ReviewEmerging topics in life sciences2020
Arginine-rich dipeptide-repeat proteins as phase disruptors in C9-ALS/FTD.
Review in Emerging topics in life sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 43 citations in OpenAlex.
- Dysregulated neuronal mRNA transport and translation in FTD/ALS.NPJ dementia · 2026Review
- Targeting GeneInternational journal of molecular sciences · 2025Review
- NLS-binding deficient Kapβ2 reduces neurotoxicity via selective interaction with C9orf72-ALS/FTD dipeptide repeats.Communications biology · 2025Article
- Nuclear-import receptors as gatekeepers of pathological phase transitions in ALS/FTD.Molecular neurodegeneration · 2024Review
- CLIP-Seq analysis enables the design of protective ribosomal RNA bait oligonucleotides againstScience advances · 2023Article
- Transcriptome-wide RNA binding analysis of C9orf72 poly(PR) dipeptides.Life science alliance · 2023Article
- Poly(A)-binding protein is an ataxin-2 chaperone that regulates biomolecular condensates.Molecular cell · 2023Article
- Aberrant phase separation is a common killing strategy of positively charged peptides in biology and human disease.bioRxiv : the preprint server for biology · 2023Article
- Energy landscapes and heat capacity signatures for peptides correlate with phase separation propensity.QRB discovery · 2023Article
- RAN proteins in neurodegenerative disease: Repeating themes and unifying therapeutic strategies.Current opinion in neurobiology · 2022Review
- Nuclear-Import Receptors Counter Deleterious Phase Transitions in Neurodegenerative Disease.Journal of molecular biology · 2022Review
- p53 Transactivation Domain Mediates Binding and Phase Separation with Poly-PR/GR.International journal of molecular sciences · 2021Article
- C9orf72-derived arginine-rich poly-dipeptides impede phase modifiers.Nature communications · 2021Article
- Molecular mechanisms underlying nucleotide repeat expansion disorders.Nature reviews. Molecular cell biology · 2021Review
- Biochemical Timekeeping Via Reentrant Phase Transitions.Journal of molecular biology · 2021Review
- Proline/arginine dipeptide repeat polymers derail protein folding in amyotrophic lateral sclerosis.Nature communications · 2021Article
- Higher-order organization of biomolecular condensates.Open biology · 2021Review
- Combating deleterious phase transitions in neurodegenerative disease.Biochimica et biophysica acta. Molecular cell research · 2021Review
- Dihedral Angle Measurements for Structure Determination by Biomolecular Solid-State NMR Spectroscopy.Frontiers in molecular biosciences · 2021Review
- Nuclear Import Receptors Directly Bind to Arginine-Rich Dipeptide Repeat Proteins and Suppress Their Pathological Interactions.Cell reports · 2020Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
A hexanucleotide repeat expansion GGGGCC (G4C2) within chromosome 9 open reading frame 72 (C9orf72) is the most common genetic cause of amyotrophic lateral sclerosis and frontotemporal dementia (C9-ALS/FTD). This seminal realization has rapidly focused our attention to the non-canonical translation (RAN translation) of the repeat expansion, which yields dipeptide-repeat protein products (DPRs). The mechanisms by which DPRs might contribute to C9-ALS/FTD are widely studied. Arginine-rich DPRs (R-DPRs) are the most toxic of the five different DPRs produced in neurons, but how do R-DPRs promote C9-ALS/FTD pathogenesis? Proteomic analyses have uncovered potential pathways to explore. For example, the vast majority of the R-DPR interactome is comprised of disease-linked RNA-binding proteins (RBPs) with low-complexity domains (LCDs), strongly suggesting a link between R-DPRs and aberrations in liquid-liquid phase separation (LLPS). In this review, we showcase several potential mechanisms by which R-DPRs disrupt various phase-separated compartments to elicit deleterious neurodegeneration. We also discuss potential therapeutic strategies to counter R-DPR toxicity in C9-ALS/FTD.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.