Evidence map›Paper›PMID 31022909›Full record

ReviewMolecules (Basel, Switzerland)2019

Fused in Sarcoma: Properties, Self-Assembly and Correlation with Neurodegenerative Diseases.

Chen Chen, Xiufang Ding, Nimrah Akram, Song Xue, Shi-Zhong Luo

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
8.3field-weighted citation impact, top 2% 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

47 citing papers in PubMed, 99 citations in OpenAlex.

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

5 authors at 1 institution in 1 country.

Chen ChenBeijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, China. 2017201117@mail.buct.edu.cn.
Xiufang DingBeijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, China. 13552909516@163.com.
Nimrah AkramBeijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, China. nimrahchaudhry@outlook.com.
Song XueBeijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, China. xues@mail.buct.edu.cn.ORCID 0000-0002-7955-4529
Shi-Zhong LuoBeijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, China. luosz@mail.buct.edu.cn.
Beijing University of Chemical Technology · CN

Funding

Fundamental Research Funds for the Central Universities Grand No.PYBZ1711, PT1613-08, 20130801National Natural Science Foundation of China Grant No. 91853116,21672019,21372026,21402006
6 · The paper itself

Abstract

Fused in sarcoma (FUS) is a DNA/RNA binding protein that is involved in RNA metabolism and DNA repair. Numerous reports have demonstrated by pathological and genetic analysis that FUS is associated with a variety of neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS), frontotemporal lobar degeneration (FTLD), and polyglutamine diseases. Traditionally, the fibrillar aggregation of FUS was considered to be the cause of those diseases, especially via its prion-like domains (PrLDs), which are rich in glutamine and asparagine residues. Lately, a nonfibrillar self-assembling phenomenon, liquid-liquid phase separation (LLPS), was observed in FUS, and studies of its functions, mechanism, and mutual transformation with pathogenic amyloid have been emerging. This review summarizes recent studies on FUS self-assembling, including both aggregation and LLPS as well as their relationship with the pathology of ALS, FTLD, and other neurodegenerative diseases.

Indexed as

Amyotrophic Lateral SclerosisAsparagineFrontotemporal Lobar DegenerationGPI-Linked ProteinsHumansNeurodegenerative DiseasesPeptidesPrionsProtein Aggregation, PathologicalProtein DomainsRNA-Binding Protein FUSAsparagineFUS protein, humanGPI-Linked ProteinsPeptidespolyglutaminePrionsPRND protein, humanRNA-Binding Protein FUSaggregationfused in sarcoma (FUS)neurodegenerative diseasesphase separationphase transitionprion-like domainsself-assemble

Identifiers

PMID31022909
PMCPMC6514960
OpenAlexW2942320535

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.