Results 11 to 20 of about 57,548 (261)

Pharmacological Agents Targeting the Cellular Prion Protein [PDF]

Pathogens, 2018
Prion diseases are associated with the conversion of the cellular prion protein (PrPC), a glycoprotein expressed at the surface of a wide variety of cell types, into a misfolded conformer (the scrapie form of PrP, or PrPSc) that accumulates in brain ...
Maria Letizia Barreca, Nunzio Iraci, Silvia Biggi, Violetta Cecchetti, Emiliano Biasini   +4 more
doaj   +3 more sources

Cellular Prion Protein: From Physiology to Pathology [PDF]

Viruses, 2012
The human cellular prion protein (PrPC) is a glycosylphosphatidylinositol (GPI) anchored membrane glycoprotein with two N-glycosylation sites at residues 181 and 197. This protein migrates in several bands by Western blot analysis (WB).
Yutaka Kikuchi, José B. Oliveira-Martins, Yoshiko Sugita-Konishi, Sei-ichi Yusa   +3 more
doaj   +3 more sources

Endoproteolysis of cellular prion protein by plasmin hinders propagation of prions. [PDF]

Front Mol Neurosci, 2022
Many questions surround the underlying mechanism for the differential metabolic processing observed for the prion protein (PrP) in healthy and prion-infected mammals. Foremost, the physiological α-cleavage of PrP interrupts a region critical for both toxicity and conversion of cellular PrP (PrPC) into its misfolded pathogenic isoform (PrPSc) by ...
Mays CE, Trinh THT, Telling G, Kang HE, Ryou C.   +4 more
europepmc   +4 more sources

Prion protein scrapie and the normal cellular prion protein [PDF]

Prion, 2015
Prions are infectious proteins and over the past few decades, some prions have become renowned for their causative role in several neurodegenerative diseases in animals and humans. Since their discovery, the mechanisms and mode of transmission and molecular structure of prions have begun to be established. There is, however, still much to be elucidated
Atkinson, Caroline J, Zhang, Kai, Munn, Alan L, Wiegmans, Adrian, Wei, Ming Q   +4 more
openaire   +3 more sources

Cellular prion protein transduces neuroprotective signals [PDF]

The EMBO Journal, 2002
To test for a role for the cellular prion protein (PrP(c)) in cell death, we used a PrP(c)-binding peptide. Retinal explants from neonatal rats or mice were kept in vitro for 24 h, and anisomycin (ANI) was used to induce apoptosis. The peptide activated both cAMP/protein kinase A (PKA) and Erk pathways, and partially prevented cell death induced by ANI
Luciana B, Chiarini, Adriana R O, Freitas, Silvio M, Zanata, Ricardo R, Brentani, Vilma R, Martins, Rafael, Linden   +5 more
openaire   +2 more sources

α-Cleavage of cellular prion protein [PDF]

Prion, 2012
The cellular prion protein (PrP (C) ) is subjected to various processing under physiological and pathological conditions, of which the α-cleavage within the central hydrophobic domain not only disrupts a region critical for both PrP toxicity and PrP (C) to PrP (Sc) conversion but also produces the N1 fragment that is neuroprotective and the C1 ...
Liang, Jingjing, Kong, Qingzhong
openaire   +2 more sources

Cellular prion protein conformation and function [PDF]

Proceedings of the National Academy of Sciences, 2011
In the otherwise highly conserved NMR structures of cellular prion proteins (PrP C ) from different mammals, species variations in a surface epitope that includes a loop linking a β-strand, β2, with a helix, α2, are associated with NMR manifestations of a dynamic equilibrium between locally different conformations ...
Damberger, F F, Christen, B, Pérez, D R, Hornemann, S, Wüthrich, K   +4 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

Physiological Functions of the Cellular Prion Protein [PDF]

Frontiers in Molecular Biosciences, 2017
The prion protein, PrPC, is a small, cell-surface glycoprotein notable primarily for its critical role in pathogenesis of the neurodegenerative disorders known as prion diseases. A hallmark of prion diseases is the conversion of PrPC into an abnormally folded isoform, which provides a template for further pathogenic conversion of PrPC, allowing disease
Andrew R. Castle, Andrew Gill
openaire   +4 more sources

Cytosolic Prion Protein Toxicity Is Independent of Cellular Prion Protein Expression and Prion Propagation [PDF]

Journal of Virology, 2007
ABSTRACT Prion diseases are transmissible neurodegenerative diseases caused by a conformational isoform of the prion protein (PrP), a host-encoded cell surface sialoglycoprotein. Recent evidence suggests a cytosolic fraction of PrP (cyPrP) functions either as an initiating factor or toxic element of prion disease.
Eric M, Norstrom, Mark F, Ciaccio, Benjamin, Rassbach, Robert, Wollmann, James A, Mastrianni   +4 more
openaire   +2 more sources