Results 51 to 60 of about 78,455 (315)
The Molecular Pathology of Prion Diseases [PDF]
, 2004 Prion diseases, or transmissible spongiform encephalopathies (TSEs), are a group of invariably fatal neurodegenerative disorders. Uniquely, they may present as sporadic, inherited, or infectious forms, all of which involve conversion of the normal ...
Herms, Jochen +2 more
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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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Prion pathogenesis and secondary lymphoid organs (SLO): Tracking the SLO spread of prions to the brain [PDF]
, 2012 Prion diseases are subacute neurodegenerative diseases that affect humans and a range of domestic and free-ranging animal species. These diseases are characterized by the accumulation of PrP(Sc), an abnormally folded isoform of the cellular prion protein
Mabbott, N. A.
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Formation of Condition‐Dependent Alpha‐Synuclein Fibril Strain in Artificial Cerebrospinal Fluid
Advanced Science, EarlyView.α‐synuclein aggregation in artificial cerebrospinal fluid (aCSF) leads to a distinct conformation with an electron density pocket motif found in aggregates from PD and MSA patients. Such fibrils has low stability outside the reaction conditions, hinting about the influence of cerebrospinal fluid components not only on the formation, but also on the ...
Rūta Sniečkutė +7 more
wiley +1 more source
ZNRD2 Mediated Nucleoprotein Aggregation Impairs Respiratory Syncytial Virus Replication
Advanced Science, EarlyView.During RSV infection, nucleoprotein (N) forms RNA‐bound oligomers. The host protein ZNRD2 binds to these oligomers, promoting their transition into insoluble aggregates. These aggregates simultaneously sequester functional N to restrict viral production and disrupt chaperonin assembly quality control by interfering with ZNRD2's role as an adaptor ...
Haiwu Zhou +8 more
wiley +1 more source
An overview of human prion diseases
Virology Journal, 2011 Prion diseases are transmissible, progressive and invariably fatal neurodegenerative conditions associated with misfolding and aggregation of a host-encoded cellular prion protein, PrPC.
Imran Muhammad, Mahmood Saqib
doaj +1 more source
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
Neurobiology of DiseaseSporadic Creutzfeldt-Jakob disease (sCJD), the most common human prion disease, is thought to occur when the cellular prion protein (PrPC) spontaneously misfolds and assembles into prion fibrils, culminating in fatal neurodegeneration.
Emma Jones +18 more
doaj +1 more source
Are amyloids infectious? Prions and prion-like proteins: myths and facts [PDF]
, 2018 Transmissible Spongiform Encephalopathies (TSEs) or prion diseases are a group of fatal neurodegenerative disorders affecting mammals. Albeit their low incidence in humans, prion diseases are a subject of passionate research due to their unorthodox ...
Morales Loyola, Rodrigo
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Molecular dynamics as an approach to study prion protein misfolding and the effect of pathogenic mutations [PDF]
, 2011 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 ...
Daggett, Valerie, van der Kamp, Marc W
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