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TranscriptomicsGene expression profile of a murin neuroblastoma cell line infected with the prion strain 22L
The underlying pathogenic mechanisms of prion infection are not well characterized. To study the effect of prion infection on gene expression in neuronal cell cultures, a neuroblastoma (N2a) cell clone was infected with either the mouse adapted prion strain 22L or exposed to uninfected brain homogen...
ORGANISM(S): Mus musculus 
2010-05-26 | E-GEOD-7119 | biostudies-arrayexpress
TranscriptomicsTranscription profiling of mouse brain infected with prions in eight mouse-prion strain combinations in a systems approach to the study of prion disease
Prions cause transmissible neurodegenerative diseases and replicate by conformational conversion of normal, benign forms of prion protein (PrPC) to disease-causing PrPSc isoforms. A systems approach to disease postulates that disease arises from the pathological perturbation (genetic and/or environm...
ORGANISM(S): Mus musculus 
2009-03-25 | E-MTAB-76 | biostudies-arrayexpress
TranscriptomicsPrion infected ScN2a and GT1
A comparison of prion infected and non-infected samples from neuroblastoma cells (N2a), and a comparison of prion infected and non-infected samples from hypothalmus cells (GT1). 11 dual-color DNA-chip hybridizations of cDNAs were made. Keywords: other
ORGANISM(S): Mus musculus 
2010-06-09 | E-GEOD-1803 | biostudies-arrayexpress
TranscriptomicsComprehensive transcriptional profiling of prion infection in mouse models reveals networks of responsive genes.
Prion infection results in progressive neurodegeneration of the central nervous system invariably resulting in death. The pathological effects of prion diseases in the brain are morphologically well defined, such as gliosis, vacuolation, and the accumulation of disease-specific protease-resistant p...
ORGANISM(S): Mus musculus 
2010-05-26 | E-GEOD-10310 | biostudies-arrayexpress
TranscriptomicsDevelopmental influence of the cellular prion protein on the gene expression profile in mouse hippocampus
A key event in the pathogenic process of prion diseases is the conversion of the cellular prion protein (PrPC) to an abnormal and protease-resistant isoform (PrPSc). Mice lacking PrP are resistant to prion infection, and down-regulation of PrPC during prion infection prevents neuronal loss and the p...
ORGANISM(S): Mus musculus 
2011-04-12 | E-GEOD-21718 | biostudies-arrayexpress
MetabolomicsThe effect of prions on cellular metabolism: The metabolic impact of the [RNQ+] prion and the native role of Rnq1p
Not available
ORGANISM(S): Saccharomyces cerevisiae 
ST002478 | MetabolomicsWorkbench
TranscriptomicsExpression data from C2C12 myotubes infected with RML prions
Prion infection in animals results in neurodegeneration and eventually death. To examine the cellular impact of Prion disease, we profiled non-proliferative fully differentiated C2C12 cells, which can replicate prions to high levels. Results suggest that accumulation of high levels of PrPSc in C2C12...
ORGANISM(S): Mus musculus 
2013-12-22 | E-GEOD-44563 | biostudies-arrayexpress
TranscriptomicsExpression data for inbred mouse brains
Prion diseases are fatal neurodegenerative disorders that include bovine spongiform encephalopathy (BSE) and scrapie in animals and Creutzfeldt-Jakob disease (CJD) in humans. They are characterized by long incubation periods, variation in which is determined by many factors including genetic backgro...
ORGANISM(S): Mus musculus 
2012-09-04 | E-GEOD-38205 | biostudies-arrayexpress
TranscriptomicsGenome-wide translational changes induced by the prion [PSI+]
Prions are infectious proteins that can adopt a structural conformation different from that of the normal protein. This change of conformation is then propagated among other molecules of the same protein. Prions are associated with neurodegenerative diseases in mammals, but are also found in fungi (...
ORGANISM(S): Saccharomyces cerevisiae 
2014-07-18 | E-GEOD-41590 | biostudies-arrayexpress
ProteomicsProteomic analysis of [PSI+] yeast strain
The yeast Sup35 protein is a subunit of the translation termination factor, and its conversion to the [PSI+] prion state leads to more translational read-through. Although extensive studies have been done on [PSI+], changes at the proteomic level have not been performed exhaustively. We therefore us...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2018-10-24 | PXD007168 | Pride
Yeast prion Proteomics Sup35 Mass spectrometry Silac Aneuploidy Amyloids 
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