defined groups: Creutzfeldt-Jakob disease (CJD) and Gerstmann-Sträussler-Scheinker disease (GSS).
Cali, Ignazio, Cracco, Laura, Gambetti, Pierluigi, Ghetti, Bernardino, Lavrich, Jody, Nemani, Satish K., Notari, Silvio, Surewicz, Witold K., Xiao, Xiangzhu   +8 more
core   +1 more source

Amyloid prions in fungi [PDF]

, 2016
Prions are infectious protein polymers that have been found to cause fatal diseases in mammals. Prions have also been identified in fungi (yeast and filamentous fungi), where they behave as cytoplasmic non-Mendelian genetic elements.
Aguzzi, Aguzzi, Aigle, Alberti, Aron, Balguerie, Ball, Bardill, Baudin-Baillieu, Baxa, Baxa, Borchsenius, Brachmann, Bradley, Brown, Byers, Cai, Chakrabortee, Chen, Chernoff, Collinge, Coustou, Coustou-Linares, Cox, Daskalov, Daskalov, Daskalov, Daskalov, Derkatch, Derkatch, Derkatch, Diaz-Avalos, DiSalvo, Douglas, Eichner, Espinosa Angarica, Fan, Garcia, Glover, Glover, Gorkovskiy, Griswold, Habenstein, Halfmann, Halfmann, Harrison, Higurashi, Holmes, Huang, Jarosz, Jarosz, Jung, Kabir, Kajava, Kajava, Kelly, King, King, Koch, Kochneva-Pervukhova, Krishnan, Kryndushkin, Kumar, Kunz, Lancaster, Li, Lum, Malato, Masel, Masison, Masison, Mathur, McGlinchey, Mizuno, Nakayashiki, Nelson, Newnam, Ohhashi, Patel, Patino, Paushkin, Prusiner, Rajon, Ritter, Rizet, Roberts, Ross, Ross, Schlieker, Schlumpberger, Sen, Seuring, Shewmaker, Shorter, Sondheimer, Sondheimer, Speldewinde, Stein, Taneja, Tapia, Tessier, Tipton, Tompa, Toyama, True, True, Tsai, Tycko, Tyedmers, Uptain, Van Melckebeke, Verges, Wan, Wasmer, Watts, Westergard, Wickner, Wickner, Wickner, Wickner, Wickner, Wickner, Zhou   +122 more
core   +2 more sources

Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding [PDF]

, 2010
Transmissible spongiform encephalopathies, or prion diseases, are caused by misfolding and aggregation of the prion protein PrP. These diseases can be hereditary in humans and four of the many disease-associated missense mutants of PrP are in the ...
Daggett, Valerie, van der Kamp, Marc W
core   +2 more sources

Syntaxin-6 delays prion protein fibril formation and prolongs the presence of toxic aggregation intermediates

eLife
Prions replicate via the autocatalytic conversion of cellular prion protein (PrPC) into fibrillar assemblies of misfolded PrP. While this process has been extensively studied in vivo and in vitro, non-physiological reaction conditions of fibril formation
Daljit Sangar, Elizabeth Hill, Kezia Jack, Mark Batchelor, Beenaben Mistry, Juan M Ribes, Graham S Jackson, Simon Mead, Jan Bieschke   +8 more
doaj   +1 more source

Molecular Dynamics Studies on the Buffalo Prion Protein [PDF]

, 2015
It was reported that buffalo is a low susceptibility species resisting to prion diseases, which are invariably fatal and highly infectious neurodegenerative diseases that affect a wide variety of species.
Chatterjee, Subhojyoti, Wang, Feng, Zhang, Jiapu   +2 more
core   +3 more sources