Results 41 to 50 of about 1,598,142 (264)
Viruses, 2014 The key event in prion pathogenesis is the structural conversion of the normal cellular protein, PrPC, into an aberrant and partially proteinase K resistant isoform, PrPSc.
Evgenia Salta +5 more
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Prion Protein Misfolding [PDF]
Current Molecular Medicine, 2009 The crucial event in the development of transmissible spongiform encephalopathies (TSEs) is the conformational change of a host-encoded membrane protein - the cellular PrP(C) - into a disease associated, fibril-forming isoform PrP(Sc). This conformational transition from the alpha-helix-rich cellular form into the mainly beta-sheet containing ...
Kupfer, L, Hinrichs, W, Groschup, M.H
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Effects of post-translational modifications on prion protein aggregation and the propagation of scrapie-like characteristics in vitro [PDF]
, 2007 Prion diseases, or transmissible spongiform encephalopathies (TSEs) are typically characterised by CNS accumulation of PrPSc, an aberrant conformer of a normal cellular protein PrPC.
Oxley, David +9 more
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Prion, 2019 A number of fungal proteins are capable of adopting multiple alternative, self-perpetuating prion conformations. These prion variants are associated with functional alterations of the prion-forming protein and thus the generation of new, heritable traits
Ben Allwein +4 more
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The crystal structure of the globular domain of sheep prion protein [PDF]
, 2004 The prion protein PrP is a naturally occurring polypeptide that becomes transformed from a normal conformation to that of an aggregated form, characteristic of pathological states in fatal transmissible spongiform conditions such as Creutzfeld–Jacob ...
Vasisht N +28 more
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Hsp40/JDP Requirements for the Propagation of Synthetic Yeast Prions
Viruses, 2022 Yeast prions are protein-based transmissible elements, most of which are amyloids. The chaperone protein network in yeast is inexorably linked to the spreading of prions during cell division by fragmentation of amyloid prion aggregates. Specifically, the
Sarah C. Miller +5 more
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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
Vé Ronique Gayrard +13 more
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AMYCO: evaluation of mutational impact on prion-like proteins aggregation propensity
BMC Bioinformatics, 2019 Background Around 1% of human proteins are predicted to contain a disordered and low complexity prion-like domain (PrLD). Mutations in PrLDs have been shown promote a transition towards an aggregation-prone state in several diseases. Results Recently, we
Valentin Iglesias +3 more
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Neural regeneration research, 2013 Transmissible spongiform encephalopathy or prion disease is triggered by the conversion from cellular prion protein to pathogenic prion protein. Growing evidence has concentrated on prion protein configuration changes and their correlation with prion disease transmissibility and pathogenicity.
Song, Zhiqi, Zhao, Deming, Yang, Lifeng
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The Prion-like domain in the exomer-dependent cargo Pin2 serves as a trans-Golgi retention motif [PDF]
, 2014 Prion and prion-like domains (PLDs) are found in many proteins throughout the animal kingdom. We found that the PLD in the S. cerevisiae exomer-depen- dent cargo protein Pin2 is involved in the regulation of protein transport and localization. The domain
Ritz, Alicja M. +11 more
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