Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Skeletal-Muscle Glutamate-Ammonia Ligase as Potential Biomarker of Preclinical Prion Diseases

ABSTRACT: Skeletal-Muscle Glutamate-Ammonia Ligase as Potential Biomarker of Preclinical Prion Diseases

PROVIDER: PRJNA863860 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Similar Datasets

Skeletal-Muscle Glutamate-Ammonia Ligase as Potential Biomarker of Preclinical Prion Diseases

Project description:We provide here a comprehensive transcriptional profiling of murine blood, spleen and skeletal muscle and brain on eight different time points after intracerebral prion inoculation. Our findings provide a detailed time course of extra-neural, transcriptional changes during prion disease which we presume to be of immediate relevance for biomarker development. Data analysis scripts can be found on https://github.com/marusakod/RML_extraneural_organs.

2022-09-01 | GSE210128 | GEO

Cell-type specific translational changes in prion diseases

Project description:Identification of genome-wide translational changes during prion disease via cell-type specific ribosome profiling.

2020-09-29 | GSE149805 | GEO

Genome-wide transcriptomics identifies an early preclinical signature of prion infection

Project description:Genome-wide transcriptomics identifies an early preclinical signature of prion infection

| PRJNA604764 | ENA

Single-cell transcriptomics of mammalian prion diseases identifies dynamic gene signatures shared between species [mouse_scRNAseq]

Project description:Mammalian prion diseases are fatal and transmissible neurological conditions caused by the propagation of prions, self-replicating multimeric assemblies of misfolded forms of host cellular prion protein. Despite extensive studies investigating the changes in transcriptional profiles in prion diseases the mechanisms by which prion diseases induce cellular toxicity, including changes in gene expression profiles are yet to be fully characterized. Here, we took advantage of the recent developments in single-cell technologies and performed an unbiased whole-transcriptome single-nucleus transcriptomic analysis in prion disease.

2023-01-31 | GSE214375 | GEO

Single-cell transcriptomics of mammalian prion diseases identifies dynamic gene signatures shared between species [human_scRNAseq]

2023-01-31 | GSE214374 | GEO

Single-cell transcriptomics of mammalian prion diseases identifies dynamic gene signatures shared between species [human_bulkRNAseq]

2023-01-31 | GSE214373 | GEO

Genome-wide transcriptomics identifies an early preclinical signature of prion infection

Project description:We constructed a searchable genome-wide atlas of mRNA abundance, splicing and editing alterations during the course of disease in prion-inoculated mice.

2020-06-12 | GSE144738 | GEO

The Prion Protein (PrP) is involved in translation via RNA granule-like mRNPs, a connection which is impaired during neurodegenerative diseases

Project description:Cytoplasmic RNA granules have emerged as important elements of posttranscriptional and translational regulation. Stress, germinal and neuronal granules contain RNA-binding proteins capable of self-assembly due to prion-like domains. Hyperassembly mediated by these prion-like domains causes several neurodegenerative diseases. Here, we report a subset of the mammalian prion protein (PrP), also prone to self-assembly, propagation and to cause devastating diseases, is a component of naturally occurring messenger ribonucleoproteins (mRNPs) in adult mouse brains. Biomolecules co-purified with PrP revealed a multitude of diverse RNA granule associated proteins and mRNAs encoding members of the translation machinery, indicating a role in a specialized translation process. Importantly, PrP mutations linked to Creutzfeldt-Jakob disease (CJD) or fatal familial insomnia (FFI) severely impaired recovery of mRNPs from preclinical mice, possibly representing a very early pathological process. Thus, mutant PrP may cause dysfunction in RNA regulation, thereby joining the constantly expanding ranks of disease associated RNP granule proteins. The file Enrichment_analysis.xlsx contains mRNAs (FDR < 0.01) co-purified with PrP in both WT sample pools as identified by DESeq2 and the respective gene counts and log2 fold changes for CJD and FFI PrP:IP sample pools.

2015-11-01 | GSE57233 | GEO

Prions induce an early Arc response in the hippocampus of prion-infected mice

Project description:Synapse dysfunction and synaptic loss are a central feature of neurodegenerative disorders, including prion disease. The cellular prion protein (PrPC) binds prion, amyloid-β, tau, and α-synuclein oligomers, resulting in the activation of macromolecular complexes and signaling at the post-synapse, yet the initial signaling events are unclear. Here we used a transcriptomic approach focused on the early-stage, prion-infected hippocampus of male wild type mice, and identify immediate early genes, including the synaptic activity response gene, Arc/Arg3.1, as significantly upregulated. In a longitudinal study of the prion-infected hippocampus, Arc/Arg-3.1 protein increased, from early to terminal disease. Notably, metabotropic glutamate receptor levels (mGluR5 dimers) were markedly reduced over time, while phosphorylated AMPA receptors (pGluA1-S845) levels increased. Sporadic Creutzfeldt-Jakob disease (sCJD) post-mortem cortical samples also showed low levels of mGluR5 dimers. Together, these findings suggest that prions trigger a chronic Arc response, an increase in phosphorylated GluA1, and a reduction in mGluR5 receptors beginning in early disease.

2023-01-01 | GSE207251 | GEO

The Prion Protein (PrP) is involved in translation via RNA granule-like mRNPs, a connection which is impaired during neurodegenerative diseases

2015-11-01 | E-GEOD-57233 | biostudies-arrayexpress