Results 91 to 100 of about 5,269,629 (202)
Prediction of Prion Proteins in E. coli Based on Bimodal Sequence Characteristics
Proteins: Structure, Function, and Bioinformatics, EarlyView.ABSTRACT Prions are infectious proteins that bear misfolded conformations capable of converting folded states into misfolded aggregates under physiologically relevant conditions. In mammals, prions cause deadly maladies including Creutzfeldt‐Jakob and chronic wasting disease. To date, several prion proteins have been identified in eukaryotes, primarily
Katherine Shreeve +5 more
wiley +1 more source
Dissection and design of yeast prions. [PDF]
, 2004 Many proteins can misfold into beta-sheet-rich, self-seeding polymers (amyloids). Prions are exceptional among such aggregates in that they are also infectious.
Cox Brian S +15 more
core +2 more sources
, 2012 Creutzfeldt-Jakob disease (CJD) can be iatrogenically transmitted during transplants, grafts and transfusions from CJD infected donors and also contaminated surgical instruments.
Secker, Thomas
core +1 more source
Journal of Animal Ecology, EarlyView.This paper estimates the rate of chronic wasting disease spread in multiple regions and compares these rates with model predictions based on deer movement data. Abstract Rare long‐distance movements can increase the spatial spread of invasive species and shifts in species ranges. For wildlife disease spread, however, seasonal migrations may only matter
Paul C. Cross +3 more
wiley +1 more source
A novel, resistance-linked ovine PrP variant and its equivalent mouse variant modulate the in vitro cell-free conversion of rPrP to PrPres [PDF]
, 2006 Prion diseases are associated with the conversion of the normal cellular prion protein, PrPC, to the abnormal, disease-associated form, PrPSc. This conversion can be mimicked in vitro by using a cell-free conversion assay. It has recently been shown that
Kirby, Louise +4 more
core +1 more source
Brain Pathology, EarlyView.Beta amyloid diffuse plaques, neurofibrillary tangles and neuritic plaques, are increased in densities at the intermediate stage of Alzheimer's neuropathological change. These pathological changes releasing Pathogen‐Associated Molecular Patterns (PAMPs) and Damage‐Associated Molecular Patterns (DAMPs).
Juan Pablo de Rivero Vaccari +10 more
wiley +1 more source
Evidence for retrogene origins of the prion gene family.
PLoS ONE, 2011 The evolutionary origin of prion genes, only known to exist in the vertebrate lineage, had remained elusive until recently. Following a lead from interactome investigations of the murine prion protein, our previous bioinformatic analyses revealed the ...
Sepehr Ehsani +5 more
doaj +1 more source
Brain Pathology, EarlyView.Using the Infinium MethylationEPIC v2.0 array and Heidelberg Brain Tumor Classifier v12.8, 24 international laboratories achieved highly reproducible CNS tumor classification (97.9% correct; median β‐correlation r = 0.99), while copy number variation interpretation showed substantial interlaboratory variability, highlighting the need for harmonized CNV
Katrin Mauch‐Mücke +50 more
wiley +1 more source
α‐Synuclein strain homogeneity in multiple system atrophy subtypes
Brain Pathology, EarlyView.Two different subtypes of multiple system atrophy are recognized: MSA‐C and MSA‐P. In this manuscript, Lau et al. investigate whether MSA‐C and MSA‐P are caused by different strains of α‐synuclein aggregates. By performing conformational fingerprinting experiments as well as in vitro and in vivo seeding assays, their findings suggest that both MSA‐C ...
Heather H. C. Lau +10 more
wiley +1 more source
The Molecular Pathology of Prion Diseases [PDF]
, 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 ...
Vassallo, Neville +2 more
core