نتایج جستجو برای: prion protein

تعداد نتایج: 1238350  

2010
J D F Wadsworth E A Asante J Collinge

Transgenic mice expressing human prion protein in the absence of endogenous mouse prion protein faithfully replicate human prions. These models reproduce all of the key features of human disease, including long clinically silent incubation periods prior to fatal neurodegeneration with neuropathological phenotypes that mirror human prion strain diversity. Critical contributions to our understand...

2016
Ilia V. Baskakov Elizaveta Katorcha

Mammalian prion or PrP(Sc) is a proteinaceous infectious agent that consists of a misfolded, self-replicating state of a sialoglycoprotein called the prion protein, or PrP(C). Sialylation of the prion protein N-linked glycans was discovered more than 30 years ago, yet the role of sialylation in prion pathogenesis remains poorly understood. Recent years have witnessed extraordinary growth in int...

Journal: :Annual review of neuroscience 2001
J Collinge

Prion diseases are transmissible neurodegenerative conditions that include Creutzfeldt-Jakob disease (CJD) in humans and bovine spongiform encephalopathy (BSE) and scrapie in animals. Prions appear to be composed principally or entirely of abnormal isoforms of a host-encoded glycoprotein, prion protein. Prion propagation involves recruitment of host cellular prion protein, composed primarily of...

2008
M. D. Ter-Avanesyan

Prions were originally defined as infectious agents of protein nature, which caused neurodegenerative diseases in animals and humans. The prion concept implies that the infectious agent is a protein in special conformation that can be transmitted to the normal molecules of the same protein through protein–protein interactions. Until the 1990s, the prion phenomenon was associated with the single...

Journal: :Annual review of pathology 2008
Adriano Aguzzi Christina Sigurdson Mathias Heikenwaelder

Prion diseases are infectious neurodegenerative diseases occurring in humans and animals with an invariably lethal outcome. One fundamental mechanistic event in prion diseases is the aggregation of aberrantly folded prion protein into large amyloid plaques and fibrous structures associated with neurodegeneration. The cellular prion protein (PrPC) is absolutely required for disease development, ...

Journal: :Acta crystallographica. Section F, Structural biology and crystallization communications 2011
Pravas Kumar Baral Barbara Wieland Mridula Swayampakula Magdalini Polymenidou Adriano Aguzzi Nat N V Kav Michael N G James

Prion diseases are neurodegenerative diseases that are characterized by the conversion of the cellular prion protein PrP(c) to the pathogenic isoform PrP(sc). Several antibodies are known to interact with the cellular prion protein and to inhibit this transition. An antibody Fab fragment, Fab POM1, was produced that recognizes a structural motif of the C-terminal domain of mouse prion protein. ...

Journal: :PLoS Pathogens 2006
Romolo Nonno Michele A. Di Bari Franco Cardone Gabriele Vaccari Paola Fazzi Giacomo Dell'Omo Claudia Cartoni Loredana Ingrosso Aileen Boyle Roberta Galeno Marco Sbriccoli Hans-Peter Lipp Moira Bruce Maurizio Pocchiari Umberto Agrimi

Transmission of prions between species is limited by the "species barrier," which hampers a full characterization of human prion strains in the mouse model. We report that the efficiency of primary transmission of prions from Creutzfeldt-Jakob disease patients to a wild rodent species, the bank vole (Clethrionomys glareolus), is comparable to that reported in transgenic mice carrying human prio...

Journal: :The Journal of biological chemistry 2002
Richard G Warner Christoph Hundt Stefan Weiss Jeremy E Turnbull

Data from cell culture and animal models of prion disease support the separate involvement of both heparan sulfate proteoglycans and copper (II) ions in prion (PrP) metabolism. Though direct interactions between prion protein and heparin have been recorded, little is known of the structural features implicit in this interaction or of the involvement of copper (II) ions. Using biosensor and enzy...

Journal: :Acta Biochimica et Biophysica Sinica 2014

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