Results 71 to 80 of about 57,548 (261)
PrPSc-like prion protein peptide inhibits the function of cellular prion protein [PDF]
Biochemical Journal, 2000 Mice lacking expression of the prion protein are protected against infection with prion disease. Neurodegeneration in prion disease requires the formation of the abnormal isoform of the prion protein (PrPSc) from host prion protein. Therefore expression of normal host prion protein is necessary for prion disease.
openaire +2 more sources
Advanced Science, EarlyView.Astrocytic TIA1‐mediated stress granules (SGs) promote demyelination by sequestering the mRNA of cholesterol synthesis genes. In this model, astrocytic TIA1‐mediated SGs were increased in the optic nerves of EAE mice, leading to the downregulation of cholesterol synthesis genes such as HMGCS1 through sequestration of their mRNA into SGs, which ...
Zheyu Fang +11 more
wiley +1 more source
The cellular prion protein counteracts cardiac oxidative stress [PDF]
Cardiovascular Research, 2014 The cellular prion protein, PrP(C), whose aberrant isoforms are related to prion diseases of humans and animals, has a still obscure physiological function. Having observed an increased expression of PrP(C) in two in vivo paradigms of heart remodelling, we focused on isolated mouse hearts to ascertain the capacity of PrP(C) to antagonize oxidative ...
ZANETTI, FILIPPO +10 more
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Construction of pathogenic Sec16a mutation mouse model using CRISPR/Cas9
Animal Models and Experimental Medicine, EarlyView.Yaqiang Hu et al. engineered a pathogenic Sec16a mutant mouse model using CRISPR/Cas9 technology. They observed that the Sec16a mutant mice displayed diminished learning and memory capabilities, along with a limb‐clasping phenotype upon tail suspension.
Yaqiang Hu +6 more
wiley +1 more source
Equine models in translational medicine: A comparative approach to human health
Animal Models and Experimental Medicine, EarlyView.This diagram summarizes and contrasts rodent and equine models, outlining their strengths, limitations, and applications. Horses offer naturally occurring diseases, genetic and physiological similarities to humans, and suitability for longitudinal and clinical‐scale studies.
Shayan Boozarjomehri Amnieh +1 more
wiley +1 more source
Sequence features governing aggregation or degradation of prion-like proteins. [PDF]
PLoS Genetics, 2018 Enhanced protein aggregation and/or impaired clearance of aggregates can lead to neurodegenerative disorders such as Alzheimer's Disease, Huntington's Disease, and prion diseases.
Sean M Cascarina +3 more
doaj +1 more source
A Review on the Salt Bridge Between ASP177 and ARG163 of Wild-Type Rabbit Prion Protein
, 2015 Prion diseases are invariably fatal and highly infectious neurodegenerative diseases that affect a wide variety of mammalian species such as sheep and goats, cattle, deer, elks, humans and mice etc., but rabbits have a low susceptibility to be infected ...
Wang, Feng, Zhang, Jiapu
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Genetic Factors Contributing to the Susceptibility of Development of Prion Diseases [PDF]
, 2017 This paper won an honorable mention writing flag award in the research category. Claire Culbertson, writing for Katherine Bruner’s BIO 325L class, “Lab Experience in Genetics”.Bruner, KatherineUndergraduate ...
Culbertson, Claire
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Cystatin F is a biomarker of prion pathogenesis in mice.
PLoS ONE, 2017 Misfolding of the cellular prion protein (PrPC) into the scrapie prion protein (PrPSc) results in progressive, fatal, transmissible neurodegenerative conditions termed prion diseases.
Mario Nuvolone +17 more
doaj +1 more source
Prion protein modulates cellular iron uptake: a novel function with implications for prion disease pathogenesis. [PDF]
PLoS ONE, 2009 Converging evidence leaves little doubt that a change in the conformation of prion protein (PrP(C)) from a mainly alpha-helical to a beta-sheet rich PrP-scrapie (PrP(Sc)) form is the main event responsible for prion disease associated neurotoxicity ...
Ajay Singh +6 more
doaj +1 more source