Results 61 to 70 of about 5,869 (184)
Identification of Candidate Proteins Binding to Prion Protein
Neurobiology of Disease, 1997 Prion diseases are disorders of protein conformation that produce neurodegeneration in humans and animals. Studies of transgenic (Tg) mice indicate that a factor designated protein X is involved in the conversion of the normal cellular prion protein ...
Fruma Yehiely +7 more
doaj +1 more source
Kosmotropic Anions Promote Conversion of Recombinant Prion Protein into a PrPSc-Like Misfolded Form
PLoS ONE, 2012 Prions are self-propagating proteins involved in transmissible spongiform encephalopaties in mammals. An aberrant conformation with amyloid-like features of a cell surface protein, termed prion protein (PrP), is thought to be the essential component of the infectious particle, though accessory co-factor molecules such as lipids and nucleotides may be ...
Rodrigo Diaz-Espinoza +2 more
openaire +4 more sources
MRI characteristics of sporadic CJD with valine homozygosity at codon 129 of the prion protein gene and PrPSc type 2 in Japan [PDF]
Journal of Neurology, Neurosurgery & Psychiatry, 2004 Two Japanese sporadic Creutzfeld-Jakob disease (sCJD) patients with valine homozygosity at codon 129 of the prion protein gene and protease-resistant prion protein (PrP(Sc)) type 2 (VV2) are described. In contrast with Western countries, this type of sCJD is very rare in Japan.
R, Fukushima +5 more
openaire +2 more sources
Brain and Behavior, Volume 15, Issue 12, December 2025.This study investigates the sleep‐related manifestations of Creutzfeldt–Jakob disease (CJD) by analyzing electroencephalography (EEG) and polysomnography (PSG) findings in a cohort of seven patients diagnosed between 2013 and 2023. Although only three patients initially reported sleep‐related complaints, comprehensive assessments revealed that all ...
Ezgi Demirel +4 more
wiley +1 more source
Recombinant PrP and Its Contribution to Research on Transmissible Spongiform Encephalopathies
Pathogens, 2017 The misfolding of the cellular prion protein (PrPC) into the disease-associated isoform (PrPSc) and its accumulation as amyloid fibrils in the central nervous system is one of the central events in transmissible spongiform encephalopathies (TSEs). Due to
Jorge M. Charco +7 more
doaj +1 more source
Copper and Zinc Interactions with Cellular Prion Proteins Change Solubility of Full-Length Glycosylated Isoforms and Induce the Occurrence of Heterogeneous Phenotypes. [PDF]
PLoS ONE, 2016 Prion diseases are characterized biochemically by protein aggregation of infectious prion isoforms (PrPSc), which result from the conformational conversion of physiological prion proteins (PrPC).
Svetlana Brim +2 more
doaj +1 more source
Neurobiology of Disease, 2001 A nine-octapeptide insertional mutation in the prion protein (PrP) gene is associated with an inherited variant of Creutzfeldt-Jakob disease in humans. Transgenic mice that express the mouse PrP homologue of this mutation (designated PG14) under control of a PrP promoter display a progressive neurological disorder characterized by ataxia, apoptosis of ...
Roberto Chiesa +6 more
openaire +3 more sources
A Prion‐Like Domain in EBV EBNA1 Promotes Phase Separation and Enables SRRM1 Splicing
Advanced Science, Volume 12, Issue 41, November 6, 2025.This study discoveries that EBV EBNA1 behaves as a prion‐like protein, verified using cell‐based assays and the Saccharomyces cerevisiae Sup35p prion identification system. The prion‐like domain of EBNA1 drives liquid–liquid phase separation. EBNA1 interacts with the splicing factor SRSF1 to regulate the expression of the SRRM1 splicing isoforms ...
Xiaoyue Zhang +17 more
wiley +1 more source
The Chemical Record, Volume 25, Issue 10, October 2025.This review explores aptamers as therapeutic oligonucleotides targeting neurodegenerative diseases, including Alzheimer's, Parkinson's, and Huntington's, with a focus on G‐quadruplex‐forming sequences. It discusses chemical modifications that enhance aptamer stability and function, alongside the use of clay nanoparticles, such as halloysite nanotubes ...
Valentina Arciuolo +9 more
wiley +1 more source
The FASEB Journal, Volume 39, Issue 17, 15 September 2025.Knock‐in mice expressing PrP with a partial deletion of the C‐terminal signal sequence (KIBVPrP248) showed reduced PrPC expression and resistance to prion infection. The underlying mechanism is that the mutant PrP is aberrantly retained in the endoplasmic reticulum and eventually undergoes proteasomal degradation.
Miryeong Yoo +12 more
wiley +1 more source