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

