Results 41 to 50 of about 1,549,882 (213)
Prion acute synaptotoxicity is largely driven by protease-resistant PrPSc species. [PDF]
Although misfolding of normal prion protein (PrPC) into abnormal conformers (PrPSc) is critical for prion disease pathogenesis our current understanding of the underlying molecular pathophysiology is rudimentary. Exploiting an electrophysiology paradigm,
Simote Totauhelotu Foliaki +11 more
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Pharmacological Agents Targeting the Cellular Prion Protein
Prion diseases are associated with the conversion of the cellular prion protein (PrPC), a glycoprotein expressed at the surface of a wide variety of cell types, into a misfolded conformer (the scrapie form of PrP, or PrPSc) that accumulates in brain ...
Maria Letizia Barreca +4 more
doaj +1 more source
Prion protein amino acid sequence influences formation of authentic synthetic PrPSc
AbstractSynthetic prions, generated de novo from minimal, non-infectious components, cause bona fide prion disease in animals. Transmission of synthetic prions to hosts expressing syngeneic PrPC results in extended, variable incubation periods and incomplete attack rates.
Alyssa J. Block +4 more
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Detecting a psoriatic antigen analogous to infectious prion proteins
Until now, psoriatic antigen as a specific antigen derived from some infectious agent potentially related to origin of psoriasis has not been identified, thereby strongly arguing against infectious theory of psoriasis.
B. F. Sinitsyn
doaj +1 more source
Amyloid-based neurodegenerative diseases such as prion, Alzheimer's, and Parkinson's diseases have distinct etiologies and clinical manifestations, but they share common pathological events.
Benoit Schneider +17 more
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Charged bipolar suramin derivatives induce aggregation of the prion protein at the cell surface and inhibit PrPSc replication [PDF]
The conversion of the cellular prion protein (PrPc) into a pathogenic isoform (PrPSc) is one of the underlying events in the pathogenesis of the fatal transmissible spongiform encephalopathies (TSEs). Numerous compounds have been described to inhibit prion replication and PrPSc accumulation in cell culture.
Max, Nunziante +5 more
openaire +2 more sources
Creutzfeldt-Jakob Disease, Prion Protein Gene Codon 129VV, and a Novel PrPSc Type in a Young British Woman [PDF]
Variant Creutzfeldt-Jakob disease (vCJD) is an acquired prion disease causally related to bovine spongiform encephalopathy that has occurred predominantly in young adults. All clinical cases studied have been methionine homozygotes at codon 129 of the prion protein gene (PRNP) with distinctive neuropathological findings and molecular strain type (PrP ...
Simon, Mead +7 more
openaire +2 more sources
INTERRELATION OF PRIONS WITH NON-CODING RNAS
Prions are alternative infectious conformations for some cellular proteins. For the protein PrPC (PrP – prion protein, С – common), a prion conformation, called PrPSc (S – scrapie), is pathological.
R. N. Mustafin, E. K. Khusnutdinova
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Post-translational modifications in prion diseases
More than 650 reversible and irreversible post-translational modifications (PTMs) of proteins have been listed so far. Canonical PTMs of proteins consist of the covalent addition of functional or chemical groups on target backbone amino-acids or the ...
Chloé Bizingre +12 more
doaj +1 more source
Prediction of Prion Proteins in E. coli Based on Bimodal Sequence Characteristics
ABSTRACT Prions are infectious proteins that bear misfolded conformations capable of converting folded states into misfolded aggregates under physiologically relevant conditions. In mammals, prions cause deadly maladies including Creutzfeldt‐Jakob and chronic wasting disease. To date, several prion proteins have been identified in eukaryotes, primarily
Katherine Shreeve +5 more
wiley +1 more source

