ArticleBiochemistry2020
Side Chain Hydrogen-Bonding Interactions within Amyloid-like Fibrils Formed by the Low-Complexity Domain of FUS: Evidence from Solid State Nuclear Magnetic Resonance Spectroscopy.
Article in Biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 42 citations in OpenAlex.
- Nanoscale profiling of evolving intermolecular interactions in ageing FUS condensates.Communications chemistry · 2025Article
- Conformations of a low-complexity protein in homogeneous and phase-separated frozen solutions.Biophysical journal · 2024Article
- A solid beta-sheet structure is formed at the surface of FUS droplets during aging.Nature chemical biology · 2024Article
- Solid-state NMR studies of proteins in condensed phases.Magnetic resonance letters · 2024Review
- Conformations of a Low-Complexity Protein in Homogeneous and Phase-Separated Frozen Solutions.bioRxiv : the preprint server for biology · 2024Article
- Expanding the molecular grammar of polar residues and arginine in FUS prion-like domain phase separation and aggregation.bioRxiv : the preprint server for biology · 2024Article
- The Role H-Bonding and Supramolecular Structures in Homogeneous and Enzymatic Catalysis.International journal of molecular sciences · 2023Article
- Glutathionylation on RNA-binding proteins: a regulator of liquid‒liquid phase separation in the pathogenesis of amyotrophic lateral sclerosis.Experimental & molecular medicine · 2023Review
- Ultrafast Magic Angle Spinning Solid-State NMR Spectroscopy: Advances in Methodology and Applications.Chemical reviews · 2023Review
- Liquid Droplet Aging and Seeded Fibril Formation of the Cytotoxic Granule Associated RNA Binding Protein TIA1 Low Complexity Domain.Journal of the American Chemical Society · 2023Article
- Different Intermolecular Interactions Drive Nonpathogenic Liquid-Liquid Phase Separation and Potentially Pathogenic Fibril Formation by TDP-43.International journal of molecular sciences · 2022Article
- Structure-dependent recruitment and diffusion of guest proteins in liquid droplets of FUS.Scientific reports · 2022Article
- Article
- Sequence Determines the Switch in the Fibril Forming Regions in the Low-Complexity FUS Protein and Its Variants.The journal of physical chemistry letters · 2021Article
- The Different Faces of the TDP-43 Low-Complexity Domain: The Formation of Liquid Droplets and Amyloid Fibrils.International journal of molecular sciences · 2021Review
- Real-time observation of structure and dynamics during the liquid-to-solid transition of FUS LC.Biophysical journal · 2021Article
- Characterization of design grammar of peptides for regulating liquid droplets and aggregates of FUS.Scientific reports · 2021Article
- Solid-state NMR spectroscopy.Nature reviews. Methods primers · 2021Article
- Molecular structure and interactions within amyloid-like fibrils formed by a low-complexity protein sequence from FUS.Nature communications · 2020Article
- Hydration and Dynamics of Full-Length Tau Amyloid Fibrils Investigated by Solid-State Nuclear Magnetic Resonance.Biochemistry · 2020Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
In aqueous solutions, the 214-residue low-complexity domain of the FUS protein (FUS-LC) is known to undergo liquid-liquid phase separation and also to self-assemble into amyloid-like fibrils. In previous work based on solid state nuclear magnetic resonance (ssNMR) methods, a structural model for the FUS-LC fibril core was developed, showing that residues 39-95 form the fibril core. Unlike fibrils formed by amyloid-β peptides, α-synuclein, and other amyloid-forming proteins, the FUS-LC core is largely devoid of purely hydrophobic amino acid side chains. Instead, the core-forming segment contains numerous hydroxyl-bearing residues, including 18 serines, six threonines, and eight tyrosines, suggesting that the FUS-LC fibril structure may be stabilized in part by inter-residue hydrogen bonds among side chain hydroxyl groups. Here we describe ssNMR measurements, performed on
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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.