Results 231 to 240 of about 57,548 (261)

Cellular Prion Protein: Implications in Seizures and Epilepsy

Cellular and Molecular Neurobiology, 2002
1. Cellular prion (PrPc) is a plasma membrane protein involved with copper uptake, protection against oxidative stress, cell adhesion, differentiation, signaling, and survival in the central nervous system. 2. Deletion of PrPc gene (Pmp) in mice enhances sensitivity to seizures in vivo and neuronal excitability in vitro which can be related to: (i ...
Roger, Walz, Rosa Maria R P S, Castro, Tonicarlo R, Velasco, Carlos G, Carlotti, Américo C, Sakamoto, Ricardo R, Brentani, Vilma R, Martins   +6 more
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Copper(II) Ion Binding to Cellular Prion Protein

Journal of Chemical Information and Modeling, 2008
Prion diseases are fatal neurodegenerative diseases thought to arise from the post-translational conversion of normal cellular prion protein to a scrapie isoform. Experimental data suggest a role for copper(II) ions in the process. An ab initio QM/MM approach and available experimental data were combined in order to identify and evaluate three ...
Jernej, Zidar, Elizabeta T, Pirc, Milan, Hodoscek, Peter, Bukovec   +3 more
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Prion search and cellular prion protein expression in stranded dolphins.

Journal of biological regulators and homeostatic agents, 2012
The recent description of a prion disease (PD) case in a free-ranging bottlenose dolphin (Tursiops truncatus) prompted us to carry out an extensive search for the disease-associated isoform (PrPSc) of the cellular prion protein (PrPC) in the brain and in a range of lymphoid tissues from 23 striped dolphins (Stenella coeruleoalba), 5 bottlenose dolphins
DI GUARDO, Giovanni, Cocumelli C, Meoli R, Barbaro K, Terracciano G, DI FRANCESCO, Cristina Esmeralda, Mazzariol S, Eleni C.   +7 more
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The cellular prion protein binds copper in vivo

Nature, 1997
The normal cellular form of prion protein (PrPC) is a precursor to the pathogenic protease-resistant forms (PrPSc) believed to cause scrapie, bovine spongiform encephalopathy (BSE) and Creutzfeldt-Jakob disease. Its amino terminus contains the octapeptide PHGGGWGQ, which is repeated four times and is among the best-preserved regions of mammalian PrPC ...
D R, Brown, K, Qin, J W, Herms, A, Madlung, J, Manson, R, Strome, P E, Fraser, T, Kruck, A, von Bohlen, W, Schulz-Schaeffer, A, Giese, D, Westaway, H, Kretzschmar   +12 more
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Cellular Prion Protein Signaling in Serotonergic Neuronal Cells

Annals of the New York Academy of Sciences, 2007
Abstract: The cellular prion protein PrPCis the normal counterpart of the scrapie prion protein PrPSc, the main component of the infectious agent of transmissible spongiform encephalopathies (TSEs). It is a ubiquitous cell‐surface glycoprotein, abundantly expressed in neurons, which constitute the targets of TSE pathogenesis.
Sophie, Mouillet-Richard, Benoît, Schneider, Elodie, Pradines, Mathéa, Pietri, Myriam, Ermonval, Jacques, Grassi, J Grayson, Richards, Vincent, Mutel, Jean-Marie, Launay, Odile, Kellermann   +9 more
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Analysis of Cellular Prion Protein Endoproteolytic Processing

2017
Like numerous proteins of various structural and functional classes, the glycosylphosphatidylinositol (GPI)-anchored cellular prion protein (PrPC) has been recognized to undergo endoproteolytic processing for decades, a phenomenon observed in various cultured cell lines, as well as human and several animal tissue extracts.
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Cellular prion protein binds laminin and mediates neuritogenesis

Molecular Brain Research, 2000
Laminin (LN) plays a major role in neuronal differentiation, migration and survival. Here, we show that the cellular prion protein (PrPc) is a saturable, specific, high-affinity receptor for LN. The PrPc-LN interaction is involved in the neuritogenesis induced by NGF plus LN in the PC-12 cell line and the binding site resides in a carboxy-terminal ...
Graner, E., Mercadante, A. F., Zanata, S. M., Forlenza, O. V., Cabral, ALB, Veiga, S. S., Juliano, M. A., Roesler, R., Walz, R., Minetti, A., Izquierdo, I, Martins, V. R., Brentani, R. R.   +12 more
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Biosynthesis and cellular processing of the prion protein

2001
Publisher Summary The chapter provides a detailed picture of the biosynthesis and cellular processing of PrPC and PrPSc. PrPC is synthesized and matures along the secretory pathway much like other membrane glycoproteins. One important feature is the addition of a GPI anchor that serves to attach the polypeptide chain to the lipid bilayer without the ...
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Targeting The Cellular Prion Protein To Treat Neurodegeneration

Future Medicinal Chemistry, 2012
Biasini, Emiliano, Harris, David A.
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Prion-like transmission of protein aggregates in neurodegenerative diseases

Nature Reviews Molecular Cell Biology, 2010
Patrik Brundin, Ronald Melki, Ron Kopito
exaly