Results 41 to 50 of about 3,400,014 (272)

Characterization of the prion protein in relation to normal cellular function and in disease [PDF]

, 2012
Transmissible spongiform encephalopathies (TSEs), also known as prion diseases, are a group of rare and fatal neurodegenerative disorders that can affect both human and animals.
Wik, Lotta
core   +1 more source

Prion Protein Misfolding [PDF]

Current Molecular Medicine, 2009
The crucial event in the development of transmissible spongiform encephalopathies (TSEs) is the conformational change of a host-encoded membrane protein - the cellular PrP(C) - into a disease associated, fibril-forming isoform PrP(Sc). This conformational transition from the alpha-helix-rich cellular form into the mainly beta-sheet containing ...
Kupfer, L, Hinrichs, W, Groschup, M.H
openaire   +2 more sources

Enhanced phosphorylation of PERK in primary cultured neurons as an autonomous neuronal response to prion infection.

PLoS ONE, 2020
Conversion of cellular prion protein (PrPC) into the pathogenic isoform of prion protein (PrPSc) in neurons is one of the key pathophysiological events in prion diseases.
Misaki Tanaka, Takeshi Yamasaki, Rie Hasebe, Akio Suzuki, Motohiro Horiuchi   +4 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

Use of bovine recombinant prion protein and real-time quaking-induced conversion to detect cattle transmissible mink encephalopathy prions and discriminate classical and atypical L- and H-Type bovine spongiform encephalopathy. [PDF]

PLoS ONE, 2017
Prions are amyloid-forming proteins that cause transmissible spongiform encephalopathies through a process involving conversion from the normal cellular prion protein to the pathogenic misfolded conformation (PrPSc).
Soyoun Hwang, Justin J Greenlee, Eric M Nicholson   +2 more
doaj   +1 more source

Distribution of Misfolded Prion Protein Seeding Activity Alone Does Not Predict Regions of Neurodegeneration.

PLoS Biology, 2016
Protein misfolding is common across many neurodegenerative diseases, with misfolded proteins acting as seeds for "prion-like" conversion of normally folded protein to abnormal conformations.
James Alibhai, Richard A Blanco, Marcelo A Barria, Pedro Piccardo, Byron Caughey, V Hugh Perry, Tom C Freeman, Jean C Manson   +7 more
doaj   +1 more source

A novel protective prion protein variant that colocalizes with kuru exposure. [PDF]

, 2009
BACKGROUND: Kuru is a devastating epidemic prion disease that affected a highly restricted geographic area of the Papua New Guinea highlands; at its peak, it predominantly affected adult women and children of both sexes.
Whittaker, John, Mein, C., Shah, Paresh, Campbell, T., Whitfield, Jerome, Mein, Charles A, Whittaker, J., Alpers, Michael Philip, Hummerich, H., Collinge, J., Hummerich, Holger, Collinge, John, Uphill, J., Poulter, Mark, Beck, Jon, Al-Dujaily, Huda, Mead, S., Al-Dujaily, H., Alpers, Michael P, Beck, J., Verzilli, C., Mead, Simon, Verzilli, Claudio, Shah, P., Uphill, James, Poulter, M., Campbell, Tracy   +26 more
core   +1 more source

Metabolism of minor isoforms of prion proteins: Cytosolic prion protein and transmembrane prion protein.

Neural regeneration research, 2013
Transmissible spongiform encephalopathy or prion disease is triggered by the conversion from cellular prion protein to pathogenic prion protein. Growing evidence has concentrated on prion protein configuration changes and their correlation with prion disease transmissibility and pathogenicity.
Song, Zhiqi, Zhao, Deming, Yang, Lifeng
openaire   +2 more sources

Effects of cellular prion protein on rapid eye movement sleep deprivation-induced spatial memory impairment

Journal of Integrative Neuroscience, 2019
The effects of cellular prion protein on rapid eye movement sleep deprivation-induced spatial memory impairment were investigated, and the related mechanisms explored.
Li Hu, Peng Li, Zhendong You, Zhaohuan Zhang, Hongyang Jin, Liuqing Huang   +5 more
doaj   +1 more source

Prion pathogenesis is unaltered in the absence of SIRPα-mediated "don't-eat-me" signaling. [PDF]

PLoS ONE, 2017
Prion diseases are neurodegenerative conditions caused by misfolding of the prion protein, leading to conspicuous neuronal loss and intense microgliosis.
Mario Nuvolone, Marta Paolucci, Silvia Sorce, Veronika Kana, Rita Moos, Takashi Matozaki, Adriano Aguzzi   +6 more
doaj   +1 more source