Results 131 to 140 of about 16,662 (259)
Prion diseases are fatal, irreversible, and infectious neurodegenerative diseases caused by proteinase K‐resistant prion protein (PrPSc). Against PrPSc, several endogenous proteases involved in cellular degradation mechanisms can be activated to remove PrPSc.
Yong-Chan Kim +2 more
openaire +2 more sources
Potential health benefits of cold‐water immersion: the central role of PGC‐1α
Abstract figure legend Cold‐water immersion (CWI) elicits autonomic, somato‐motoric (shivering thermogenesis), endocrine and metabolic, sensory transduction, and local biophysical effects that may converge on the transcriptional co‐activator PGC‐1α (centre).
Erich Hohenauer +2 more
wiley +1 more source
Prion Protein Misfolding, Strains, and Neurotoxicity: An Update from Studies on Mammalian Prions
Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a group of fatal neurodegenerative disorders affecting humans and other mammalian species.
Ilaria Poggiolini +2 more
doaj +1 more source
Infection Risk From Humans and Animals in the Anatomy Laboratory: A Scoping Review
ABSTRACT Whole‐body dissection is a cornerstone of anatomy education. During and following the COVID‐19 pandemic, exposure to infectious agents and other risks of dissection were highlighted. To identify potential risks, one must have the data outlining these risks in specific situations.
Margaret A. McNulty, Elizabeth R. Agosto
wiley +1 more source
Sporadic Creutzfeldt-Jakob disease (sCJD), the most common human prion disease, is thought to occur when the cellular prion protein (PrPC) spontaneously misfolds and assembles into prion fibrils, culminating in fatal neurodegeneration.
Emma Jones +18 more
doaj +1 more source
Functions of J‐domain proteins in mitochondrial protein biogenesis
Abstract Mitochondrial biogenesis and functions depend on the import and assembly of more than 1000 proteins that are made as precursors on cytosolic ribosomes. The majority of these precursor proteins are transported from the ribosome to the translocase of the outer membrane (TOM complex), which constitutes the main entry site for mitochondrial ...
Vitasta Tiku +3 more
wiley +1 more source
Toxic mechanisms of amyloid oligomers and therapeutic strategies
Abstract Amyloid oligomers are increasingly recognized as the major toxic contributors across protein‐misfolding disorders. In this review, we cover mechanistic evidence showing how these transient and structurally heterogeneous oligomers disrupt cellular homeostasis by: (i) permeabilizing lipid membranes and forming ion‐conducting pores; (ii ...
Magdalena I. Ivanova +2 more
wiley +1 more source
Cellular distribution of the prion protein in palatine tonsils of mule deer (Odocoileus hemionus) and Rocky Mountain elk (Cervus elaphus nelsoni) [PDF]
Chronic wasting disease (CWD) is a transmissible spongiform encephalopathy (TSE) that affects members of the Cervidae family, including deer (Odocoileus spp.), elk (Cervus Canadensis spp.), and moose (Alces alces spp.).
Belden, E. Lee +2 more
core +1 more source
Abstract Alpha‐synuclein (αSyn) is a presynaptic protein associated with several neurodegenerative diseases. While the non‐amyloid component (NAC) region of the αSyn sequence (residues 65–90) forms the core of all αSyn fibrils, recent findings suggest that the flanking regions play a key role in initiating or preventing amyloid formation. Two motifs in
Van T. T. Nguyen +4 more
wiley +1 more source
Prions: an evolutionary perspective [PDF]
Studies in both prion-due diseases in mammals and some non-Mendelian hereditary processes in yeasts have demonstrated that certain proteins are able to transmit structural information and self-replication.
Alfonso Ogayar, Miguel Sánchez-Pérez
core +2 more sources

