hnRNP A3 binds to GGGGCC repeats and is a constituent of p62-positive/TDP43-negative inclusions in the hippocampus of patients with C9orf72 mutations. - Test2 - elhamkhani - TriplyDB

hnRNP A3 binds to GGGGCC repeats and is a constituent of p62-positive/TDP43-negative inclusions in the hippocampus of patients with C9orf72 mutations.

hnRNP A3 binds to GGGGCC repeats and is a constituent of p62-positive/TDP43-negative inclusions in the hippocampus of patients with C9orf72 mutations.

http://www.wikidata.org/entity/Q44742682

about

Protein interaction analysis of senataxin and the ALS4 L389S mutant yields insights into senataxin post-translational modification and uncovers mutant-specific binding with a brain cytoplasmic RNA-encoded peptide RNA toxicity from the ALS/FTD C9ORF72 expansion is mitigated by antisense intervention The hnRNP family: insights into their role in health and disease Inside out: the role of nucleocytoplasmic transport in ALS and FTLD There has been an awakening: Emerging mechanisms of C9orf72 mutations in FTD/ALS Prion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative disease Immunoprecipitation and mass spectrometry defines an extensive RBM45 protein-protein interaction network Phenotypic Heterogeneity of Monogenic Frontotemporal Dementia Pathological mechanisms underlying TDP-43 driven neurodegeneration in FTLD-ALS spectrum disorders Converging mechanisms in ALS and FTD: disrupted RNA and protein homeostasis A perspective on stem cell modeling of amyotrophic lateral sclerosis Emerging mechanisms of molecular pathology in ALS RNA-mediated pathogenic mechanisms in polyglutamine diseases and amyotrophic lateral sclerosis Glycine-alanine dipeptide repeat protein contributes to toxicity in a zebrafish model of C9orf72 associated neurodegeneration Loss of C9ORF72 impairs autophagy and synergizes with polyQ Ataxin-2 to induce motor neuron dysfunction and cell death Reduced hnRNPA3 increases C9orf72 repeat RNA levels and dipeptide-repeat protein deposition Modeling key pathological features of frontotemporal dementia with C9ORF72 repeat expansion in iPSC-derived human neurons Kinase Inhibitor Screening Identifies Cyclin-Dependent Kinases and Glycogen Synthase Kinase 3 as Potential Modulators of TDP-43 Cytosolic Accumulation during Cell Stress.Cytoplasmic poly-GA aggregates impair nuclear import of TDP-43 in C9orf72 ALS/FTLD.C9ORF72 hexanucleotide repeat exerts toxicity in a stable, inducible motor neuronal cell model, which is rescued by partial depletion of Pten.Sequestration of multiple RNA recognition motif-containing proteins by C9orf72 repeat expansions Hippocampal sclerosis dementia with the C9ORF72 hexanucleotide repeat expansion Mouse Models of C9orf72 Hexanucleotide Repeat Expansion in Amyotrophic Lateral Sclerosis/ Frontotemporal Dementia SRSF1-dependent nuclear export inhibition of C9ORF72 repeat transcripts prevents neurodegeneration and associated motor deficits.Molecular network analysis suggests a logical hypothesis for the pathological role of c9orf72 in amyotrophic lateral sclerosis/frontotemporal dementia.C9orf72 hypermethylation protects against repeat expansion-associated pathology in ALS/FTD.C9orf72 amyotrophic lateral sclerosis and frontotemporal dementia: gain or loss of function?RNA-protein interactions in unstable microsatellite diseases.Targeted exon capture and sequencing in sporadic amyotrophic lateral sclerosis.Expanded GGGGCC repeat RNA associated with amyotrophic lateral sclerosis and frontotemporal dementia causes neurodegeneration Toxic RNA as a driver of disease in a common form of ALS and dementia.Phosphorylation of hnRNP K by cyclin-dependent kinase 2 controls cytosolic accumulation of TDP-43.Dysregulation of RNA Binding Protein Aggregation in Neurodegenerative Disorders.G-quadruplex structures contribute to the neuroprotective effects of angiogenin-induced tRNA fragments.Hypermethylation of repeat expanded C9orf72 is a clinical and molecular disease modifier.Drosha inclusions are new components of dipeptide-repeat protein aggregates in FTLD-TDP and ALS C9orf72 expansion cases A network of RNA and protein interactions in Fronto Temporal Dementia.C9ORF72 GGGGCC Expanded Repeats Produce Splicing Dysregulation which Correlates with Disease Severity in Amyotrophic Lateral Sclerosis Proteins with Intrinsically Disordered Domains Are Preferentially Recruited to Polyglutamine Aggregates.RNA-binding protein misregulation in microsatellite expansion disorders

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P2860

hnRNP A3 binds to GGGGCC repeats and is a constituent of p62-positive/TDP43-negative inclusions in the hippocampus of patients with C9orf72 mutations.

http://www.wikidata.org/entity/Q44742682

description

2013 nî lūn-bûn

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2013年の論文

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2013年学术文章

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2013年学术文章

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2013年學術文章

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2013年學術文章

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name

hnRNP A3 binds to GGGGCC repea ...... tients with C9orf72 mutations.

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type

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hnRNP A3 binds to GGGGCC repea ...... tients with C9orf72 mutations.

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hnRNP A3 binds to GGGGCC repea ...... tients with C9orf72 mutations.

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prefLabel

hnRNP A3 binds to GGGGCC repea ...... tients with C9orf72 mutations.

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hnRNP A3 binds to GGGGCC repea ...... tients with C9orf72 mutations.

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Acta Neuropathologica

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Hans Kretzschmar

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Ian R A Mackenzie

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Ignasi Forné

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Jochen Herms

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Jonathan Janssens

http://www.w3.org/2001/XMLSchema#string

Marc Cruts

http://www.w3.org/2001/XMLSchema#string

Sonja Zilow

http://www.w3.org/2001/XMLSchema#string

Sven Lammich

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Thomas Arzberger

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P2860

Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS

Mutations in the endosomal ESCRTIII-complex subunit CHMP2B in frontotemporal dementia

The genetics and neuropathology of frontotemporal lobar degeneration

Mutations in the profilin 1 gene cause familial amyotrophic lateral sclerosis

A harmonized classification system for FTLD-TDP pathology

Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS

A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD

Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei

Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide

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s00401-013-1088-7

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413-423

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3

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125

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Christian Haass

Christine Van Broeckhoven

Manuela Neumann

Gernot Kleinberger

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2013-02-05T00:00:00Z

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235401187

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