Results 101 to 110 of about 5,604,422 (355)
Cell Communication and Signaling, 2020 Background The distinctive molecular structure of the prion protein, PrPsc, is established only in mammals with infectious prion diseases. Prion protein characterizes either the transmissible pathogen itself or a primary constituent of the disease.
Ji-Hong Moon, Sang-Youel Park
doaj +1 more source
The LBFGS Quasi-Newtonian Method for Molecular Modeling Prion AGAAAAGA Amyloid Fibrils [PDF]
, 2012 Experimental X-ray crystallography, NMR (Nuclear Magnetic Resonance) spectroscopy, dual polarization interferometry, etc are indeed very powerful tools to determine the 3-Dimensional structure of a protein (including the membrane protein); theoretical ...
Hou, Yating +4 more
core +3 more sources
Journal of Biological Chemistry, 2014 Background: The structures of infectious mammalian prions remain unclear. Results: Based in part on NMR data, we developed models with single PrP molecules spanning the entire cross-section of prion fibrils.
B. Groveman +5 more
semanticscholar +1 more source
To develop with or without the prion protein [PDF]
Frontiers in Cell and Developmental Biology, 2014 The deletion of the cellular form of the prion protein (PrP(C)) in mouse, goat, and cattle has no drastic phenotypic consequence. This stands in apparent contradiction with PrP(C) quasi-ubiquitous expression and conserved primary and tertiary structures in mammals, and its pivotal role in neurodegenerative diseases such as prion and Alzheimer's ...
Bruno Passet +10 more
openaire +6 more sources
Advanced Science, EarlyView.SeNSs provide a biocompatible, anti‐inflammatory UC therapy. SeNSs form protein coronas enriched with AKT/PI3K/NF‐κB pathway proteins, suppress GP130 via hydrophobic interactions, and inhibit pro‐inflammatory cytokines. In DSS‐induced UC mice, SeNSs reduce inflammation, tissue damage, and disease activity by modulating cytokine, chemokine, and ...
Dingyi Shen +5 more
wiley +1 more source
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
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The Neutral Sphingomyelinase Pathway Regulates Packaging of the Prion Protein into Exosomes*
Journal of Biological Chemistry, 2014 Background: Exosomes are a novel mechanism of intercellular transmission of infectious prions. Results: Chemical and RNAi inhibition of the neutral sphingomyelinase (nSMase) pathway impairs exosome formation and prion packaging.
Belinda B. Guo, S. Bellingham, A. Hill
semanticscholar +1 more source
Prion protein in ESC regulation [PDF]
Prion, 2011 A large number of studies have analysed the putative functions of the prion protein (PrP(C)) in mammals. Although its sequence conservation over a wide range of different animals may indicate that this protein could have a key role in prion diseases, an absolutely accepted involvement has not been found so far.
Miranda Bedate, Alberto +3 more
openaire +6 more sources
Solving the Amyloid Paradox: Unveiling the Complex Pathogenicity of Amyloid Fibrils
Aggregate, EarlyView.This review addresses the gap between strong evidence for the involvement of amyloid fibrils in neurodegeneration and the failure of anti‐amyloid therapies, a phenomenon herein termed the “amyloid paradox.” To address this paradox, we provide a comprehensive summary of the current understanding of fibrils' pathogenic properties and mechanisms ...
Maksim I. Sulatsky +3 more
wiley +1 more source
Prion propagation can occur in a prokaryote and requires the ClpB chaperone
eLife, 2014 Prions are self-propagating protein aggregates that are characteristically transmissible. In mammals, the PrP protein can form a prion that causes the fatal transmissible spongiform encephalopathies.
Andy H Yuan +3 more
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