Results 61 to 70 of about 56,806 (329)

A Review on the Salt Bridge Between ASP177 and ARG163 of Wild-Type Rabbit Prion Protein

open access: yes, 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
core   +2 more sources

ZNRD2 Mediated Nucleoprotein Aggregation Impairs Respiratory Syncytial Virus Replication

open access: yesAdvanced 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

The Way forward for the Origin of Life: Prions and Prion-Like Molecules First Hypothesis

open access: yesLife, 2021
In this paper the hypothesis that prions and prion-like molecules could have initiated the chemical evolutionary process which led to the eventual emergence of life is reappraised.
Sohan Jheeta   +3 more
doaj   +1 more source

Social Determinants of Health and Health‐Related Quality of Life: The Potential Mediating Role of Social Activities, Access to Medical Services, and Access to Social Services

open access: yesAustralian Journal of Social Issues, EarlyView.
ABSTRACT This study explored the mediating influences of access to social activities, social services, and health and medical services on the relationship between social determinants of health and health‐related quality of life. A survey of 602 adults was conducted in a regional area of Australia.
Candice Oster   +4 more
wiley   +1 more source

Artificial strain of human prions created in vitro

open access: yesNature Communications, 2018
Synthetic prions have previously been generated from recombinant rodent PrP. Here the authors generate synthetic human prions, by seeding human PrP with CJD prions, and characterize its infectivity in mice.
Chae Kim   +11 more
doaj   +1 more source

The Molecular Pathology of Prion Diseases [PDF]

open access: yes, 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
core  

Cellular Prion Protein Mediates Toxic Signaling of Amyloid Beta [PDF]

open access: yes, 2011
Prion diseases in humans and animals comprise a group of invariably fatal neurodegenerative diseases characterized by the formation of a pathogenic protein conformer designated PrPSc and infectious particles denoted prions.
Resenberger, Ulrike K.   +2 more
core   +1 more source

Construction of pathogenic Sec16a mutation mouse model using CRISPR/Cas9

open access: yesAnimal 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

Rational design of structure‐based vaccines targeting misfolded alpha‐synuclein conformers of Parkinson's disease and related disorders

open access: yesBioengineering & Translational Medicine
Synucleinopathies, including Parkinson's disease (PD), multiple system atrophy (MSA), and dementia with Lewy bodies (DLB), are neurodegenerative disorders caused by the accumulation of misfolded alpha‐synuclein protein.
Jose Miguel Flores‐Fernandez   +13 more
doaj   +1 more source

Conformational diversity in purified prions produced in vitro.

open access: yesPLoS Pathogens, 2023
Prion diseases are caused by misfolding of either wild-type or mutant forms of the prion protein (PrP) into self-propagating, pathogenic conformers, collectively termed PrPSc.
Daniel J Walsh   +3 more
doaj   +1 more source

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