Results 61 to 70 of about 14,159 (251)

Distinct patterns of prion strain deposition and toxicity in a novel whole brain organotypic slice culture system

open access: yesScientific Reports
Prion diseases are fatal transmissible neurodegenerative diseases that affect many mammals, including humans, caused by the templated misfolding of the prion protein.
Hailey Pineau, Valerie L. Sim
doaj   +1 more source

Improving the Predictive Value of Prion Inactivation Validation Methods to Minimize the Risks of Iatrogenic Transmission With Medical Instruments

open access: yesFrontiers in Bioengineering and Biotechnology, 2020
Prions are pathogenic infectious agents responsible for fatal, incurable neurodegenerative diseases in animals and humans. Prions are composed exclusively of an aggregated and misfolded form (PrPSc) of the cellular prion protein (PrPC).
Mohammed Moudjou   +9 more
doaj   +1 more source

Detection of β-amyloid aggregates/plaques in 5xFAD mice by labelled native PLGA nanoparticles: implication in the diagnosis of Alzheimer’s disease

open access: yesJournal of Nanobiotechnology, 2023
Evidence suggests that increased level/aggregation of β-amyloid (Aβ) peptide, together with enhanced phosphorylation/aggregation of tau protein, play a critical role in the development of Alzheimer’s disease (AD), the leading cause of dementia in the ...
Karthivashan Govindarajan   +1 more
doaj   +1 more source

A Skull Bone Marrow‐to‐Brain Axis Links Osteoblastic Activity to Myeloid Cell Trafficking, Cerebral Blood Flow, and Cognition in Alzheimer's Progression

open access: yesAdvanced Science, EarlyView.
This study reveals that Alzheimer's disease–linked APP expression in bone‐forming cells drives skull bone marrow remodeling and alters its vascular connections to the brain. These changes disrupt immune cell trafficking, cerebral blood flow, and cognition. Targeting bone marrow macrophages restores brain function, highlighting a previously unrecognized
Lei Xiong   +6 more
wiley   +1 more source

Aptamer‐Targeted PrPC Drives Colorectal Cancer Metastasis via a LYN‐STAT3 Complex and Enables Liquid Biopsy Detection

open access: yesAdvanced Science, EarlyView.
The aptamer WHY‐3E identifies PrPC as a CRC driver. Stabilized by USP18, endocytosed PrPC forms a LYN/STAT3 complex, upregulating MSN transcription to promote metastasis. Crucially, WHY‐3E sensitively detects PrPC‐positive circulating exosomes, establishing a robust theoretical foundation for non‐invasive clinical diagnostics.
Chunlin Wang   +23 more
wiley   +1 more source

Native PLGA nanoparticles attenuate Aβ-seed induced tau aggregation under in vitro conditions: potential implication in Alzheimer’s disease pathology

open access: yesScientific Reports
Evidence suggests that beta-amyloid (Aβ)-induced phosphorylation/aggregation of tau protein plays a critical role in the degeneration of neurons and development of Alzheimer’s disease (AD), the most common cause of dementia affecting the elderly ...
Pallabi Sil Paul   +9 more
doaj   +1 more source

Prions And Prion Diseases

open access: yesAfrican Journal of Clinical and Experimental Microbiology, 2008
A prion is a small infectious particle, which resist inactivation by procedures that modify nucleic acids. Transmissible spongiform encephalopathies (TSEs also known as prion diseases) are a group of progressive conditions that affects the brain and nervous system of humans and animals and are transmitted by prions.
Obi, R K, Nwanebu, F C
openaire   +3 more sources

p300 Degradation by the p53‐SIAH1 Axis Relieves TBK1 Acetylation to Enhance Innate Antiviral Immunity

open access: yesAdvanced Science, EarlyView.
This study identifies p300 as the acetyltransferase that acetylates TBK1 and inhibits its phosphorylation. Activation of the p53‐SIAH1 axis by immune response downregulates p300 expression to sustain innate antiviral immunity. Conditional p300 knockout in alveolar epithelial cells in vivo promotes antiviral responses and suppresses virus replication ...
Huidi Yu   +6 more
wiley   +1 more source

Prions in Yeast [PDF]

open access: yesGenetics, 2012
AbstractThe concept of a prion as an infectious self-propagating protein isoform was initially proposed to explain certain mammalian diseases. It is now clear that yeast also has heritable elements transmitted via protein. Indeed, the “protein only” model of prion transmission was first proven using a yeast prion.
Susan W, Liebman, Yury O, Chernoff
openaire   +2 more sources

TDP‐43 Aggregation: The Healthy‐Toxic Balance of the Prion‐Like Domain

open access: yesAdvanced Science, EarlyView.
TDP‐43 function relies on a delicate balance between reversible phase‐separated states and irreversible aggregation. Under physiological conditions, TDP‐43 forms dynamic droplets and oligomers that support normal cellular functions. In pathological contexts, this balance shifts toward aberrant aggregation, leading to toxic species.
Luca Zangrando   +2 more
wiley   +1 more source

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