Results 31 to 40 of about 78,455 (315)

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

Prion Diseases [PDF]

Seminars in Neurology, 2012
Prion diseases are a group of diseases caused by abnormally conformed infectious proteins, called prions. They can be sporadic (Jakob-Creutzfeldt disease [JCD]), genetic (genetic JCD, Gerstmann-Sträussler-Scheinker, and familial fatal insomnia), or acquired (kuru, variant JCD, and iatrogenic JCD).
Takada, Leonel, Geschwind, Michael
openaire   +4 more sources

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

Genetic risk factors for Creutzfeldt-Jakob disease

Neurobiology of Disease, 2020
Prion diseases are a group of fatal neurodegenerative disorders of mammals that share a central role for prion protein (PrP, gene PRNP) in their pathogenesis.
Emma Jones, Simon Mead
doaj   +1 more source

Anti-prion drug mPPIg5 inhibits PrP(C) conversion to PrP(Sc). [PDF]

, 2013
Prion diseases, also known as transmissible spongiform encephalopathies, are a group of fatal neurodegenerative diseases that include scrapie in sheep, bovine spongiform encephalopathy (BSE) in cattle and Creutzfeldt-Jakob disease (CJD) in humans.
A Ertmer, A Janaszewska, A Taraboulos, AP Perez, AY Yam, B Caughey, B Caughey, B Caughey, B Klajnert, B Klajnert, B Klajnert, B Klajnert, B Klajnert, B Klajnert, DD Pless, Dietmar Appelhans, DR Borchelt, Ina Maja Vorberg, J Masel, J Solassol, James M. McCarthy, Jeremy C. Simpson, Jörg Tatzelt, K Doh-Ura, KA Nishina, KF Winklhofer, KF Winklhofer, M Fischer, M Miesbauer, Mark S. Rogers, Markus Franke, MP McKinley, N Nishida, NR Deleault, P Heegaard, PC Klohn, PJ Bosque, PMH Heegaard, R Klebe, RJ Kascsak, S Ghaemmaghami, S Gilch, S Supattapone, S Supattapone, SA Priola, SB Prusiner, SB Prusiner, Sibeal Waldron, Ulrike K. Resenberger, Y Lim   +49 more
core   +3 more sources

Cellular Prion Protein Mediates Toxic Signaling of Amyloid Beta [PDF]

, 2011
Prion diseases in humans and animals comprise a group of invariably fatal neurodegenerative diseases characterized by the formation of a pathogenic protein conformer designated PrPSc and infectious particles denoted prions.
Resenberger, Ulrike K., Tatzelt, Jörg, Winklhofer, Konstanze F.   +2 more
core   +1 more source

Genetic Factors Contributing to the Susceptibility of Development of Prion Diseases [PDF]

, 2017
This paper won an honorable mention writing flag award in the research category. Claire Culbertson, writing for Katherine Bruner’s BIO 325L class, “Lab Experience in Genetics”.Bruner, KatherineUndergraduate ...
Culbertson, Claire
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