نتایج جستجو برای: human prion protein
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BACKGROUND Amyloid fibrils associated with neurodegenerative diseases can be considered biologically relevant failures of cellular quality control mechanisms. It is known that in vivo human Tau protein, human prion protein, and human copper, zinc superoxide dismutase (SOD1) have the tendency to form fibril deposits in a variety of tissues and they are associated with different neurodegenerative...
Prions represent an unusual structural form of a protein that is 'infectious'. In mammals, prions are associated with fatal neurodegenerative diseases such as CJD (Creutzfeldt-Jakob disease), while in fungi they act as novel epigenetic regulators of phenotype. Even though most of the human prion diseases arise spontaneously, we still know remarkably little about how infectious prions form de no...
The Semliki-Forest virus (SFV) system was used to overexpress human wild-type and mutant prion proteins as well as FLAG-tagged human and bovine PrP in mammalian cells. The application of recombinant SFV vectors allowed a high-level production of highly glycosylated prion proteins with a molecular weight ranging from 25 to 30 kDa for recombinant wild-type human PrP and from 26 to 32 kDa for wild...
A familial form of Creutzfeldt-Jakob disease (CJD) is linked to the D178N/V129 prion protein (PrP) mutation. Tg(CJD) mice expressing the mouse homolog of this mutant PrP synthesize a misfolded form of the mutant protein, which is aggregated and protease resistant. These mice develop clinical and pathological features reminiscent of CJD, including motor dysfunction, memory impairment, cerebral P...
Background: A polymorphism in position 129 in the human prion protein modulates susceptibility to prion infection and disease phenotype. Results: Mutations to various amino acids highlights the importance of position 129 during amyloid fibrillation. Conclusion: Position 129 is a key site for early intermolecular interactions during fibrillation. Significance: Insight into early mechanisms of ag...
Disease-related prion protein, PrP(Sc), is classically distinguished from its normal cellular precursor, PrP(C), by its detergent insolubility and partial resistance to proteolysis. Molecular diagnosis of prion disease typically relies upon detection of protease-resistant fragments of PrP(Sc) using proteinase K, however it is now apparent that the majority of disease-related PrP and indeed prio...
found to be a minor component of amyloid plaques in Alzheimer's disease [19]. Alternatively, it is possible that there is an inhibitor of prion generation and propagation whose activity is inhibited by an excess of another prion. Excess Hsp104p cures [PSI + ] [20], excess Ydj1p (an Hsp40) can cure [URE3] [21], and Sis1p (another Hsp40) cures [RNQ + ] [22]. Overexpression of Ssb members of the H...
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