Prion protein—Semisynthetic prion protein (PrP) variants with posttranslational modifications [PDF]
Journal of Peptide Science, 2019 Deciphering the pathophysiologic events in prion diseases is challenging, and the role of posttranslational modifications (PTMs) such as glypidation and glycosylation remains elusive due to the lack of homogeneous protein preparations. So far, experimental studies have been limited in directly analyzing the earliest events of the conformational change ...
Stefanie Hackl, Christian F.W. Becker
openaire +4 more sources
PLoS Biology, 2016 Protein misfolding is common across many neurodegenerative diseases, with misfolded proteins acting as seeds for "prion-like" conversion of normally folded protein to abnormal conformations.
James Alibhai +7 more
doaj +1 more source
Prion pathogenesis is unaltered in the absence of SIRPα-mediated "don't-eat-me" signaling. [PDF]
PLoS ONE, 2017 Prion diseases are neurodegenerative conditions caused by misfolding of the prion protein, leading to conspicuous neuronal loss and intense microgliosis.
Mario Nuvolone +6 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
Use of bovine recombinant prion protein and real-time quaking-induced conversion to detect cattle transmissible mink encephalopathy prions and discriminate classical and atypical L- and H-Type bovine spongiform encephalopathy. [PDF]
PLoS ONE, 2017 Prions are amyloid-forming proteins that cause transmissible spongiform encephalopathies through a process involving conversion from the normal cellular prion protein to the pathogenic misfolded conformation (PrPSc).
Soyoun Hwang +2 more
doaj +1 more source
On the statistical mechanics of prion diseases
, 2001 We simulate a two-dimensional, lattice based, protein-level statistical mechanical model for prion diseases (e.g., Mad Cow disease) with concommitant prion protein misfolding and aggregation.
A. Coghlan +25 more
core +1 more source
Synthesis and structural characterization of a mimetic membrane-anchored prion protein [PDF]
, 2006 During pathogenesis of transmissible spongiform encephalopathies (TSEs) an abnormal form (PrPSc) of the host encoded prion protein (PrPC) accumulates in insoluble fibrils and plaques. The two forms of PrP appear to have identical covalent structures, but
Andrew C. Gill +44 more
core +1 more source
PLoS ONE, 2006 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 +5 more sources
Journal of Integrative Neuroscience, 2019 The effects of cellular prion protein on rapid eye movement sleep deprivation-induced spatial memory impairment were investigated, and the related mechanisms explored.
Li Hu +5 more
doaj +1 more source
Prion protein in the cerebrospinal fluid of healthy and naturally scrapie-affected sheep [PDF]
, 2006 The aim of this study was to characterize the cerebrospinal fluid (CSF) prion protein (PrP) of healthy and naturally scrapie-affected sheep. The soluble form of CSF PrPC immunoblotted with an anti-octarepeat and an anti-C terminus mAb showed two isoforms
Andréoletti +24 more
core +3 more sources