Results 71 to 80 of about 4,254,953 (206)

Cystatin F is a biomarker of prion pathogenesis in mice.

PLoS ONE, 2017
Misfolding of the cellular prion protein (PrPC) into the scrapie prion protein (PrPSc) results in progressive, fatal, transmissible neurodegenerative conditions termed prion diseases.
Mario Nuvolone, Nicolas Schmid, Gino Miele, Silvia Sorce, Rita Moos, Christian Schori, Roger R Beerli, Monika Bauer, Philippe Saudan, Klaus Dietmeier, Ingolf Lachmann, Michael Linnebank, Roland Martin, Ulf Kallweit, Veronika Kana, Elisabeth J Rushing, Herbert Budka, Adriano Aguzzi   +17 more
doaj   +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

14‐3‐3γ Protects Against Postoperative Cognitive Dysfunction by Regulating Tau Thr205 Phosphorylation and Synaptic Integrity

Advanced Science, EarlyView.
Integrative multi‐cohort analyses identify 14‐3‐3γ as a biomarker and regulator of cognitive vulnerability. Experimental studies show that 14‐3‐3γ loss is associated with Tau Thr205 phosphorylation, synaptic dysfunction, and cognitive impairment, while genetic overexpression or pharmacological stabilization of 14‐3‐3γ confers protective effects in ...
Shouqiang Zhu, Xue Han, Heng Zhang, Chang Ye, Tianjiao Xia, Xiaoping Gu   +5 more
wiley   +1 more source

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

Cellular Prion Protein: From Physiology to Pathology

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   +1 more source

Prion‐Like Protein LENG8‐Mediated Nucleation Drives Stress Granule Assembly

Advanced Science, EarlyView.
LENG8 is a newly identified stress granule (SG) nucleator required for SG assembly. Following stress, nuclear LENG8 granules disassemble, allowing LENG8 to translocate into the cytoplasm and form independent nucleation foci. These foci fuse with canonical early G3BP1/TIA1 seeds via LENG8‐TIA1 binding to drive SG maturation.
Mingxing Zhang, Xin Wang, Yilan Teng, Zhicheng Wu, Jing Fan, Hongwen Zhu, Peng Dai   +6 more
wiley   +1 more source

Roles of prion proteins in mammalian development

Animal Cells and Systems
Prion protein (PrP) is highly conserved and is expressed in most tissues in a developmental stage-specific manner. Glycosylated cellular prion protein (PrPC) is found in most cells and subcellular areas as a physiological regulating molecule.
Yong-Pil Cheon, Chongsuk Ryou, Željko M. Svedružić   +2 more
doaj   +1 more source

Probing the Energy Landscape of α‐Synuclein Amyloid Fibril Formation by Systematic K‐to‐Q Mutagenesis

Advanced Science, EarlyView.
We use lysine‐to‐glutamine mutations to study the effect of electrostatics on the kinetics and thermodynamics of alpha‐synuclein amyloid fibril formation. We find that mutational effects map on their structural context within fibrils and identify residues that modulate the energy landscape of alpha‐synuclein self‐assembly. Our work outlines a scalable,
Antonin Kunka, Azad Farzadfard, Jacob Aunstrup Larsen, Rasmus Krogh Norrild, Federica Saraceno, Celia Fricke, Hossein Mohammad‐Beigi, Ahmed Sadek, Jonas Folke, Susana Aznar, Alexander K. Buell   +10 more
wiley   +1 more source

Regulation of GABA(A) and glutamate receptor expression, synaptic facilitation and long-term potentiation in the hippocampus of prion mutant mice [PDF]

, 2009
Background: Prionopathies are characterized by spongiform brain degeneration, myoclonia, dementia, and periodic electroencephalographic (EEG) disturbances.
Delgado-García, J. M., Llorens Torres, Franc, Rangel, Alejandra (R17729), Madroñal, Noelia, Rangel Rincones, Alejandra Helena, Rangel, A., Del Río, J. A., Llorens, Franc, Lauro Sumoy, Madroñal, N., Torres Juan María, Torres, Juan M., Sumoy, Lauro, Alejandra Rangel, Rosalina Gavín, Gruart i Massó, Agnès, Massó Agnès Gruart i., Llorens Franc, Noelia Madroñal, Río José Antonio Del, Juan María Torres, Gavin, Rosalina, Agnès Gruart, Gruart i Massó, A., Sumoy, L., Rangel Alejandra, Gavín Rosalina, Madroñal Noelia, Delgado-Garcia, Jose M., Franc Llorens, José Antonio Del Río, Sumoy Lauro, Río Fernández, José Antonio del, Torres, Juan María, Gavín Marín, Rosalina, José María Delgado-García, Agnès Gruart i. Massó, Rio, Jose A. del, Delgado-García José María, Delgado García, José M.   +39 more
core   +1 more source

Cellular Aspects of Prion Replication In Vitro

Viruses, 2013
Prion diseases or transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative disorders in mammals that are caused by unconventional agents predominantly composed of aggregated misfolded prion protein (PrP).
Ina Vorberg, Hanna Wolf, James Graham, Julia Hofmann, Andrea Grassmann   +4 more
doaj   +1 more source