Results 21 to 30 of about 3,400,014 (272)
Morphine Withdrawal Modifies Prion Protein Expression in Rat Hippocampus. [PDF]
The hippocampus is a vulnerable brain structure susceptible to damage during aging and chronic stress. Repeated exposure to opioids may alter the brain so that it functions normally when the drugs are present, thus, a prolonged withdrawal might lead to ...
Vincenzo Mattei +9 more
doaj +1 more source
Organotypic cerebellar slices represent a suitable model for characterizing and manipulating prion replication in complex cell environments. Organotypic slices recapitulate prion pathology and are amenable to drug testing in the absence of a blood-brain ...
Hanna eWolf +7 more
doaj +1 more source
Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding [PDF]
Transmissible spongiform encephalopathies, or prion diseases, are caused by misfolding and aggregation of the prion protein PrP. These diseases can be hereditary in humans and four of the many disease-associated missense mutants of PrP are in the ...
Valerie Daggett +3 more
core +1 more source
Hepatic endothelial Alk1 signaling protects from development of vascular malformations while maintaining organ‐specific endothelial differentiation and angiocrine portmanteau of the names Wingless and Int‐1 signaling. Abstract Background and Aims In hereditary hemorrhagic telangiectasia (HHT), severe liver vascular malformations are associated with ...
Christian David Schmid +20 more
wiley +1 more source
Molecular dynamics as an approach to study prion protein misfolding and the effect of pathogenic mutations [PDF]
Computer simulation of protein dynamics offers unique high-resolution information that complements experiment. Using experimentally derived structures of the natively folded prion protein (PrP), physically realistic dynamics and conformational changes ...
Valerie Daggett +3 more
core +1 more source
Prions are known to cause transmissible spongiform encephalopathies (TSE) after accumulation in the central nervous system. There is increasing evidence that prions are also present in body fluids and that prion infection by blood transmission is possible.
Franscini, Nicola +8 more
openaire +6 more sources
Prion protein glycosylation [PDF]
AbstractThe transmissible spongiform encephalopathies (TSE), or prion diseases are a group of transmissible neurodegenerative disorders of humans and animals. Although the infectious agent (the ‘prion’) has not yet been formally defined at the molecular level, much evidence exists to suggest that the major or sole component is an abnormal isoform of ...
Lawson, Victoria A +3 more
openaire +3 more sources
A Sequence-Dependent DNA Condensation Induced by Prion Protein
Different studies indicated that the prion protein induces hybridization of complementary DNA strands. Cell culture studies showed that the scrapie isoform of prion protein remained bound with the chromosome. In present work, we used an oxazole dye, YOYO,
Alakesh Bera, Sajal Biring
doaj +1 more source
A quantitative characterization of interaction between prion protein with nucleic acids
Binding of recombinant prion protein with small highly structured RNAs, prokaryotic and eukaryotic prion protein mRNA pseudoknots, tRNA and polyA has been studied by the change in fluorescence anisotropy of the intrinsic tryptophan groups of the protein.
Alakesh Bera, Sajal Biring
doaj +1 more source
Intraperitoneal Infection of Wild-Type Mice with Synthetically Generated Mammalian Prion. [PDF]
The prion hypothesis postulates that the infectious agent in transmissible spongiform encephalopathies (TSEs) is an unorthodox protein conformation based agent.
Xinhe Wang +6 more
doaj +1 more source

