Results 31 to 40 of about 4,254,953 (206)

Proteinase K-Resistant Material in ARR/VRQ Sheep Brain Affected with Classical Scrapie Is Composed Mainly of VRQ Prion Protein [PDF]

, 2011
Classical scrapie is a prion disease in sheep and goats. In sheep, susceptibility to disease is genetically influenced by single amino acid substitutions.
Bossers, A., A. Bossers, T. Sklaviadis, I. Lantier, F. Lantier, L. J. M. van Keulen, Van Keulen, L., S. McCutcheon, Berthon, P., Lantier, Isabelle, van Keulen, L.J.M., van Zijderveld, F.G., P. Berthon, Lantier, Frédéric, F., Zijderveld, F.G., van, Jacobs, J.G., Keulen, L., Van, Langeveld, J.P.M., Lantier, I., H. Rezaei, J. P. M. Langeveld, Rezaei, Human, Sklaviadis, T., Berthon, Patricia, J. G. Jacobs, F. G. van Zijderveld, Lantier, F., McCutcheon, S., Rezaei, H.   +28 more
core   +1 more source

Soluble Aβ aggregates can inhibit prion propagation [PDF]

Open Biology, 2017
Mammalian prions cause lethal neurodegenerative diseases such as Creutzfeldt–Jakob disease (CJD) and consist of multi-chain assemblies of misfolded cellular prion protein (PrPC).
Claire J. Sarell, Emma Quarterman, Daniel C.-M. Yip, Cassandra Terry, Andrew J. Nicoll, Jonathan D. F. Wadsworth, Mark A. Farrow, Dominic M. Walsh, John Collinge   +8 more
doaj   +1 more source

Prion protein in the cerebrospinal fluid of healthy and naturally scrapie-affected sheep [PDF]

, 2006
The aim of this study was to characterize the cerebrospinal fluid (CSF) prion protein (PrP) of healthy and naturally scrapie-affected sheep. The soluble form of CSF PrPC immunoblotted with an anti-octarepeat and an anti-C terminus mAb showed two isoforms
Vé Ronique Gayrard, Moudjou, Mohammed, Gayrard-Troy, Véronique, V., Pierre-Louis Toutain, Mohammed Moudjou, Chantal Imbs, Viguié, Catherine, Toutain, Pierre-Louis, Imbs, Chantal, Moudjou, Mohammed, M., Catherine Viguié, Nicole Picard-Hagen, Picard-Hagen, Nicole, Gayrard, Véronique   +13 more
core   +1 more source

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 ...
Valerie Daggett, Daggett, Valerie, van der Kamp, Marc W, Marc W. van der Kamp   +3 more
core   +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

Exploring the mechanisms involved in prion degradation and spreading from cell-to-cell in neuronal cell models [PDF]

, 2011
Transmissible spongiform encephalopathies (TSE), also known as prion diseases, are fatal neurodegenerative disorders present both in human and animals with different aetiology as they can occur genetically, spontaneously or by infection (Prusiner 1998 ...
Marzo, Ludovica
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

Molecular dynamics as an approach to study prion protein misfolding and the effect of pathogenic mutations [PDF]

, 2011
Computer simulation of protein dynamics offers unique high-resolution information that complements experiment. Using experimentally derived structures of the natively folded prion protein (PrP), physically realistic dynamics and conformational changes ...
Valerie Daggett, Daggett, Valerie, van der Kamp, Marc W, Marc W. van der Kamp   +3 more
core   +1 more source

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

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.
Jeremy C. Simpson (29225), Franke, Markus, Sibeal Waldron (277507), Appelhans Dietmar, Rogers Mark S., Dietmar Appelhans (277509), Resenberger, Ulrike K., Simpson Jeremy C., Simpson, Jeremy C., Jörg Tatzelt, Franke Markus, Resenberger Ulrike K., Rogers, Mark S., McCarthy James M., Mark S. Rogers (277510), James M McCarthy, Sibeal Waldron, Dietmar Appelhans, Appelhans, Dietmar, Mark S Rogers, Tatzelt Jörg, Tatzelt, Jörg, Ulrike K. Resenberger (277506), McCarthy, James M., Waldron, Sibeal, Markus Franke, Ulrike K Resenberger, Markus Franke (277505), Waldron Sibeal, Jeremy C Simpson, Jörg Tatzelt (277508), James M. McCarthy (277504)   +31 more
core   +2 more sources