Results 111 to 120 of about 5,604,422 (355)

Prion-induced neurotoxicity: Possible role for cell cycle activity and DNA damage response. [PDF]

, 2015
Protein misfolding neurodegenerative diseases arise through neurotoxicity induced by aggregation of host proteins. These conditions include Alzheimer's disease, Huntington's disease, Parkinson's disease, motor neuron disease, tauopathies and prion ...

core   +1 more source

Prion neuropathology follows the accumulation of alternate prion protein isoforms after infective titre has peaked

Nature Communications, 2014
Prions are lethal infectious agents thought to consist of multi-chain forms (PrPSc) of misfolded cellular prion protein (PrPC). Prion propagation proceeds in two distinct mechanistic phases: an exponential phase 1, which rapidly reaches a fixed level of ...
Malin K. Sandberg, H. Al-Doujaily, Bernadette Sharps, Michael Wiggins De Oliveira, Christian Schmidt, A. Richard-Londt, S. Lyall, J. Linehan, S. Brandner, J. Wadsworth, A. Clarke, J. Collinge   +11 more
semanticscholar   +1 more source

Emergence and evolution of yeast prion and prion-like proteins [PDF]

BMC Evolutionary Biology, 2016
Prions are transmissible, propagating alternative states of proteins, and are usually made from the fibrillar, beta-sheet-rich assemblies termed amyloid. Prions in the budding yeast Saccharomyces cerevisiae propagate heritable phenotypes, uncover hidden genetic variation, function in large-scale gene regulation, and can act like diseases.
An, Lu, Fitzpatrick, David A., Harrison, Paul M.   +2 more
openaire   +3 more sources

A Drosophila model of prion disease and its metabolic changes in the brain

Animal Models and Experimental Medicine, EarlyView.
We developed a Drosophila model for prion disease, and flies were capable of expressing the hamster prion protein (HaPrP) under the control of the GAL4/UAS system. The model exhibited some characteristics of the disease in mammals and displayed alterations in protein, sphingolipid, and carbohydrate metabolism. Preliminary applications have demonstrated
Dongdong Wang, Zhixin Sun, Pei Wen, Mengyang Zhao, Yuheng He, Fengting Gou, Jingjing Wang, Qing Fan, Xueyuan Li, Tianying Ma, Xiaoyu Wang, Wen Li, Sen Chen, Deming Zhao, Lifeng Yang   +14 more
wiley   +1 more source

Prion protein in the cerebrospinal fluid of healthy and naturally scrapie-affected sheep [PDF]

, 2006
The aim of this study was to characterize the cerebrospinal fluid (CSF) prion protein (PrP) of healthy and naturally scrapie-affected sheep. The soluble form of CSF PrPC immunoblotted with an anti-octarepeat and an anti-C terminus mAb showed two isoforms
Andréoletti, Banks, Baron, Baylis, Bieschke, Brown, Buschmann, Catherine Viguié, Chantal Imbs, Ecroyd, Elsen, Green, Hunter, Le Dur, Mohammed Moudjou, Morel, Moudjou, Nicole Picard-Hagen, Pierre-Louis Toutain, Rezaei, Safar, Toutain, Véronique Gayrard, Weller, Wong   +24 more
core   +3 more sources

Probing the N-terminal β-sheet conversion in the crystal structure of the human prion protein bound to a nanobody.

Journal of the American Chemical Society, 2014
Prions are fatal neurodegenerative transmissible agents causing several incurable illnesses in humans and animals. Prion diseases are caused by the structural conversion of the cellular prion protein, PrP(C), into its misfolded oligomeric form, known as ...
R. Abskharon, Gabriele Giachin, A. Wohlkonig, Sameh H. Soror, E. Pardon, G. Legname, J. Steyaert   +6 more
semanticscholar   +1 more source

Blood α‐Synuclein Separates Parkinson's Disease from Dementia with Lewy Bodies

Annals of Neurology, EarlyView.
Objective Aggregation of misfolded α‐synuclein (aSyn) within the brain is the pathologic hallmark of Lewy body diseases (LBDs), including Parkinson's disease (PD), and dementia with Lewy bodies (DLB) disease. Although evidence exists for aSyn “strains,” conformations with distinct biological properties, biomarkers for PD versus DLB are lacking.
George T. Kannarkat, Rebecca Zack, R. Tyler Skrinak, James F. Morley, Roseanne Davila‐Rivera, Sanaz Arezoumandan, Katherine Dorfman, Kelvin Luk, David A. Wolk, Daniel Weintraub, Thomas F. Tropea, Edward B. Lee, Sharon X. Xie, Ganesh Chandrasekaran, Virginia M.‐Y. Lee, David Irwin, Rizwan S. Akhtar, Alice S. Chen‐Plotkin   +17 more
wiley   +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

Genome-wide association study of behavioural and psychiatric features in human prion disease. [PDF]

, 2015
Prion diseases are rare neurodegenerative conditions causing highly variable clinical syndromes, which often include prominent neuropsychiatric symptoms.
Carswell, C, Collinge, J, Lowe, J, Lukic, A, MacKay, A, Mead, S, Porter, MC, Rudge, P, Thompson, AG, Uphill, J   +9 more
core   +1 more source

Prion Protein Amyloidosis

Brain Pathology, 1996
The prion protein (PrP) plays an essential role in the pathogenesis of a group of sporadic, genetically determined and infectious fatal degenerative diseases, referred to as “prion diseases”, affecting the central nervous system of humans and other mammals. The cellular PrP is encoded by a single copy gene, highly conserved across mammalian species. In
Katherine Young, Pedro Piccardo, Stephen R. Dlouhy, Frances Prelli, Fabrizio Tagliavini, Giorgio Giaccone, Martin R. Farlow, Orso Bugiani, Bernardino Ghetti, B. Frangione   +9 more
openaire   +3 more sources