نتایج جستجو برای: human prion protein

تعداد نتایج: 2481093  

Journal: :Acta biochimica et biophysica Sinica 2013
Zhen Yuan Deming Zhao Lifeng Yang

Rabbits have low susceptibility to prion infection. Studies on prion protein (PrP) from animal species of different susceptibility to prion diseases identified key amino acid residues, specific motif, and special features in rabbit prion protein (RaPrP(C)) that contribute to the stability of rabbit PrP(C) and low susceptibility to prion infection. However, there is no evidence showing that rabb...

2015
Emmanuel A. Asante Andrew Grimshaw Michelle Smidak Tatiana Jakubcova Andrew Tomlinson Asif Jeelani Shyma Hamdan Caroline Powell Susan Joiner Jacqueline M. Linehan Sebastian Brandner Jonathan D. F. Wadsworth John Collinge Jason Bartz

Inherited prion disease (IPD) is caused by autosomal-dominant pathogenic mutations in the human prion protein (PrP) gene (PRNP). A proline to leucine substitution at PrP residue 102 (P102L) is classically associated with Gerstmann-Sträussler-Scheinker (GSS) disease but shows marked clinical and neuropathological variability within kindreds that may be caused by variable propagation of distinct ...

2011
Iva Hafner-Bratkovič Lars Gaedtke Andrej Ondracka Peter Veranič Ina Vorberg Roman Jerala

Prion diseases are fatal neurodegenerative diseases, which can be acquired, sporadic or genetic, the latter being linked to mutations in the gene encoding prion protein. We have recently described the importance of subdomain separation in the conversion of prion protein (PrP). The goal of the present study was to investigate the effect of increasing the hydrophobic interactions within the H2-H3...

2010
Wei Hu Stefan Nessler Bernhard Hemmer Todd N. Eagar Lawrence P. Kane S. Rutger Leliveld Andreas Müller-Schiffmann Anne R. Gocke Amy Lovett-Racke Li-Hong Ben Rehana Z. Hussain Andreas Breil Jeffrey L. Elliott Krishna Puttaparthi Petra D. Cravens Mahendra P. Singh Benjamin Petsch Lothar Stitz Michael K. Racke Carsten Korth Olaf Stüve

The primary biological function of the endogenous cellular prion protein has remained unclear. We investigated its biological function in the generation of cellular immune responses using cellular prion protein gene-specific small interfering ribonucleic acid in vivo and in vitro. Our results were confirmed by blocking cellular prion protein with monovalent antibodies and by using cellular prio...

Journal: :Chemical science 2017
S Alexis Paz Eric Vanden-Eijnden Cameron F Abrams

We study the thermodynamic stability of the native state of the human prion protein using a new free-energy method, replica-exchange on-the-fly parameterization. This method is designed to overcome hidden-variable sampling limitations to yield nearly error-free free-energy profiles along a conformational coordinate. We confirm that all four (M129V, D178N) polymorphs have a ground-state conforma...

Journal: :The Journal of clinical investigation 2014
Charles E Mays Chae Kim Tracy Haldiman Jacques van der Merwe Agnes Lau Jing Yang Jennifer Grams Michele A Di Bari Romolo Nonno Glenn C Telling Qingzhong Kong Jan Langeveld Debbie McKenzie David Westaway Jiri G Safar

The symptoms of prion infection can take years or decades to manifest following the initial exposure. Molecular markers of prion disease include accumulation of the misfolded prion protein (PrPSc), which is derived from its cellular precursor (PrPC), as well as downregulation of the PrP-like Shadoo (Sho) glycoprotein. Given the overlapping cellular environments for PrPC and Sho, we inferred tha...

Journal: :Neuro-degenerative diseases 2005
Christina Sigurdson Magdalini Polymenidou Adriano Aguzzi

With the epizootics of bovine spongiform encephalopathy (BSE) in North American cattle, BSE infections in goats, new forms of human Creutzfeldt-Jakob disease (CJD) and the spread of chronic wasting disease in North American deer and elk, one wonders whether we are gaining control over the transmissible spongiform encephalopathies (TSEs). Although many basic scientific questions in the prion fie...

Journal: :Brain research 2012
Oliver D King Aaron D Gitler James Shorter

Prions are self-templating protein conformers that are naturally transmitted between individuals and promote phenotypic change. In yeast, prion-encoded phenotypes can be beneficial, neutral or deleterious depending upon genetic background and environmental conditions. A distinctive and portable 'prion domain' enriched in asparagine, glutamine, tyrosine and glycine residues unifies the majority ...

Journal: :Neuron 1998
Roberto Chiesa Pedro Piccardo Bernardino Ghetti David A Harris

Familial prion diseases are caused by mutations in the gene encoding the prion protein (PrP). We have produced transgenic mice that express the mouse homolog of a mutant human PrP containing a nine octapeptide insertion associated with prion dementia. These mice exhibit a slowly progressive neurological disorder characterized clinically by ataxia and neuropathologically by cerebellar atrophy an...

Journal: :World journal of virology 2015
Raymond Bujdoso Matthias Landgraf Walker S Jackson Alana M Thackray

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 diseases. Collectively, these conditions are a challenge to society because of the increasing aged population and through the real threat to human fo...

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