Results 21 to 30 of about 56,657 (298)

Deposition pattern and subcellular distribution of disease-associated prion protein in cerebellar organotypic slice cultures infected with scrapie

Frontiers in Neuroscience, 2015
Organotypic cerebellar slices represent a suitable model for characterizing and manipulating prion replication in complex cell environments. Organotypic slices recapitulate prion pathology and are amenable to drug testing in the absence of a blood-brain ...
Hanna eWolf, Andre eHossinger, Andrea eFehlinger, Sven eBuettner, Valerie eSim, Debbie eMcKenzie, Ina Maja Vorberg, Ina Maja Vorberg   +7 more
doaj   +1 more source

Novel insertion/deletion polymorphisms and genetic features of the shadow of prion protein gene (SPRN) in dogs, a prion-resistant animal

Frontiers in Veterinary Science, 2022
Prion diseases are fatal infectious neurodegenerative disorders that are induced by misfolded prion protein (PrPSc). Previous studies have reported that the shadow of prion protein (Sho) encoded by the shadow of prion protein gene (SPRN) plays a critical
Yong-Chan Kim, Yong-Chan Kim, Hyeon-Ho Kim, Hyeon-Ho Kim, An-Dang Kim, Byung-Hoon Jeong, Byung-Hoon Jeong   +6 more
doaj   +1 more source

ALK1 controls hepatic vessel formation, angiodiversity, and angiocrine functions in hereditary hemorrhagic telangiectasia of the liver

Hepatology, EarlyView., 2022
Hepatic endothelial Alk1 signaling protects from development of vascular malformations while maintaining organ‐specific endothelial differentiation and angiocrine portmanteau of the names Wingless and Int‐1 signaling. Abstract Background and Aims In hereditary hemorrhagic telangiectasia (HHT), severe liver vascular malformations are associated with ...
Christian David Schmid, Victor Olsavszky, Manuel Reinhart, Vanessa Weyer, Felix A. Trogisch, Carsten Sticht, Manuel Winkler, Sina W. Kürschner, Johannes Hoffmann, Roxana Ola, Theresa Staniczek, Joerg Heineke, Beate K. Straub, Jens Mittler, Kai Schledzewski, Peter ten Dijke, Karsten Richter, Steven Dooley, Cyrill Géraud, Sergij Goerdt, Philipp‐Sebastian Koch   +20 more
wiley   +1 more source

Effects of post-translational modifications on prion protein aggregation and the propagation of scrapie-like characteristics in vitro [PDF]

, 2007
Prion diseases, or transmissible spongiform encephalopathies (TSEs) are typically characterised by CNS accumulation of PrPSc, an aberrant conformer of a normal cellular protein PrPC.
Oxley, David, Meersman, Filip, Webster, Judith, Kazlauskaite, Jurate, Pinheiro, Teresa J. T., Young, Duncan S., Dear, Denise V., Lowe, Christopher R., Gill, Andrew C., Bronstein, Igor   +9 more
core   +1 more source

Morphine Withdrawal Modifies Prion Protein Expression in Rat Hippocampus. [PDF]

PLoS ONE, 2017
The hippocampus is a vulnerable brain structure susceptible to damage during aging and chronic stress. Repeated exposure to opioids may alter the brain so that it functions normally when the drugs are present, thus, a prolonged withdrawal might lead to ...
Vincenzo Mattei, Stefano Martellucci, Francesca Santilli, Valeria Manganelli, Tina Garofalo, Niccolò Candelise, Alessandra Caruso, Maurizio Sorice, Sergio Scaccianoce, Roberta Misasi   +9 more
doaj   +1 more source

Prion Protein in Milk

PLoS ONE, 2006
Prions are known to cause transmissible spongiform encephalopathies (TSE) after accumulation in the central nervous system. There is increasing evidence that prions are also present in body fluids and that prion infection by blood transmission is possible.
Franscini, Nicola, Gedaily, Ahmed El, Matthey, Ulrich, Franitza, Susanne, Sy, Man-Sun, Bürkle, Alexander, Groschup, Martin, Braun, Ueli, Zahn, Ralph   +8 more
openaire   +5 more sources

Prion protein glycosylation [PDF]

Journal of Neurochemistry, 2005
AbstractThe transmissible spongiform encephalopathies (TSE), or prion diseases are a group of transmissible neurodegenerative disorders of humans and animals. Although the infectious agent (the ‘prion’) has not yet been formally defined at the molecular level, much evidence exists to suggest that the major or sole component is an abnormal isoform of ...
Lawson, Victoria A, Collins, Steven J, Masters, Colin L, Hill, Andrew F   +3 more
openaire   +3 more sources

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

Sequence features governing aggregation or degradation of prion-like proteins. [PDF]

PLoS Genetics, 2018
Enhanced protein aggregation and/or impaired clearance of aggregates can lead to neurodegenerative disorders such as Alzheimer's Disease, Huntington's Disease, and prion diseases.
Sean M Cascarina, Kacy R Paul, Satoshi Machihara, Eric D Ross   +3 more
doaj   +1 more source

Insight into the conserved structural dynamics of the C-terminus of mammal PrPC identifies structural core and possible structural role of pharmacological chaperones

Prion, 2023
Misfolding of the prion protein is central to prion disease aetiology. Although understanding the dynamics of the native fold helps to decipher the conformational conversion mechanism, a complete depiction of distal but coupled prion protein sites common
Patricia Soto, Garrett M. Gloeb, Kaitlin A. Tsuchida, Austin A. Charles, Noah M. Greenwood, Heidi Hendrickson   +5 more
doaj   +1 more source