Results 131 to 140 of about 16,662 (259)

Abnormal Expression of Proteolytic Stress‐Related Proteins and Protective Effect of Fibrinolytic Enzymes in Prion Diseases

open access: yesTransboundary and Emerging Diseases
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

open access: yesThe Journal of Physiology, EarlyView.
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

open access: yesInternational Journal of Cell Biology, 2013
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

open access: yesClinical Anatomy, Volume 39, Issue 3, Page 346-367, April 2026.
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

Characterisation and prion transmission study in mice with genetic reduction of sporadic Creutzfeldt-Jakob disease risk gene Stx6

open access: yesNeurobiology of Disease
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

open access: yesProtein Science, Volume 35, Issue 4, April 2026.
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

open access: yesProtein Science, Volume 35, Issue 4, April 2026.
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]

open access: yes, 2019
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

In silico peptide self‐assembly reveals the importance of N‐terminal motifs and the inhibition mechanism of the mutation L38M in α‐synuclein fibrillation

open access: yesProtein Science, Volume 35, Issue 4, April 2026.
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]

open access: yes, 2010
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

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