Results 61 to 70 of about 33,090 (271)

First Report of Polymorphisms and Genetic Characteristics of Prion-like Protein Gene (PRND) in Cats

open access: yesAnimals
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

Spongiform encephalopathy in siblings with no evidence of protease-resistant prion protein or a mutation in the prion protein gene

open access: yesJournal of Neurology, 2013
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

Developing a Functional Polyelectrolyte Hybrid Layer Scaffold Coating and Evaluation of Its Performance for Interaction With Neural Cells

open access: yesAdvanced Materials Interfaces, EarlyView.
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

open access: yes, 2005
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]

open access: yes, 2009
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

A comprehensive phylogeny of mammalian PRNP gene reveals no influence of prion misfolding propensity on the evolution of this gene.

open access: yesPLoS Pathogens
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]

open access: yesMolecular Microbiology, 2003
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

open access: yesAdvanced Science, EarlyView.
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]

open access: yesJournal of Biological Chemistry, 1997
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

open access: yesAdvanced Science, EarlyView.
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

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