منابع مشابه
Prion Protein Misfolding
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 counterpart initiates an 'autocatalytic' reaction wh...
متن کاملDeadly Conformations—Protein Misfolding in Prion Disease
and progressive dementia, occurring after age 40, associated , as in kuru, with plaques in the brain of affected * Department of Genetics and Howard Hughes Medical Institute individuals (Gerstmann et al., 1936). Multiple affected family members were observed, in a pattern indicating Yale University School of Medicine New Haven, Connecticut 06510 autosomal-dominant inheritance. Similar genetic t...
متن کاملMisfolding of the prion protein: linking biophysical and biological approaches.
Prion diseases are a group of neurodegenerative diseases that can arise spontaneously, be inherited, or acquired by infection in mammals. The propensity of the prion protein to adopt different structures is a clue to its pathological and perhaps biological role too. While the normal monomeric PrP is well characterized, the misfolded conformations responsible for neurodegeneration remain elusive...
متن کاملLow density subcellular fractions enhance disease-specific prion protein misfolding.
The production of prion particles in vitro by amplification with or without exogenous seed typically results in infectivity titers less than those associated with PrP(Sc) isolated ex vivo and highlights the potential role of co-factors that can catalyze disease-specific prion protein misfolding in vivo. We used a cell-free conversion assay previously shown to replicate many aspects of transmiss...
متن کاملTwo Misfolding Routes for the Prion Protein around pH 4.5
Using molecular dynamics simulations, we show that the prion protein (PrP) exhibits a dual behavior, with two possible transition routes, upon protonation of H187 around pH 4.5, which mimics specific conditions encountered in endosomes. Our results suggest a picture in which the protonated imidazole ring of H187 experiences an electrostatic repulsion with the nearby guanidinium group of R136, t...
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ژورنال
عنوان ژورنال: Current Molecular Medicine
سال: 2009
ISSN: 1566-5240
DOI: 10.2174/156652409789105543