Defining the Protein Seeds of Neurodegeneration using Real-Time Quaking-Induced Conversion Assays
Biomolecules, 2020 Neurodegenerative diseases are characterized by the accumulation of disease-related misfolded proteins. It is now widely understood that the characteristic self-amplifying (i.e., seeding) capacity once only attributed to the prions of transmissible ...
Matteo Manca, Allison Kraus
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Molecular Nanobiotechnological Approaches for the Detection and Therapy of Prion Related Diseases [PDF]
Nano Biomedicine and Engineering, 2012 Prion diseases are associated with the accumulation in the brain of an abnormal, protease resistant isoform of a host encoded glycoprotein known as prion protein (PrP). Nanotechnology in combination with biotechniques promises a broad spectrum of highly innovative approaches for overcoming the challenges posed by the prions.
PK Praseetha +3 more
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Transmission Characteristics of Variably Protease-Sensitive Prionopathy
Emerging Infectious Diseases, 2014 Variably protease-sensitive prionopathy (VPSPr), a recently identified and seemingly sporadic human prion disease, is distinct from Creutzfeldt-Jakob disease (CJD) but shares features of Gerstmann-Sträussler-Scheinker disease (GSS).
Silvio Notari +11 more
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Emerging Infectious Diseases, 2021 Chronic wasting disease (CWD) is a fatal prion disease of cervids. We examined host range of CWD by oronasally inoculating Suffolk sheep with brain homogenate from a CWD-positive white-tailed deer.
Eric D. Cassmann +2 more
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Shortest known prion protein allele in highly BSE-susceptible lemurs [PDF]
, 2000 We describe the shortest prion protein allele known to date. Surprisingly, it is found as a polymorphism exactly in a species (prosimian lemurs) which seems highly susceptible to oral infection with BSE-derived prions. The truncation of the prion protein
Gilch, S. +2 more
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Insufficient hydrogen‐bond desolvation and prion‐related disease [PDF]
European Journal of Biochemistry, 2002 A structuring and eventual exclusion of water surrounding backbone hydrogen bonds takes place during protein folding as hydrophobic residues cluster around such bonds. Taken as an average over all hydrogen bonds, the extent of desolvation is nearly a constant of motion, as revealed by re‐examination of the longest all‐atom trajectory with explicit ...
openaire +2 more sources
THERPA v2: an update of a small molecule database related to prion protein regulation and prion disease progression [PDF]
Prion, 2019 Prion diseases are rare, rapidly progressive neurodegenerative disorders that affect mammalian species [1,2].
Sol Moe Lee +3 more
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Cross infection control measures and the treatment of patients at risk of Creutzfeldt Jakob disease in UK general dental practice [PDF]
, 2001 AIMS: To determine the suitability of key infection control measures currently employed in UK dental practice for delivery of dental care to patients at risk of prion diseases.
A Smith +22 more
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Emerging Infectious Diseases, 2017 In the United-Kingdom, ≈1 of 2,000 persons could be infected with variant Creutzfeldt-Jakob disease (vCJD). Therefore, risk of transmission of vCJD by medical procedures remains a major concern for public health authorities.
Jean Y. Douet +11 more
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Heterologous prion-forming proteins interact to cross-seed aggregation in Saccharomyces cerevisiae [PDF]
, 2017 The early stages of protein misfolding remain incompletely understood, as most mammalian proteinopathies are only detected after irreversible protein aggregates have formed.
Keefer, Kathryn M +2 more
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