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PrionHome: a database of prions and other sequences relevant to prion phenomena.

open access: yesPLoS ONE, 2012
Prions are units of propagation of an altered state of a protein or proteins; prions can propagate from organism to organism, through cooption of other protein copies.
Djamel Harbi   +7 more
doaj   +4 more sources

Creutzfeldt-Jakob Disease Incidence, South Korea, 2001–2019

open access: yesEmerging Infectious Diseases, 2022
We found increasing trends of Creutzfeldt-Jakob disease (CJD) cases and annual incidence in South Korea during 2001–2019. We noted relatively low (5.7%) distribution of familial CJD.
Yong-Chan Kim, Byung-Hoon Jeong
doaj   +1 more source

Immunomodulation for prion and prion-related diseases [PDF]

open access: yesExpert Review of Vaccines, 2010
Prion diseases are a unique category of illness, affecting both animals and humans, where the underlying pathogenesis is related to a conformational change of a normal self protein called cellular prion protein to a pathological and infectious conformer known as scrapie prion protein (PrP(Sc)). Currently, all prion diseases lack effective treatment and
Thomas, Wisniewski, Fernando, Goñi
openaire   +2 more sources

Human J-Domain Protein DnaJB6 Protects Yeast from [PSI+] Prion Toxicity

open access: yesBiology, 2022
Human J-domain protein (JDP) DnaJB6 has a broad and potent activity that prevents formation of amyloid by polypeptides such as polyglutamine, A-beta, and alpha-synuclein, related to Huntington’s, Alzheimer’s, and Parkinson’s diseases, respectively.
Richard E. Dolder   +3 more
doaj   +1 more source

Nanoimaging for prion related diseases [PDF]

open access: yesPrion, 2010
Misfolding and aggregation of prion proteins is linked to a number of neurodegenerative disorders such as Creutzfeldt-Jacob disease (CJD) and its variants: Kuru, Gerstmann-Straussler-Scheinker syndrome and fatal familial insomnia. In prion diseases, infectious particles are proteins that propagate by transmitting a misfolded state of a protein, leading
Alexey V, Krasnoslobodtsev   +4 more
openaire   +2 more sources

Uptake, Retention, and Excretion of Infectious Prions by Experimentally Exposed Earthworms

open access: yesEmerging Infectious Diseases, 2021
Prions are proteinaceous infectious agents that can be transmitted through various components of the environment, including soil particles. We found that earthworms exposed to prion-contaminated soil can bind, retain, and excrete prions, which remain ...
Sandra Pritzkow   +3 more
doaj   +1 more source

Saccharomyces cerevisiae in neuroscience: how unicellular organism helps to better understand prion protein?

open access: yesNeural Regeneration Research, 2021
The baker’s yeast Saccharomyces (S.) cerevisiae is a single-celled eukaryotic model organism widely used in research on life sciences. Being a unicellular organism, S. cerevisiae has some evident limitations in application to neuroscience. However, yeast
Takao Ishikawa
doaj   +1 more source

THERPA: A small molecule database related to prion protein regulation and prion diseases progression [PDF]

open access: yesPrion, 2018
Prion diseases are fatal neurodegenerative disorders that affect humans and animals. Although various small molecules have been evaluated for application in the treatment of prion diseases, none have been shown to be efficacious. Expanding our knowledge of these molecules is important for understanding of the complex mechanisms of prion diseases.
Sol Moe Lee   +6 more
openaire   +2 more sources

Identification of Prion Disease-Related Somatic Mutations in the Prion Protein Gene (PRNP) in Cancer Patients [PDF]

open access: yesCells, 2020
Prion diseases are caused by misfolded prion protein (PrPSc) and are accompanied by spongiform vacuolation of brain lesions. Approximately three centuries have passed since prion diseases were first discovered around the world; however, the exact role of certain factors affecting the causative agent of prion diseases is still debatable.
Yong-Chan Kim   +2 more
openaire   +3 more sources

Stability and Cu(II) Binding of Prion Protein Variants Related to Inherited Human Prion Diseases [PDF]

open access: yesBiophysical Journal, 2003
All inherited forms of human prion diseases are linked with mutations in the prion protein (PrP) gene. Here we have investigated the stability and Cu(II) binding properties of three recombinant variants of murine full-length PrP(23-231)-containing destabilizing point mutations that are associated with human Gerstmann-Sträussler-Scheinker disease (F198S)
Cereghetti GM   +3 more
openaire   +5 more sources

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