Results 61 to 70 of about 1,553,593 (211)
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
Proteína prion celular (PrPc) altera a suscetibilidade ao etanol através da modulação do sistema dopaminérgico [PDF]
, 2013 Tese (doutorado) - Universidade Federal de Santa Catarina, Centro de Ciências Biológicas, Programa de Pós-Graduação em FarmacologiaO consumo de drogas com potencial aditivo, como o etanol, induz alterações sinápticas profundas na via mesocorticolímbica ...
Rial, Daniel
core
The interaktion of the cellular prion protein (PrPc) with relevant proteins of Alzheimer's disease
, 2014 Previous studies indicate an important role for the cellular prion Protein (PrPc) in the development of Alzheimer's disease pathology. In the present study the interaction of PrPc with Alzheimer relevant proteins such as APP, BACE, tau and phosphorylated
Maibach-Wulf, Katharina
core +1 more source
Trapping Prion Protein in the Endoplasmic Reticulum Impairs PrPC Maturation and Prevents PrPSc Accumulation [PDF]
Journal of Biological Chemistry, 2005 The conversion of the normal cellular prion protein (PrP(C)) into the abnormal scrapie isoform (PrP(Sc)) is a key feature of prion diseases. The pathogenic mechanisms and the subcellular sites of the conversion are complex and not completely understood.
Cardinale, A +5 more
openaire +4 more sources
Frontiers in Cellular Neuroscience, 2016 The cellular prion protein (PrPc) and hypoxia appear to be tightly intertwined. Beneficial effects of PrPc on neuronal survival under hypoxic conditions such as focal cerebral ischemia are strongly supported.
Sanja Ramljak, Holger Herlyn, Inga Zerr
doaj +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
The Molecular Pathology of Prion Diseases [PDF]
, 2004 Prion diseases, or transmissible spongiform encephalopathies (TSEs), are a group of invariably fatal neurodegenerative disorders. Uniquely, they may present as sporadic, inherited, or infectious forms, all of which involve conversion of the normal ...
Vassallo, Neville +2 more
core
, 2004 Solvation energy calculation is one of the main difficulties for the estimation of protein-ligand binding free energy and the correct scoring in docking studies.
Zhou, JJ, Wang, Q, Pei, JF, Lai, LH
core +1 more source
Journal of Neuroinflammation, 2017 Background The cellular prion protein (PrPC) is an evolutionary conserved protein abundantly expressed not only in the central nervous system but also peripherally including the immune system.
Ø. Salvesen +5 more
doaj +1 more source
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