Results 71 to 80 of about 73,750 (253)
Frontiers in Aging Neuroscience, 2018 Prion diseases are fatal neurological disorders affecting various mammalian species including humans. Lack of proper diagnostic tools and non-availability of therapeutic remedies are hindering the control strategies for prion diseases. MicroRNAs (miRNAs)
Syed Zahid Ali Shah +4 more
doaj +1 more source
Loss of PIKfyve drives the spongiform degeneration in prion diseases
EMBO Molecular Medicine, 2021 Brain‐matter vacuolation is a defining trait of all prion diseases, yet its cause is unknown. Here, we report that prion infection and prion‐mimetic antibodies deplete the phosphoinositide kinase PIKfyve—which controls endolysosomal maturation—from mouse
Asvin K K Lakkaraju +6 more
doaj +1 more source
Glycosylphosphatidylinositols: More than just an anchor? [PDF]
, 2016 There is increasing interest in the role of glycosylphosphatidylinositol (GPI) anchors that attach some proteins to cell membranes. Far from being biologically inert, GPIs influence the targeting, intracellular trafficking and function of the attached ...
Bate, C, Nolan, W, Williams, A
core +1 more source
Sensing and Filtering Environmental Fluctuations: The Case of Biomolecular Condensates in Plants
Advanced Science, EarlyView.The diversity of plant condensates reflects constraints of sessile organisms to coordinate postembryonic development with environmental adaptation. This review examines how plants employ condensates to integrate temperature, light, redox, and nutrient signals.
Panagiotis N. Moschou, Dorothee Staiger
wiley +1 more source
Evidence for Oxidative Stress in Experimental Prion Disease
Neurobiology of Disease, 2000 Oxidative stress has been shown to be important in several neurodegenerative disorders. Previous in vitro studies have already demonstrated the ability of a prion protein fragment to induce oxidative stress in cultured cells.
Marin Guentchev +4 more
doaj +1 more source
Veterinary Research, 2021 Prion diseases are transmissible spongiform encephalopathies induced by the abnormally-folded prion protein (PrPSc), which is derived from the normal prion protein (PrPC).
Yong-Chan Kim +3 more
doaj +1 more source
Heterologous prion-forming proteins interact to cross-seed aggregation in Saccharomyces cerevisiae [PDF]
, 2017 The early stages of protein misfolding remain incompletely understood, as most mammalian proteinopathies are only detected after irreversible protein aggregates have formed.
Keefer, Kathryn M +2 more
core +2 more sources
Advanced Science, EarlyView.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
Acta Neuropathologica CommunicationsCultured brain slices rapidly replicate murine prions, exhibit prion pathology, and are amenable towards drug discovery, but have not been infected with human prions.
Jessy A. Slota +9 more
doaj +1 more source
Targeted Mutagenesis of the Oligopeptide Repeat Domain of the Yeast Prion Sup35 [PDF]
, 2014 The formation of prions in the baker’s yeast Saccharomyces cerevisiae is determined by amino acid composition rather than the primary sequence of amino acids.
Davis, Emily, Knox, James D.
core +1 more source