ArticleiScience2022
Molecular structure of an amyloid fibril formed by FUS low-complexity domain.
Article in iScience, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 39 citations in OpenAlex.
- Assessment of Aggregation- and Condensation-Prone Regions of Proteins Involved in Neurodegenerative, Neurological and Mental-State Diseases.Biomolecules · 2026Article
- Sequence-encoded conformational biases correlate with self-assembly modes of intrinsically disordered proteins.PNAS nexus · 2026Article
- Pharmacological targeting of oncogenic condensates in cancer: mechanistic insights and therapeutic opportunities.Acta pharmacologica Sinica · 2026Review
- Amyloidogenic oligomers derived from TDP-43 LCD promote the condensation and phosphorylation of TDP-43.Chemical science · 2026Article
- Structural basis for T-cell intracellular antigen-1 amyloid fibril formation revealed by cryo-electron microscopy.PNAS nexus · 2025Article
- How Sup35 monomer conformation and amyloid fibril polymorphism determine yeast strain phenotypes.Research square · 2025Article
- Purification tags markedly affect self-aggregation of CPEB3.FEBS letters · 2025Article
- Amyloid fibril structures link CHCHD10 and CHCHD2 to neurodegeneration.Nature communications · 2025Article
- RNA-binding proteins in ALS and FTD: from pathogenic mechanisms to therapeutic insights.Molecular neurodegeneration · 2025Review
- Capturing the Conformational Heterogeneity of HSPB1 Chaperone Oligomers at Atomic Resolution.Journal of the American Chemical Society · 2025Article
- Probing the Formation and Liquid-to-Solid Transition of FUS Condensates via the Lifetimes of Fluorescent Proteins.The journal of physical chemistry letters · 2025Article
- Review
- Targeting Protein Aggregation in ALS.Biomolecules · 2024Review
- Molecular Mechanisms of Phase Separation and Amyloidosis of ALS/FTD-linked FUS and TDP-43.Aging and disease · 2024Review
- A solid beta-sheet structure is formed at the surface of FUS droplets during aging.Nature chemical biology · 2024Article
- Amyloid fibril structures link CHCHD10 and CHCHD2 to neurodegeneration.bioRxiv : the preprint server for biology · 2024Article
- Conformational fluctuations and phases in fused in sarcoma (FUS) low-complexity domain.Biopolymers · 2024Review
- Article
- Nucleocapsid proteins from human coronaviruses possess phase separation capabilities and promote FUS pathological aggregation.Protein science : a publication of the Protein Society · 2023Article
- Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
FUS is a multifunctional nuclear protein which undergoes liquid-liquid phase separation in response to stress and DNA damage. Dysregulation of FUS dynamic phase separation leads to formation of pathological fibril closely associated with neurodegenerative diseases such as amyotrophic lateral sclerosis and frontotemporal dementia. In this study, we determined the cryo-EM structure of a cytotoxic fibril formed by the low-complexity (LC) domain of FUS at 2.9 Å resolution. The fibril structure exhibits a new and extensive serpentine fold consisting of three motifs incorporating together via a Tyr triad. FUS LC employs 91 residues to form an enlarged and stable fibril core via hydrophilic interaction and hydrogen bonds, which is distinct from most of previously determined fibrils commonly stabilized by hydrophobic interaction. Our work reveals the structural basis underlying formation of a cytotoxic and thermostable fibril of FUS LC and sheds light on understanding the liquid-to-solid phase transition of FUS in disease.
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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.