Results 1 to 10 of about 16,731 (246)

Large-scale lipidomic profiling identifies novel potential biomarkers for prion diseases and highlights lipid raft-related pathways [PDF]

open access: yesVeterinary Research, 2021
Prion diseases are transmissible spongiform encephalopathies induced by the abnormally-folded prion protein (PrPSc), which is derived from the normal prion protein (PrPC).
Yong-Chan Kim   +3 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

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, Grazia M.   +3 more
openaire   +4 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

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

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

Interaction networks of prion, prionogenic and prion-like proteins in budding yeast, and their role in gene regulation. [PDF]

open access: yesPLoS ONE, 2014
Prions are transmissible, propagating alternative states of proteins. Prions in budding yeast propagate heritable phenotypes and can function in large-scale gene regulation, or in some cases occur as diseases of yeast.
Djamel Harbi, Paul M Harrison
doaj   +1 more source

ALK1 controls hepatic vessel formation, angiodiversity, and angiocrine functions in hereditary hemorrhagic telangiectasia of the liver

open access: yesHepatology, EarlyView., 2022
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

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