Results 21 to 30 of about 50,704 (271)
Morphine Withdrawal Modifies Prion Protein Expression in Rat Hippocampus. [PDF]
PLoS ONE, 2017 The hippocampus is a vulnerable brain structure susceptible to damage during aging and chronic stress. Repeated exposure to opioids may alter the brain so that it functions normally when the drugs are present, thus, a prolonged withdrawal might lead to ...
Vincenzo Mattei +9 more
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Prion protein interconversions† [PDF]
Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences, 2001 The transmissible spongiform encephalopathies (TSEs), or prion diseases, remain mysterious neurodegenerative diseases that involve perturbations in prion protein (PrP) structure. This article summarizes our use ofin vitromodels to describe how PrP is converted to the disease–associated, protease–resistant form.
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Prion Neurotoxicity: Insights from Prion Protein Mutants [PDF]
Current Issues in Molecular Biology, 2010 The chemical nature of prions and the mechanism by which they propagate are now reasonably well understood. In contrast, much less is known about the identity of the toxic prion protein (PrP) species that are responsible for neuronal death, and the cellular pathways that these forms activate.
Solomon, Isaac H. +2 more
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Prion protein and prion disease at a glance [PDF]
Journal of Cell Science, 2021 ABSTRACT Prion diseases are neurodegenerative disorders caused by conformational conversion of the cellular prion protein (PrPC) into scrapie prion protein (PrPSc). As the main component of prion, PrPSc acts as an infectious template that recruits and converts normal cellular PrPC into its pathogenic, misfolded isoform. Intriguingly, the
Zhu, Caihong, Aguzzi, Adriano
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The cellular prion protein beyond prion diseases
Swiss Medical Weekly, 2020 The cellular prion protein (PrPC), a cell surface glycoprotein originally identified for its central role in prion diseases (also called transmissible spongiform encephalopathies), has recently been implicated in the pathogenesis of other neurodegenerative disorders, such as Alzheimer’s and Parkinson’s diseases, by acting as a toxicity-transducing ...
Manni, Giorgia +7 more
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Frontiers in Cell and Developmental Biology, 2014 The cellular prion protein (PrP(C)) has been widely investigated ever since its conformational isoform, the prion (or PrP(Sc)), was identified as the etiological agent of prion disorders. The high homology shared by the PrP(C)-encoding gene among mammals, its high turnover rate and expression in every tissue strongly suggest that PrP(C) may possess key
Gasperini, Lisa, Legname, Giuseppe
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Prion, 2023 Misfolding of the prion protein is central to prion disease aetiology. Although understanding the dynamics of the native fold helps to decipher the conformational conversion mechanism, a complete depiction of distal but coupled prion protein sites common
Patricia Soto +5 more
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A Sequence-Dependent DNA Condensation Induced by Prion Protein
Journal of Nucleic Acids, 2018 Different studies indicated that the prion protein induces hybridization of complementary DNA strands. Cell culture studies showed that the scrapie isoform of prion protein remained bound with the chromosome. In present work, we used an oxazole dye, YOYO,
Alakesh Bera, Sajal Biring
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A quantitative characterization of interaction between prion protein with nucleic acids
Biochemistry and Biophysics Reports, 2018 Binding of recombinant prion protein with small highly structured RNAs, prokaryotic and eukaryotic prion protein mRNA pseudoknots, tRNA and polyA has been studied by the change in fluorescence anisotropy of the intrinsic tryptophan groups of the protein.
Alakesh Bera, Sajal Biring
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Potential Therapeutic Use of Stem Cells for Prion Diseases
Cells, 2023 Prion diseases are neurodegenerative disorders that are progressive, incurable, and deadly. The prion consists of PrPSc, the misfolded pathogenic isoform of the cellular prion protein (PrPC).
Mohammed Zayed +2 more
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