Results 31 to 40 of about 1,598,142 (264)

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   +6 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

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

The cellular prion protein beyond prion diseases

Swiss Medical Weekly, 2020
The cellular prion protein (PrPC), a cell surface glycoprotein originally identified for its central role in prion diseases (also called transmissible spongiform encephalopathies), has recently been implicated in the pathogenesis of other neurodegenerative disorders, such as Alzheimer’s and Parkinson’s diseases, by acting as a toxicity-transducing ...
Manni, Giorgia, Lewis, Victoria, Senesi, Matteo, Spagnolli, Giovanni, Fallarino, Francesca, Collins, Steven, Mouillet-Richard, Sophie, Biasini, Emiliano   +7 more
openaire   +6 more sources

Prion and Prion-Like Protein Strains: Deciphering the Molecular Basis of Heterogeneity in Neurodegeneration

Viruses, 2019
Increasing evidence suggests that neurodegenerative disorders share a common pathogenic feature: the presence of deposits of misfolded proteins with altered physicochemical properties in the Central Nervous System.
Carlo Scialò, Elena De Cecco, Paolo Manganotti, Giuseppe Legname   +3 more
doaj   +1 more source

Saccharomyces cerevisiae in neuroscience: how unicellular organism helps to better understand prion protein?

Neural Regeneration Research, 2021
The baker’s yeast Saccharomyces (S.) cerevisiae is a single-celled eukaryotic model organism widely used in research on life sciences. Being a unicellular organism, S. cerevisiae has some evident limitations in application to neuroscience. However, yeast
Takao Ishikawa
doaj   +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

Prion protein and cancers [PDF]

Acta Biochimica et Biophysica Sinica, 2014
The normal cellular prion protein, PrP(C) is a highly conserved and widely expressed cell surface glycoprotein in all mammals. The expression of PrP is pivotal in the pathogenesis of prion diseases; however, the normal physiological functions of PrP(C) remain incompletely understood.
Xiaowen, Yang, Yan, Zhang, Lihua, Zhang, Tianlin, He, Jie, Zhang, Chaoyang, Li   +5 more
openaire   +2 more sources

Regulation of MicroRNAs-Mediated Autophagic Flux: A New Regulatory Avenue for Neurodegenerative Diseases With Focus on Prion Diseases

Frontiers in Aging Neuroscience, 2018
Prion diseases are fatal neurological disorders affecting various mammalian species including humans. Lack of proper diagnostic tools and non-availability of therapeutic remedies are hindering the control strategies for prion diseases. MicroRNAs (miRNAs)
Syed Zahid Ali Shah, Deming Zhao, Tariq Hussain, Naveed Sabir, Lifeng Yang   +4 more
doaj   +1 more source

Spreading of a prion domain from cell-to-cell by vesicular transport in Caenorhabditis elegans. [PDF]

PLoS Genetics, 2013
Prion proteins can adopt self-propagating alternative conformations that account for the infectious nature of transmissible spongiform encephalopathies (TSEs) and the epigenetic inheritance of certain traits in yeast.
Carmen I Nussbaum-Krammer, Kyung-Won Park, Liming Li, Ronald Melki, Richard I Morimoto   +4 more
doaj   +1 more source