نتایج جستجو برای: prion protein

تعداد نتایج: 1238350  

Journal: :Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 2001

Journal: :Acta biochimica et biophysica Sinica 2013
Zheng Zhou Gengfu Xiao

Prion diseases are a group of infectious fatal neurodegenerative diseases. The conformational conversion of a cellular prion protein (PrP(C)) into an abnormal misfolded isoform (PrP(Sc)) is the key event in prion diseases pathology. Under normal conditions, the high-energy barrier separates PrP(C) from PrP(Sc) isoform. However, pathogenic mutations, modifications as well as some cofactors, such...

2015
Federico Benetti Giuseppe Legname

Prions are the etiological agent of fatal neurodegenerative diseases called prion diseases or transmissible spongiform encephalopathies. These maladies can be sporadic, genetic or infectious disorders. Prions are due to post-translational modifications of the cellular prion protein leading to the formation of a β-sheet enriched conformer with altered biochemical properties. The molecular events...

Journal: :Molecular cell 2007
Mark Kristiansen Pelagia Deriziotis Derek E Dimcheff Graham S Jackson Huib Ovaa Heike Naumann Anthony R Clarke Fijs W B van Leeuwen Victoria Menéndez-Benito Nico P Dantuma John L Portis John Collinge Sarah J Tabrizi

The mechanism of cell death in prion disease is unknown but is associated with the production of a misfolded conformer of the prion protein. We report that disease-associated prion protein specifically inhibits the proteolytic beta subunits of the 26S proteasome. Using reporter substrates, fluorogenic peptides, and an activity probe for the beta subunits, this inhibitory effect was demonstrated...

Journal: :Science 1991
S B Prusiner

Prions cause transmissible and genetic neurodegenerative diseases, including scrapie and bovine spongiform encephalopathy of animals and Creutzfeldt-Jakob and Gerstmann-Sträussler-Scheinker diseases of humans. Infectious prion particles are composed largely, if not entirely, of an abnormal isoform of the prion protein, which is encoded by a chromosomal gene. A posttranslational process, as yet ...

Journal: :Journal of virology 2007
Yuri Kawasaki Keiichi Kawagoe Chun-jen Chen Kenta Teruya Yuji Sakasegawa Katsumi Doh-ura

The establishment of effective therapeutic interventions for prion diseases is necessary. We report on a newly developed amyloidophilic compound that displays therapeutic efficacy when administered orally. This compound inhibited abnormal prion protein formation in prion-infected neuroblastoma cells in a prion strain-dependent manner: effectively for RML prion and marginally for 22L prion and F...

Journal: :Journal of Neurochemistry 2005

Journal: :The Biochemical journal 2003
Sheena M Whyte Ian D Sylvester Stephen R Martin Andrew C Gill Franziska Wopfner Hermann M Schätzl Guy G Dodson Peter M Bayley

Both prion protein and the structurally homologous protein doppel are associated with neurodegenerative disease by mechanisms which remain elusive. We have prepared murine doppel, and a mutant with one of the two disulphide bonds removed, in the expectation of increasing the similarity of doppel to prion protein in terms of conformation and stability. Unfolding studies of doppel and the mutant ...

2013
Paul Shapshak

Human prion brain disease has been studied intensely since 1920. Examples of such diseases include Creutzfeldt-Jakob disease (CJD), fatal familial insomnia, Gerstmann-StrausslerScheinker disease, and Kuru. Central in the epidemiology and pathogenesis of prion diseases is the prion protein itself and the gene for this protein resides on chromosome 12, at locus 20pterp12. The prion protein is ter...

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