Results 71 to 80 of about 3,400,014 (272)

The presence of valine at residue 129 in human prion protein accelerates amyloid formation [PDF]

, 2005
The polymorphism at residue 129 of the human PRNP gene modulates disease susceptibility and the clinicopathological phenotypes in human transmissible spongiform encephalopathies.
Tahiri-Alaoui, Abdessamad, Gill, A, Shaw, Michael, Shaw, M, Baskakov, I, Breydo, L, James, W, Tahiri-Alaoui, A, Disterer, Petra, Gill, Andrew, Baskakov, Ilia, Breydo, Leonid, Disterer, P, James, William   +13 more
core   +1 more source

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

Preserving Proton Resolution Under Cryogenic Dynamic Nuclear Polarization for Biomolecular Solid‐State NMR

Angewandte Chemie, EarlyView.
High‐resolution proton detection is preserved under cryogenic dynamic nuclear polarization (DNP) by combining fast MAS, extensive deuteration and selective methyl protonation. This strategy enables proton‐detected structural studies of biomolecular solids with enhanced sensitivity under DNP conditions.
James Tolchard, Tanguy Le Marchand, Nadia El Mammeri, Kshama Sharma, Ajit Kumar Bishoyi, Mélanie Berbon, Kristaps Jaudzems, Dorothea Wisser, Asen Daskalov, Sven J. Saupe, Jan Stanek, Zhiyu Sun, Olivier Ouari, Birgit Habenstein, Anne Lesage, Guido Pintacuda, Antoine Loquet   +16 more
wiley   +2 more sources

Multifaceted role of sialylation in prion diseases

Frontiers in Neuroscience, 2016
Mammalian prion or PrPSc is a proteinaceous infectious agent that consists of a misfolded, self-replicating state of a sialoglycoprotein called the prion protein or PrPC. Sialylation of the prion protein N-linked glycans was discovered more than 30 years
Ilia V Baskakov, Ilia V Baskakov, Elizaveta Katorcha, Elizaveta Katorcha   +3 more
doaj   +1 more source

Prion peptide-mediated calcium level alteration governs neuronal cell damage through AMPK-autophagy flux

Cell Communication and Signaling, 2020
Background The distinctive molecular structure of the prion protein, PrPsc, is established only in mammals with infectious prion diseases. Prion protein characterizes either the transmissible pathogen itself or a primary constituent of the disease.
Ji-Hong Moon, Sang-Youel Park
doaj   +1 more source

Characterizing Cutaneous α‐Synuclein Deposition and Seeding Activity in Parkinson's Disease Subtypes

Annals of Clinical and Translational Neurology, EarlyView.
ABSTRACT Objective Cutaneous phosphorylated α‐synuclein (p‐syn) and α‐synuclein seeding activity are promising biomarkers for Parkinson's disease (PD), but their clinical value remains uncertain due to disease heterogeneity. This study evaluates these two biomarkers in PD patients to inform phenotype‐specific diagnosis and disease severity assessment ...
Yuting Jin, Tianyuan Yang, Minglei Liu, Haiyang Luo, Jing Yuan, Ke Zhang, Xinsheng Han, Jing Yang, Yuming Xu   +8 more
wiley   +1 more source

The Molecular Pathology of Prion Diseases [PDF]

, 2004
Prion diseases, or transmissible spongiform encephalopathies (TSEs), are a group of invariably fatal neurodegenerative disorders. Uniquely, they may present as sporadic, inherited, or infectious forms, all of which involve conversion of the normal ...
Vassallo, Neville, Herms, Jochen, Kretzschmar, Hans A.   +2 more
core  

Genetic variability of the prion protein gene (PRNP) in wild ruminants from Italy and Scotland [PDF]

, 2009
The genetics of the prion protein gene (PRNP) play a crucial role in determining the relative susceptibility to transmissible spongiform encephalopathies (TSEs) in several mammalian species.
Acutis, Pier Luigi, Pier Luigi Acutis, Ezio Ferroglio, Simone Peletto, Hugh W. Reid, Perucchini, Matteo, Serena Robetto, Acin, Cristina, Bozzetta, Elena, Reid, Hugh W., Dalgleish, Mark P., Orusa, Riccardo, Elena Bozzetta, Ferroglio, Ezio, Sacchi, Paola, Paula Stewart, Daniela Meloni, Wilfred Goldmann, Meloni, Daniela, Gennero, Silvia, Riccardo Orusa, Roberto Rasero, Rasero, Roberto, Cristina Acín, Matteo Perucchini, Mark P. Dalgleish, Goldmann, Wilfred, Stewart, Paula, Maria Caramelli, Silvia Gennero, Caramelli, Maria, Robetto, Serena, Peletto, Simone, Paola Sacchi   +33 more
core   +1 more source

Protein-lipid interactions and protein anchoring modulate the modes of association of the globular domain of the Prion protein and Doppel protein to model membrane patches

Frontiers in Bioinformatics
The Prion protein is the molecular hallmark of the incurable prion diseases affecting mammals, including humans. The protein-only hypothesis states that the misfolding, accumulation, and deposition of the Prion protein play a critical role in toxicity ...
Patricia Soto, Davis T. Thalhuber, Frank Luceri, Jamie Janos, Mason R. Borgman, Noah M. Greenwood, Sofia Acosta, Hunter Stoffel   +7 more
doaj   +1 more source

Unique Properties of the Rabbit Prion Protein Oligomer. [PDF]

PLoS ONE, 2016
Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a group of fatal neurodegenerative disorders infecting both humans and animals.
Ziyao Yu, Pei Huang, Yuanhui Yu, Zhen Zheng, Zicheng Huang, Chenyun Guo, Donghai Lin   +6 more
doaj   +1 more source