Results 41 to 50 of about 7,097 (179)
TDP‐43 Aggregation: The Healthy‐Toxic Balance of the Prion‐Like Domain
Advanced Science, Volume 13, Issue 40, 17 July 2026.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
Rapid generation of prion disease models using AAV‐delivered PrP variants in knockout mice
Brain Pathology, Volume 36, Issue 4, July 2026.We developed a rapid AAV‐based system to generate prion disease models in weeks rather than months. Following systemic AAV9P31 delivery of modified PrP to knockout mice, we achieved brain‐wide expression and successful propagation of both classical (RML) and atypical (GSS‐A117V) prion strains.
Maitena San‐Juan‐Ansoleaga +11 more
wiley +1 more source
Identifying Key Components of the PrPC-PrPSc Replicative Interface [PDF]
Journal of Biological Chemistry, 2008 In prion disease, direct interaction between the cellular prion protein (PrP(C)) and its misfolded disease-associated conformer PrP(Sc) is a crucial, although poorly understood step promoting the formation of nascent PrP(Sc) and prion infectivity. Recently, we hypothesized that three regions of PrP (corresponding to amino acid residues 23-33, 98-110 ...
Gil C, Abalos +7 more
openaire +2 more sources
Brain Pathology, Volume 36, Issue 4, July 2026.A single amino acid change (L108I) combined with PrP overexpression drives spontaneous atypical prion formation in mice, enabling also efficient propagation of diverse prion strains. This model allows studying how spontaneous prion diseases arise and provides powerful tools for investigating strain emergence, transmission barriers, and mechanisms ...
Hasier Eraña +20 more
wiley +1 more source
HaloTag Fusion Enables Dynamic Analysis of Prion Protein Biosynthesis, Turnover, and Misfolding
ChemBioChem, Volume 27, Issue 11, 15 June 2026.Prion protein (PrP) misfolding underlies fatal neurodegenerative diseases. We developed a HaloTag‐based PrP fusion enabling spatiotemporal labeling of distinct PrP populations in living cells. This system recapitulates native PrP biology, reveals early misfolding events in disease‐associated mutants, and allows mechanistic interrogation of PrP‐lowering
Antonio Masone +2 more
wiley +1 more source
Advanced NanoBiomed Research, Volume 6, Issue 6, June 2026.Using a 3D cell culture model of the fibrotic barrier in pancreatic cancer, this work shows that inhibiting NUAK2 kinase in pancreatic stellate cells enhances macromolecular drug delivery. Mechanistically, NUAK2 inhibition disrupted actin stress fiber assembly to downregulate collagen I expression, thus enhancing macromolecular permeability.
Misaki Nakamura +14 more
wiley +1 more source
PAD-Beads enrichment enhances detection of PrPSc using real-time quaking-induced conversion
BMC Research Notes, 2019 Objective Scrapie is a transmissible spongiform encephalopathy (TSE) that naturally occurs in sheep and goats. This fatal neurodegenerative disease results from misfolding of the normal cellular prion protein (PrPC) to a pathogenic prion protein form ...
Soyoun Hwang +2 more
doaj +1 more source
Relationship between magnetism and prion protein
Journal of Biological Research, 2010 The mechanism of conversion of the normal prion protein (PrPC) into aggregates of its pathological conformer (PrPSc) reamins unclear. The aim of this study was to evaluate the effects induced by exposure of biological samples containing PrPSC to a ...
F. Balzano +5 more
doaj +1 more source
European Journal of Histochemistry, 2021 Sporadic Creutzfeldt-Jakob disease (sCJD) is a rare and fatal neurodegenerative disorder with an incidence of 1.5 to 2 cases per million population/year. The disease is caused by a proteinaceous infectious agent, named prion (or PrPSc), which arises from
Federico Angelo Cazzaniga +6 more
doaj +1 more source
CNS Neuroscience &Therapeutics, Volume 32, Issue 6, June 2026.NBP counteracts PrP106‐126‐induced neurotoxicity by activating NRF2 and restoring OPA1/DRP1‐mediated mitochondrial dynamics. It suppresses oxidative stress and preserves mitochondrial function and bioenergetics. These actions support NBP as a promising therapeutic candidate for prion‐related neurodegeneration.
Wei Wu +3 more
wiley +1 more source