Results 41 to 50 of about 57,548 (261)

Heat shock factor 1 regulates lifespan as distinct from disease onset in prion disease [PDF]

, 2008
Prion diseases are fatal, transmissible, neurodegenerative diseases caused by the misfolding of the prion protein (PrP). At present, the molecular pathways underlying prion-mediated neurotoxicity are largely unknown.
Aguzzi, Adriano, Borkowski, Andrew W., Heppner, Frank L., Hutter, Gregor, Jackson, Walter S., King, Oliver D., Lindquist, Susan, Raymond, Gregory J., Steele, Andrew D.   +8 more
core   +3 more sources

The Cellular Prion Protein Identifies Bipotential Cardiomyogenic Progenitors [PDF]

Circulation Research, 2010
Rationale : The paucity of specific surface markers for cardiomyocytes and their progenitors has impeded the development of embryonic or pluripotent stem cell–based transplantation therapy. Identification of relevant surface markers may also enhance our
Hidaka, K, Shirai, M, Lee, J-K, Wakayama, T, Kodama, I, Schneider, MD, Morisaki, T   +6 more
openaire   +4 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

Protease-resistant prions selectively decrease Shadoo protein. [PDF]

PLoS Pathogens, 2011
The central event in prion diseases is the conformational conversion of the cellular prion protein (PrP(C)) into PrP(Sc), a partially protease-resistant and infectious conformer. However, the mechanism by which PrP(Sc) causes neuronal dysfunction remains
Joel C Watts, Jan Stöhr, Sumita Bhardwaj, Holger Wille, Abby Oehler, Stephen J Dearmond, Kurt Giles, Stanley B Prusiner   +7 more
doaj   +1 more source

IN ABSENCE OF THE CELLULAR PRION PROTEIN, ALTERATIONS IN COPPER METABOLISM AND COPPER-DEPENDENT OXIDASE ACTIVITY AFFECT IRON DISTRIBUTION

Frontiers in Neuroscience, 2016
Essential elements as copper and iron modulate a wide range of physiological functions. Their metabolism is strictly regulated by cellular pathways, since dysregulation of metal homeostasis is responsible for many detrimental effects.
Lisa Gasperini, Elisa Meneghetti, Giuseppe Legname, Federico Benetti   +3 more
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

Identification of an intracellular site of prion conversion.

PLoS Pathogens, 2009
Prion diseases are fatal, neurodegenerative disorders in humans and animals and are characterized by the accumulation of an abnormally folded isoform of the cellular prion protein (PrP(C)), denoted PrP(Sc), which represents the major component of ...
Zrinka Marijanovic, Anna Caputo, Vincenza Campana, Chiara Zurzolo   +3 more
doaj   +1 more source

The Cellular Prion Protein: A Player in Immunological Quiescence [PDF]

Frontiers in Immunology, 2015
Despite intensive studies since the 1990s, the physiological role of the cellular prion protein (PrP(C)) remains elusive. Here, we present a novel concept suggesting that PrP(C) contributes to immunological quiescence in addition to cell protection.
Bakkebø, Maren, Mouillet-Richard, Sophie, Espenes, Arild, Goldmann, Wilfred, Tatzelt, Jörg, Tranulis, Michael   +5 more
openaire   +6 more sources

Anti-Prion Systems in Saccharomyces cerevisiae Turn an Avalanche of Prions into a Flurry

Viruses, 2022
Prions are infectious proteins, mostly having a self-propagating amyloid (filamentous protein polymer) structure consisting of an abnormal form of a normally soluble protein.
Moonil Son, Reed B. Wickner
doaj   +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