Evidence map›Paper›PMID 33607084›Full record

ArticleBiophysical journal2021

Real-time observation of structure and dynamics during the liquid-to-solid transition of FUS LC.

Raymond F Berkeley, Maryam Kashefi, Galia T Debelouchina

Abstract read
In one paragraph

Article in Biophysical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
–field-weighted citation impact
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

38 citing papers in PubMed.

  1. Article
  2. 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
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Raymond F BerkeleyDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California.
Maryam KashefiDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California.
Galia T DebelouchinaDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California. Electronic address: gdebelouchina@ucsd.edu.

Funding

UCSD Shiley-Marcos Alzheimer's Disease Research Center P30P30AG062429 · NIA · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Mark W Bondi · 2019 to 2026
$34.9M
RESOURCE FOR SOLID STATE NMR OF PROTEINSP41EB002031 · NIBIB · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI OPELLA, STANLEY J · 2003 to 2018
$16.3M
U of Calif, San Diego Neuroscience Microscopy ImagingP30NS047101 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GLEESON, JOSEPH G, ZHENG, BINHAI · 2003 to 2022
$9.0M
Chemistry-Biology Interfaces at UCSDT32GM146648 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Michael D. Burkart, Alexis C. Komor · 2022 to 2026
$876k
Chemical Biology Interfaces at UC San DiegoT32GM112584 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BURKART, MICHAEL D. · 2015 to 2019
$729k
Structural transformations of dementia-related proteins: droplets, gels and amyloidsR21AG069064 · NIA · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DEBELOUCHINA, GALIA · 2020 to 2020
$413k
NIA NIH HHS P30 AG062429NIA NIH HHS R21 AG069064NIBIB NIH HHS P41 EB002031NIGMS NIH HHS T32 GM112584NIGMS NIH HHS T32 GM146648NINDS NIH HHS P30 NS047101
6 · The paper itself

Abstract

A subset of the proteins found in pathological protein fibrils also exhibit tendencies for liquid-liquid phase separation (LLPS) both in vitro and in cells. The mechanisms underlying the connection between these phase transitions have been challenging to study due to the heterogeneous and dynamic nature of the states formed during the maturation of LLPS protein droplets into gels and solid aggregates. Here, we interrogate the liquid-to-solid transition of the low-complexity domain of the RNA-binding protein FUS (FUS LC), which has been shown to adopt LLPS, gel-like, and amyloid states. We employ magic-angle-spinning NMR spectroscopy, which has allowed us to follow these transitions in real time and with residue-specific resolution. We observe the development of β-sheet structure through the maturation process and show that the final state of FUS LC fibrils produced after LLPS is distinct from that grown from fibrillar seeds. We also apply our methodology to FUS LC G156E, a clinically relevant FUS mutant that exhibits accelerated fibrillization rates. We observe significant changes in dynamics during the transformation of the FUS LC G156E construct and begin to unravel the sequence specific contributions to this phenomenon with computational studies of the phase-separated state of FUS LC and FUS LC G156E.

Indexed as

AmyloidRNA-Binding Protein FUSMagnetic Resonance SpectroscopyPhase TransitionProtein DomainsAmyloidRNA-Binding Protein FUS

Identifiers

PMID33607084
PMCPMC8059203

What OpenQuestion holds

Textmetadata
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.