Results 61 to 70 of about 33,090 (271)
First Report of Polymorphisms and Genetic Characteristics of Prion-like Protein Gene (PRND) in Cats
Prion diseases are fatal neurodegenerative disorders caused by the misfolding of the normal cellular prion protein (PrPC) into its infectious isoform (PrPSc).
Min-Ju Jeong +2 more
doaj +1 more source
We discuss relevant aspects in two siblings with a neurodegenerative process of unclear aetiology who developed progressive dementia with global aphasia and hyperoral behaviour at the ages of 39 and 46 years and who died 6 and 5 years after disease onset.
Varges, Daniel. A. +13 more
openaire +4 more sources
Polyelectrolyte scaffold coatings modified with Cu and Fe3O4 nanoparticles regulate neural stem cell behavior in vitro. Increased Fe3O4 content enhances mitochondrial activity and neuronal differentiation, whereas higher Cu levels reduce cell viability.
Anna Grzeczkowicz +5 more
wiley +1 more source
The presence of valine at residue 129 in human prion protein accelerates amyloid formation
The polymorphism at residue 129 of the human PRNP gene modulates disease susceptibility and the clinicopathological phenotypes in human transmissible spongiform encephalopathies.
Tahiri-Alaoui, Abdessamad +13 more
core +1 more source
State-of-the-art review of goat TSE in the European Union, with special emphasis on PRNP genetics and epidemiology [PDF]
Scrapie is a fatal, neurodegenerative disease of sheep and goats. It is also the earliest known member in the family of diseases classified as transmissible spongiform encephalopathies (TSE) or prion diseases, which includes Creutzfeldt-Jakob disease in ...
Olivier Andreéoletti +54 more
core +1 more source
Prion diseases are invariably fatal neurodegenerative diseases that affect some mammalian species, including humans. These diseases are caused by the misfolding of the cellular prion protein (PrPC) into a pathologic isoform (PrPSc).
Cristina Sampedro-Torres-Quevedo +18 more
doaj +1 more source
Prion protein gene polymorphisms in Saccharomyces cerevisiae [PDF]
SummaryThe yeast Saccharomyces cerevisiae genome encodes several proteins that, in laboratory strains, can take up a stable, transmissible prion form. In each case, this requires the Asn/Gln‐rich prion‐forming domain (PrD) of the protein to be intact.
Resende, Catarina +4 more
openaire +3 more sources
Ecological Adaptation Mechanisms Underlying Successful Plant Reproduction
During floral induction, various environmental and endogenous signals converge to regulate the florigen protein, which is transported from leaves to the SAM to initiate flowering. Within the SAM, a complex network of receptor kinases and small peptides orchestrates floral development with high spatiotemporal precision.
Hang Zhao +8 more
wiley +1 more source
Prion Protein Aggregation Reverted by Low Temperature in Transfected Cells Carrying a Prion Protein Gene Mutation [PDF]
Prion diseases are characterized by the conversion of the normal cellular prion protein (PrPC), a glycoprotein that is anchored to the cell membrane by a glycosylphosphatidylinositol moiety, into an isoform that is protease-resistant (PrPres) and pathogenic.
SINGH N. +6 more
openaire +3 more sources
Redox‐Dependent Chaperoning of GBF1 Condensates Regulates Seed Germination in Arabidopsis
In dormant seeds (low ROS), GBF1 forms liquid condensates to repress the germination gene CathB3, and the chaperone GIP1 maintains condensate liquidity and repressive activity. Upon imbibition (high ROS), ROS oxidize GIP1 during germination, impairing its chaperone function.
Yunying Wang, Xiaofeng Fang
wiley +1 more source

