hnRNP A3 binds to GGGGCC repeats and is a constituent of p62-positive/TDP43-negative inclusions in the hippocampus of patients with C9orf72 mutations.
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 peptideRNA toxicity from the ALS/FTD C9ORF72 expansion is mitigated by antisense interventionThe hnRNP family: insights into their role in health and diseaseInside out: the role of nucleocytoplasmic transport in ALS and FTLDThere has been an awakening: Emerging mechanisms of C9orf72 mutations in FTD/ALSPrion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative diseaseImmunoprecipitation and mass spectrometry defines an extensive RBM45 protein-protein interaction networkPhenotypic Heterogeneity of Monogenic Frontotemporal DementiaPathological mechanisms underlying TDP-43 driven neurodegeneration in FTLD-ALS spectrum disordersConverging mechanisms in ALS and FTD: disrupted RNA and protein homeostasisA perspective on stem cell modeling of amyotrophic lateral sclerosisEmerging mechanisms of molecular pathology in ALSRNA-mediated pathogenic mechanisms in polyglutamine diseases and amyotrophic lateral sclerosisGlycine-alanine dipeptide repeat protein contributes to toxicity in a zebrafish model of C9orf72 associated neurodegenerationLoss of C9ORF72 impairs autophagy and synergizes with polyQ Ataxin-2 to induce motor neuron dysfunction and cell deathReduced hnRNPA3 increases C9orf72 repeat RNA levels and dipeptide-repeat protein depositionModeling key pathological features of frontotemporal dementia with C9ORF72 repeat expansion in iPSC-derived human neuronsKinase 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 expansionsHippocampal sclerosis dementia with the C9ORF72 hexanucleotide repeat expansionMouse Models of C9orf72 Hexanucleotide Repeat Expansion in Amyotrophic Lateral Sclerosis/ Frontotemporal DementiaSRSF1-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 neurodegenerationToxic 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 casesA 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 SclerosisProteins with Intrinsically Disordered Domains Are Preferentially Recruited to Polyglutamine Aggregates.RNA-binding protein misregulation in microsatellite expansion disorders
P2860
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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.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年学术文章
@wuu
2013年学术文章
@zh
2013年学术文章
@zh-cn
2013年学术文章
@zh-hans
2013年学术文章
@zh-my
2013年学术文章
@zh-sg
2013年學術文章
@yue
2013年學術文章
@zh-hant
name
hnRNP A3 binds to GGGGCC repea ...... tients with C9orf72 mutations.
@en
hnRNP A3 binds to GGGGCC repea ...... tients with C9orf72 mutations.
@nl
type
label
hnRNP A3 binds to GGGGCC repea ...... tients with C9orf72 mutations.
@en
hnRNP A3 binds to GGGGCC repea ...... tients with C9orf72 mutations.
@nl
prefLabel
hnRNP A3 binds to GGGGCC repea ...... tients with C9orf72 mutations.
@en
hnRNP A3 binds to GGGGCC repea ...... tients with C9orf72 mutations.
@nl
P2093
P2860
P50
P1476
hnRNP A3 binds to GGGGCC repea ...... tients with C9orf72 mutations.
@en
P2093
Hans Kretzschmar
Ian R A Mackenzie
Ignasi Forné
Jochen Herms
Jonathan Janssens
Marc Cruts
Sonja Zilow
Sven Lammich
Thomas Arzberger
P2860
P2888
P304
P356
10.1007/S00401-013-1088-7
P50
P577
2013-02-05T00:00:00Z