Results 61 to 70 of about 71,281 (314)

Helices 2 and 3 are the initiation sites in the PrPc -> PrPsc transition

open access: yes, 2012
It is established that prion protein is the sole causative agent in a number of diseases in humans and animals. However, the nature of conformational changes that the normal cellular form PrPC undergoes in the conversion process to a self-replicating ...
Chen, Jie, Thirumalai, Devarajan
core   +1 more source

A cationic tetrapyrrole inhibits toxic activities of the cellular prion protein [PDF]

open access: yes, 2016
Prion diseases are rare neurodegenerative conditions associated with the conformational conversion of the cellular prion protein (PrPC) into PrPSc, a self-replicating isoform (prion) that accumulates in the central nervous system of affected individuals.
Biasini, Emiliano   +16 more
core   +2 more sources

Stimulating the Release of Exosomes Increases the Intercellular Transfer of Prions*

open access: yesJournal of Biological Chemistry, 2016
Exosomes are small extracellular vesicles released by cells and play important roles in intercellular communication and pathogen transfer. Exosomes have been implicated in several neurodegenerative diseases, including prion disease and Alzheimer disease.
Belinda B. Guo, S. Bellingham, A. Hill
semanticscholar   +1 more source

Minimally Clinically Important Difference of the Clinical Assessment Scale in Autoimmune Encephalitis

open access: yesAnnals of Clinical and Translational Neurology, EarlyView.
ABSTRACT The Clinical Assessment Scale in Autoimmune Encephalitis (CASE) tracks disease severity in autoimmune encephalitis (AE), but no threshold for significant change exists. We aimed to determine the minimally clinically important difference (MCID) for CASE.
Yihui Goh   +8 more
wiley   +1 more source

Tracking and clarifying differential traits of classical- and atypical L-type bovine spongiform encephalopathy prions after transmission from cattle to cynomolgus monkeys.

open access: yesPLoS ONE, 2019
Classical- (C-) and atypical L-type bovine spongiform encephalopathy (BSE) prions cause different pathological phenotypes in cattle brains, and the disease-associated forms of each prion protein (PrPSc) has a dissimilar biochemical signature.
Ken'ichi Hagiwara   +9 more
doaj   +1 more source

The Structure of Human Prions: From Biology to Structural Models—Considerations and Pitfalls

open access: yesViruses, 2014
The Structure of Human Prions: From Biology to Structural Models — Considerations and ...
Claudia Y. Acevedo-Morantes   +1 more
doaj   +1 more source

Mitigation of prion infectivity and conversion capacity by a simulated natural process--repeated cycles of drying and wetting. [PDF]

open access: yesPLoS Pathogens, 2015
Prions enter the environment from infected hosts, bind to a wide range of soil and soil minerals, and remain highly infectious. Environmental sources of prions almost certainly contribute to the transmission of chronic wasting disease in cervids and ...
Qi Yuan   +4 more
doaj   +1 more source

Amyloidogenic Peptide Fragments Designed From Bacterial Collagen‐like Proteins Form Hydrogel

open access: yesAdvanced Functional Materials, EarlyView.
This study identified amyloidogenic sequence motifs in bacterial collagen‐like proteins and exploited these to design peptides that self‐assemble into β‐sheet fibers and form hydrogels. One hydrogel supported healthy fibroblast growth, showing promise for biocompatible materials. Our work demonstrates that bacterial sequences can be harnessed to create
Vamika Sagar   +5 more
wiley   +1 more source

Water and the Biology of Prions and Plaques [PDF]

open access: yes, 2007
This is an attempt to account for the insolubility and/or aggregation of prions and plaques in terms of a model of water consisting of an equilibrium between high density and low density microdomains.
Graham K. Steel, Phillippa M. Wiggins
core   +1 more source

Synthesis and structural characterization of a mimetic membrane-anchored prion protein [PDF]

open access: yes, 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

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