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Times Cited: 52
Times Cited: 52
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Similarity
Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS.
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RAN proteins and RNA foci from antisense transcripts in C9ORF72 ALS and frontotemporal dementia.
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The C9orf72 GGGGCC repeat is translated into aggregating dipeptide-repeat proteins in FTLD/ALS.
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A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD.
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Unconventional translation of C9ORF72 GGGGCC expansion generates insoluble polypeptides specific to c9FTD/ALS.
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RAN translation at C9orf72-associated repeat expansions is selectively enhanced by the integrated stress response.
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C9ORF72 GGGGCC repeat-associated non-AUG translation is upregulated by stress through eIF2α phosphorylation.
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The C9orf72 repeat expansion disrupts nucleocytoplasmic transport.
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RPS25 is required for efficient RAN translation of C9orf72 and other neurodegenerative disease-associated nucleotide repeats.
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Antisense transcripts of the expanded C9ORF72 hexanucleotide repeat form nuclear RNA foci and undergo repeat-associated non-ATG translation in c9FTD/ALS.
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Non-ATG-initiated translation directed by microsatellite expansions.
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GGGGCC repeat expansion in C9orf72 compromises nucleocytoplasmic transport.
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C9orf72 nucleotide repeat structures initiate molecular cascades of disease.
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RNA toxicity from the ALS/FTD C9ORF72 expansion is mitigated by antisense intervention.
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CUG initiation and frameshifting enable production of dipeptide repeat proteins from ALS/FTD C9ORF72 transcripts.
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DDX3X and specific initiation factors modulate FMR1 repeat-associated non-AUG-initiated translation.
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Antisense proline-arginine RAN dipeptides linked to C9ORF72-ALS/FTD form toxic nuclear aggregates that initiate in vitro and in vivo neuronal death.
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C9orf72 repeat expansions cause neurodegeneration in Drosophila through arginine-rich proteins.
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Haploinsufficiency leads to neurodegeneration in C9ORF72 ALS/FTD human induced motor neurons.
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Bidirectional transcripts of the expanded C9orf72 hexanucleotide repeat are translated into aggregating dipeptide repeat proteins.
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Modifiers of C9orf72 dipeptide repeat toxicity connect nucleocytoplasmic transport defects to FTD/ALS.
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C9orf72-mediated ALS and FTD: multiple pathways to disease.
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Translation of dipeptide repeat proteins from the C9ORF72 expanded repeat is associated with cellular stress.
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G-quadruplex-binding small molecules ameliorate C9orf72 FTD/ALS pathology in vitro and in vivo.
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The Role of Dipeptide Repeats in C9ORF72-Related ALS-FTD.
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Targeting RNA foci in iPSC-derived motor neurons from ALS patients with a C9ORF72 repeat expansion.
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eIF4B and eIF4H mediate GR production from expanded G4C2 in a Drosophila model for C9orf72-associated ALS.
Lindsey D Goodman, Mercedes Prudencio, Ananth R Srinivasan, Olivia M Rifai, Virginia M-Y Lee, Leonard Petrucelli, Nancy M Bonini. Acta Neuropathol Commun 2019
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Repeat-associated non-AUG translation in C9orf72-ALS/FTD is driven by neuronal excitation and stress.
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Gain of Toxicity from ALS/FTD-Linked Repeat Expansions in C9ORF72 Is Alleviated by Antisense Oligonucleotides Targeting GGGGCC-Containing RNAs.
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C9orf72 Dipeptide Repeats Impair the Assembly, Dynamics, and Function of Membrane-Less Organelles.
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CGG Repeat-Associated Non-AUG Translation Utilizes a Cap-Dependent Scanning Mechanism of Initiation to Produce Toxic Proteins.
Michael G Kearse, Katelyn M Green, Amy Krans, Caitlin M Rodriguez, Alexander E Linsalata, Aaron C Goldstrohm, Peter K Todd. Mol Cell 2016
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Spt4 selectively regulates the expression of C9orf72 sense and antisense mutant transcripts.
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Poly-dipeptides encoded by the C9orf72 repeats bind nucleoli, impede RNA biogenesis, and kill cells.
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Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis.
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Poly(GR) impairs protein translation and stress granule dynamics in C9orf72-associated frontotemporal dementia and amyotrophic lateral sclerosis.
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Targeted degradation of sense and antisense C9orf72 RNA foci as therapy for ALS and frontotemporal degeneration.
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Drosophila screen connects nuclear transport genes to DPR pathology in c9ALS/FTD.
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C9ORF72 poly(GA) aggregates sequester and impair HR23 and nucleocytoplasmic transport proteins.
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Hexanucleotide repeats in ALS/FTD form length-dependent RNA foci, sequester RNA binding proteins, and are neurotoxic.
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The disease-associated r(GGGGCC)n repeat from the C9orf72 gene forms tract length-dependent uni- and multimolecular RNA G-quadruplex structures.
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Differential Toxicity of Nuclear RNA Foci versus Dipeptide Repeat Proteins in a Drosophila Model of C9ORF72 FTD/ALS.
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Heterochromatin anomalies and double-stranded RNA accumulation underlie C9orf72 poly(PR) toxicity.
Yong-Jie Zhang, Lin Guo, Patrick K Gonzales, Tania F Gendron, Yanwei Wu, Karen Jansen-West, Aliesha D O'Raw, Sarah R Pickles, Mercedes Prudencio, Yari Carlomagno,[...]. Science 2019
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Nucleolar stress and impaired stress granule formation contribute to C9orf72 RAN translation-induced cytotoxicity.
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C9orf72 FTLD/ALS-associated Gly-Ala dipeptide repeat proteins cause neuronal toxicity and Unc119 sequestration.
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The C9ORF72 GGGGCC expansion forms RNA G-quadruplex inclusions and sequesters hnRNP H to disrupt splicing in ALS brains.
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A zebrafish model for C9orf72 ALS reveals RNA toxicity as a pathogenic mechanism.
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C9orf72 hexanucleotide repeat associated with amyotrophic lateral sclerosis and frontotemporal dementia forms RNA G-quadruplexes.
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Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS.
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Co-cited is the co-citation frequency, indicating how many articles cite the article together with the query article. Similarity is the co-citation as percentage of the times cited of the query article or the article in the search results, whichever is the lowest. These numbers are calculated for the last 100 citations when articles are cited more than 100 times.