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ProteomicsHuman prion disease iTRAQ
Human prion diseases are fatal neurodegenerative disorders characterized by neuronal damage in brain. Protein S-nitrosylation, the covalent adduction of a NO to cysteine, plays a role in human brain biology, and brain dysfunction is a prominent feature of pPrion disease, yet the direct brain targets...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080756 | MassIVE
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
ProteomicsHuman prion disease iTRAQ - Proteomic Analyses for the Global S-Nitrosylated Proteins in the Brain Tissues of Different Human Prion Diseases
Human prion diseases are fatal neurodegenerative disorders characterized by neuronal damage in brain. Protein S-nitrosylation, the covalent adduction of a NO to cysteine, plays a role in human brain biology, and brain dysfunction is a prominent feature of pPrion disease, yet the direct brain targets...
ORGANISM(S): Homo sapiens (Human) 
2015-10-01 | PXD002813 | Pride
S-nitrosylation Proteomic analysis Isobaric tags for relative and absolute quantitation Human prion diseases 
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
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
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
ProteomicsGPI-glycan structures of human Prion from a human brain
To determine glycosylphosphatidylinositol (GPI) structures of human prion proteins isolated from a human brain.
ORGANISM(S): Homo sapiens (Human) 
2020-04-22 | PXD017656 | Pride
Gpi Prion Gpi side-chain Brain Human 
ProteomicsGPI-glycan structures of human Prion from knock-in mice_LC-MSMS
To determine glycosylphosphatidylinositol (GPI) structures of human prion proteins isolated from knock-in mice those express human prion protein instead of mouse one.
ORGANISM(S): Mus musculus (Mouse) Homo sapiens (Human) 
2020-04-22 | PXD017655 | Pride
Gpi Prion Gpi side-chain Brain Knock-in mouse Human 
ProteomicsGPI-glycan structures of human Prion (M232R) from knock-in mice_LC-MSMS
To determine glycosylphosphatidylinositol (GPI) structures of human prion proteins with M232R mutation isolated from knock-in mice those express human prion protein instead of mouse one.
ORGANISM(S): Homo sapiens (Human) 
2023-03-08 | PXD037584 | Pride
Gpi Gpi side chain Prion Brain Knock-in mouse Human 
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