Evidence map›Paper›PMID 28942918›Full record

ArticleCell2017

Structure of FUS Protein Fibrils and Its Relevance to Self-Assembly and Phase Separation of Low-Complexity Domains.

Dylan T Murray, Masato Kato, Yi Lin, Kent R Thurber, Ivan Hung, Steven L McKnight, Robert Tycko

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 438 papers.

0numbers the graph read from it
0cells of the map it votes in
438citing papers in PubMed
28.0field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

438 citing papers in PubMed, 789 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
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  12. Construction of a COChemistry (Weinheim an der Bergstrasse, Germany) · 2026
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  13. Review
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  15. Article
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  18. Article
  19. Article
  20. Droplet growth, Ostwald's rule, and emergence of order in Fused in Sarcoma.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article

378 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 1 country.

Dylan T MurrayLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA; Postdoctoral Research Associate Program, National Institute of General Medical Sciences, National Institutes of Health, Bethesda, MD 20892-6200, USA.
Masato KatoDepartment of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9152, USA.
Yi LinDepartment of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9152, USA.
Kent R ThurberLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA.
Ivan HungNational High Magnetic Field Laboratory, Florida State University, Tallahassee, FL 32310, USA.
Steven L McKnightDepartment of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9152, USA. Electronic address: steven.mcknight@utsouthwestern.edu.
Robert TyckoLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA. Electronic address: robertty@mail.nih.gov.
The University of Texas Southwestern Medical Center · USNational Institutes of Health · USNational High Magnetic Field Laboratory · USNational Institute of Diabetes and Digestive and Kidney Diseases · US

Funding

Structural Studies of Prion Fibrils and Other Protein FibrilsZIADK075031 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI TYCKO, ROBERT · 2009 to 2025
$7.3M
Reversible Polymerization of Low Complexity Polypeptide Sequences as a FrameworkU01GM107623 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI MCKNIGHT, STEVEN L · 2014 to 2017
$2.0M
Laser Scanning Confocal for UT Southwestern Live Cell Imaging FacilityS10OD021684 · OD · UT SOUTHWESTERN MEDICAL CENTER · PI LUBY-PHELPS, KATHERINE J · 2016 to 2016
$455k
Intramural NIH HHS ZIA DK075031NIGMS NIH HHS U01 GM107623NIH HHS S10 OD021684
6 · The paper itself

Abstract

Polymerization and phase separation of proteins containing low-complexity (LC) domains are important factors in gene expression, mRNA processing and trafficking, and localization of translation. We have used solid-state nuclear magnetic resonance methods to characterize the molecular structure of self-assembling fibrils formed by the LC domain of the fused in sarcoma (FUS) RNA-binding protein. From the 214-residue LC domain of FUS (FUS-LC), a segment of only 57 residues forms the fibril core, while other segments remain dynamically disordered. Unlike pathogenic amyloid fibrils, FUS-LC fibrils lack hydrophobic interactions within the core and are not polymorphic at the molecular structural level. Phosphorylation of core-forming residues by DNA-dependent protein kinase blocks binding of soluble FUS-LC to FUS-LC hydrogels and dissolves phase-separated, liquid-like FUS-LC droplets. These studies offer a structural basis for understanding LC domain self-assembly, phase separation, and regulation by post-translational modification.

Indexed as

Amino Acid SequenceHumansMicroscopy, Atomic ForceMicroscopy, Electron, TransmissionModels, MolecularNuclear Magnetic Resonance, BiomolecularPhosphorylationProtein DomainsRNA-Binding Protein FUSFUS protein, humanRNA-Binding Protein FUSamyloid structureamyotrophic lateral sclerosiselectron microscopyFUSlabile cross-β polymerliquid dropletliquid-liquid phase separationlow-complexity sequenceneurodegenerationsolid-state nuclear magnetic resonance

Identifiers

PMID28942918
PMCPMC5650524
OpenAlexW2758396775

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

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.