Results 131 to 140 of about 57,548 (261)

All the Same? The Secret Life of Prion Strains within Their Target Cells

open access: yesViruses, 2019
Prions are infectious β-sheet-rich protein aggregates composed of misfolded prion protein (PrPSc) that do not possess coding nucleic acid. Prions replicate by recruiting and converting normal cellular PrPC into infectious isoforms.
Ina M. Vorberg
doaj   +1 more source

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

The Phenotypic Spectrum of Sporadic Creutzfeldt‐Jakob Disease Cortical Subtype

open access: yesAnnals of Neurology, Volume 99, Issue 4, Page 883-896, April 2026.
Objective The objective of this study was to characterize the phenotypic spectrum of the rare sporadic Creutzfeldt‐Jakob disease cortical subtype (sCJDMM/MV2C) in a large multicentric autopsy cohort. Methods We evaluated clinical histories, biofluid markers, brain diffusion‐weighted (DW)‐magnetic resonance imaging (MRI), and electroencephalogram (EEG ...
Simone Baiardi   +16 more
wiley   +1 more source

Prion propagation in vitro: are we there yet?

open access: yesInternational Journal of Medical Sciences, 2008
Prion diseases are caused by proteinaceous pathogens termed prions. Although the details of the mechanism of prion propagation are not fully understood, conformational conversion of cellular prion protein (PrPC) to misfolded, disease-associated scrapie ...
Chongsuk Ryou, Charles E. Mays
doaj  

Human Brain Contusions Contain Pathogenic Transmissible Species that Induce Progressive Cognitive Decline and Tau Pathology in Mice

open access: yesAnnals of Neurology, Volume 99, Issue 4, Page 897-911, April 2026.
Objective Traumatic brain injury (TBI) is an established risk factor for dementia, although the underlying mechanisms remain unclear. Our previous research demonstrated that a single severe TBI in wild‐type (WT) mice induces a prion‐like form of tau (tauTBI) that spreads throughout the brain, leading to memory deficits.
Gloria Vegliante   +19 more
wiley   +1 more source

Protein-lipid interactions and protein anchoring modulate the modes of association of the globular domain of the Prion protein and Doppel protein to model membrane patches

open access: yesFrontiers in Bioinformatics
The Prion protein is the molecular hallmark of the incurable prion diseases affecting mammals, including humans. The protein-only hypothesis states that the misfolding, accumulation, and deposition of the Prion protein play a critical role in toxicity ...
Patricia Soto   +7 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

Liquid–Liquid Phase Separation in Viral Infection and Immunology

open access: yesMedComm, Volume 7, Issue 4, April 2026.
LLPS organizes viral replication and antiviral immunity. Viruses hijack LLPS to form replication factories and evade immune sensors, while hosts assemble LLPS‐driven signaling hubs (e.g., MAVS, RIG‐I, and SGs) to amplify interferon responses. Targeting these condensate interfaces offers novel therapeutic strategies against infectious diseases ...
Jiuzhi Xu   +5 more
wiley   +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

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