Results 61 to 70 of about 56,657 (298)

Characterization of the prion protein in relation to normal cellular function and in disease [PDF]

, 2012
Transmissible spongiform encephalopathies (TSEs), also known as prion diseases, are a group of rare and fatal neurodegenerative disorders that can affect both human and animals.
Wik, Lotta
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

Inhibition and Formation of Amyloid Fibrils in the Bulk and at the Interface of Biomolecular Condensates

Angewandte Chemie, EarlyView.
In this review, we discuss how biomolecular condensates can inhibit amyloid aggregation in their interior, while still facilitating fibril formation at the interface between the dense and dilute phases, where molecular and mesoscale properties are likely optimal to promote protein aggregation.
Marcell Papp, Chiara Morelli, Sarah Khawaja, Paolo Arosio   +3 more
wiley   +2 more sources

Reversible symptoms and clearance of mutant prion protein in an inducible model of a genetic prion disease in Drosophila melanogaster

Neurobiology of Disease, 2014
Prion diseases are progressive disorders that affect the central nervous system leading to memory loss, personality changes, ataxia and neurodegeneration.
A. Murali, R.A. Maue, P.J. Dolph
doaj   +1 more source

A high-content neuron imaging assay demonstrates inhibition of prion disease-associated neurotoxicity by an anti-prion protein antibody

Scientific Reports, 2022
There is an urgent need to develop disease-modifying therapies to treat neurodegenerative diseases which pose increasing challenges to global healthcare systems.
Madeleine Reilly, Iryna Benilova, Azadeh Khalili-Shirazi, Christian Schmidt, Parvin Ahmed, Daniel Yip, Parmjit S. Jat, John Collinge   +7 more
doaj   +1 more source

Turning Unpredictable Biomolecule Adsorption to Controlled Corona Formation: Focus on Carbon Nanomaterials

Advanced Materials, EarlyView.
Controlling the protein corona formation onto carbon nanomaterials (CNMs) enhances their functionalities as platforms for cancer theranostics. Here, we reviewed the effects of the intrinsic and acquired properties of CNMs on protein corona formation, the consequent biological and toxicological outcomes, and the strategies to reshape corona formation ...
Yajuan Zou, Yalei Hu, Jie Yu, Naoki Komatsu, Yuta Nishina, Alberto Bianco   +5 more
wiley   +1 more source

Water‐Mediated Phosphoryl Wires Stabilize Pathological Tau Fibrils

Angewandte Chemie, EarlyView.
Extended 1D phosphoryl “wires” stabilize in‐register amyloid tau fibrils, as demonstrated by multiple‐quantum spin‐counting NMR, TEM, and MD simulations, using fibrils of tau peptide jR2R3‐P301L (tau295–313) with phosphorylation at S305 or Y310. ABSTRACT Hyperphosphorylation of tau is a hallmark of tauopathies, with specific phosphorylation sites ...
Lokeswara Rao Potnuru, Austin DuBose, Fiona Mon, Mesopotamia S. Nowotarski, Michael Vigers, Boqin Zhang, Chung‐Ta Han, John E. Straub, Songi Han   +8 more
wiley   +2 more sources

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

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

Prion protein interconversions† [PDF]

Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences, 2001
The transmissible spongiform encephalopathies (TSEs), or prion diseases, remain mysterious neurodegenerative diseases that involve perturbations in prion protein (PrP) structure. This article summarizes our use ofin vitromodels to describe how PrP is converted to the disease–associated, protease–resistant form.
openaire   +2 more sources