Evidence map›Paper›PMID 29723523›Full record

ReviewBrain research2018

The physiological and pathological biophysics of phase separation and gelation of RNA binding proteins in amyotrophic lateral sclerosis and fronto-temporal lobar degeneration.

Peter St George-Hyslop, Julie Qiaojin Lin, Akinori Miyashita, Emma C Phillips, Seema Qamar, Suzanne J Randle, GuoZhen Wang

Open access · hybridAbstract readReview
In one paragraph

Review in Brain research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

41 citing papers in PubMed, 83 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Biomolecular Condensates Can Enhance Homotypic RNA Clustering.bioRxiv : the preprint server for biology · 2025
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Aging can transform single-component protein condensates into multiphase architectures.Proceedings of the National Academy of Sciences of the United States of America · 2022
    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

7 authors at 2 institutions in 2 countries.

Peter St George-HyslopCambridge Institute for Medical Research, Department of Clinical Neurosciences, University of Cambridge, Cambridge CB2 0XY, UK; Tanz Centre for Research in Neurodegenerative Diseases, and Departments of Medicine, Medical Biophysics and Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario M5S 3H2, Canada. Electronic address: p.hyslop@utoronto.ca.
Julie Qiaojin LinDepartment of Physiology, Development, and Neuroscience, University of Cambridge, Cambridge CB2 3DY, UK.
Akinori MiyashitaTanz Centre for Research in Neurodegenerative Diseases, and Departments of Medicine, Medical Biophysics and Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario M5S 3H2, Canada.
Emma C PhillipsCambridge Institute for Medical Research, Department of Clinical Neurosciences, University of Cambridge, Cambridge CB2 0XY, UK.
Seema QamarCambridge Institute for Medical Research, Department of Clinical Neurosciences, University of Cambridge, Cambridge CB2 0XY, UK.
Suzanne J RandleCambridge Institute for Medical Research, Department of Clinical Neurosciences, University of Cambridge, Cambridge CB2 0XY, UK.
GuoZhen WangCambridge Institute for Medical Research, Department of Clinical Neurosciences, University of Cambridge, Cambridge CB2 0XY, UK.
University of Cambridge · GBUniversity of Toronto · CA

Funding

CIHRWellcome Trust 203249/Z/16/Z
6 · The paper itself

Abstract

Many RNA binding proteins, including FUS, contain moderately repetitive, low complexity, intrinsically disordered domains. These sequence motifs have recently been found to underpin reversible liquid: liquid phase separation and gelation of these proteins, permitting them to reversibly transition from a monodispersed state to liquid droplet- or hydrogel-like states. This function allows the proteins to serve as scaffolds for the formation of reversible membraneless intracellular organelles such as nucleoli, stress granules and neuronal transport granules. Using FUS as an example, this review examines the biophysics of this physiological process, and reports on how mutations and changes in post-translational state alter phase behaviour, and lead to neurodegenerative diseases such as amyotrophic lateral sclerosis and frontotemporal lobar degeneration.

Indexed as

Amyotrophic Lateral SclerosisBiophysicsCytoplasmic GranulesDNA-Binding ProteinsFrontotemporal DementiaFrontotemporal Lobar DegenerationHumansMutationNeurodegenerative DiseasesProtein DomainsProtein Processing, Post-TranslationalRNA-Binding Protein FUSRNA-Binding ProteinsTemporal LobeDNA-Binding ProteinsRNA-Binding Protein FUSRNA-Binding ProteinsAmyotrophic lateral sclerosisArginine methylationCation-pi interactionsFrontotemporal dementiaPhase separationRNA binding proteins

Identifiers

PMID29723523
PMCPMC6018615
OpenAlexW2800004384

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.