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Times Cited: 817
Times Cited: 817
Times Cited
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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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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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GGGGCC repeat expansion in C9orf72 compromises nucleocytoplasmic transport.
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The C9orf72 repeat expansion disrupts nucleocytoplasmic transport.
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C9orf72 repeat expansions cause neurodegeneration in Drosophila through arginine-rich proteins.
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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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C9orf72 Dipeptide Repeats Impair the Assembly, Dynamics, and Function of Membrane-Less Organelles.
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Poly-dipeptides encoded by the C9orf72 repeats bind nucleoli, impede RNA biogenesis, and kill cells.
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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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Non-ATG-initiated translation directed by microsatellite expansions.
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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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C9ORF72 poly(GA) aggregates sequester and impair HR23 and nucleocytoplasmic transport proteins.
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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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Gain of Toxicity from ALS/FTD-Linked Repeat Expansions in C9ORF72 Is Alleviated by Antisense Oligonucleotides Targeting GGGGCC-Containing RNAs.
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RNA toxicity from the ALS/FTD C9ORF72 expansion is mitigated by antisense intervention.
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C9orf72-mediated ALS and FTD: multiple pathways to disease.
Rubika Balendra, Adrian M Isaacs. Nat Rev Neurol 2018
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Phase Separation of C9orf72 Dipeptide Repeats Perturbs Stress Granule Dynamics.
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C9orf72 FTLD/ALS-associated Gly-Ala dipeptide repeat proteins cause neuronal toxicity and Unc119 sequestration.
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Aggregation-prone c9FTD/ALS poly(GA) RAN-translated proteins cause neurotoxicity by inducing ER stress.
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C9ORF72 GGGGCC repeat-associated non-AUG translation is upregulated by stress through eIF2α phosphorylation.
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Neurodegeneration. C9ORF72 repeat expansions in mice cause TDP-43 pathology, neuronal loss, and behavioral deficits.
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Loss of C9ORF72 impairs autophagy and synergizes with polyQ Ataxin-2 to induce motor neuron dysfunction and cell death.
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Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6.
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RAN translation at C9orf72-associated repeat expansions is selectively enhanced by the integrated stress response.
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Sense-encoded poly-GR dipeptide repeat proteins correlate to neurodegeneration and uniquely co-localize with TDP-43 in dendrites of repeat-expanded C9orf72 amyotrophic lateral sclerosis.
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C9orf72 nucleotide repeat structures initiate molecular cascades of disease.
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Targeted degradation of sense and antisense C9orf72 RNA foci as therapy for ALS and frontotemporal degeneration.
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Haploinsufficiency leads to neurodegeneration in C9ORF72 ALS/FTD human induced motor neurons.
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C9orf72 is required for proper macrophage and microglial function in mice.
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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 Role of Dipeptide Repeats in C9ORF72-Related ALS-FTD.
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Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis.
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TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis.
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C9orf72 poly(GR) aggregation induces TDP-43 proteinopathy.
Casey N Cook, Yanwei Wu, Hana M Odeh, Tania F Gendron, Karen Jansen-West, Giulia Del Rosso, Mei Yue, Peizhou Jiang, Edward Gomes, Jimei Tong,[...]. Sci Transl Med 2020
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Poly(GR) in C9ORF72-Related ALS/FTD Compromises Mitochondrial Function and Increases Oxidative Stress and DNA Damage in iPSC-Derived Motor Neurons.
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Reduced C9ORF72 function exacerbates gain of toxicity from ALS/FTD-causing repeat expansion in C9orf72.
Qiang Zhu, Jie Jiang, Tania F Gendron, Melissa McAlonis-Downes, Lulin Jiang, Amy Taylor, Sandra Diaz Garcia, Somasish Ghosh Dastidar, Maria J Rodriguez, Patrick King,[...]. Nat Neurosci 2020
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C9ORF72-ALS/FTD-associated poly(GR) binds Atp5a1 and compromises mitochondrial function in vivo.
So Yoen Choi, Rodrigo Lopez-Gonzalez, Gopinath Krishnan, Hannah L Phillips, Alissa Nana Li, William W Seeley, Wei-Dong Yao, Sandra Almeida, Fen-Biao Gao. Nat Neurosci 2019
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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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A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation.
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Repeat-associated non-AUG translation in C9orf72-ALS/FTD is driven by neuronal excitation and stress.
Thomas Westergard, Kevin McAvoy, Katelyn Russell, Xinmei Wen, Yu Pang, Brandie Morris, Piera Pasinelli, Davide Trotti, Aaron Haeusler. EMBO Mol Med 2019
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Translation of dipeptide repeat proteins from the C9ORF72 expanded repeat is associated with cellular stress.
Yoshifumi Sonobe, Ghanashyam Ghadge, Katsuhisa Masaki, Ataman Sendoel, Elaine Fuchs, Raymond P Roos. Neurobiol Dis 2018
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In Situ Structure of Neuronal C9orf72 Poly-GA Aggregates Reveals Proteasome Recruitment.
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Quantitative analysis and clinico-pathological correlations of different dipeptide repeat protein pathologies in C9ORF72 mutation carriers.
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14
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.