Evidence map›Paper›PMID 31595953›Full record

ReviewHuman molecular genetics2019

Inherited and Sporadic Amyotrophic Lateral Sclerosis and Fronto-Temporal Lobar Degenerations arising from Pathological Condensates of Phase Separating Proteins.

Michael Fernandopulle, GuoZhen Wang, Jonathon Nixon-Abell, Seema Qamar, Varun Balaji, Ryuta Morihara, Peter H St George-Hyslop

Open access · bronzeAbstract readReview
In one paragraph

Review in Human molecular genetics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

13 citing papers in PubMed, 19 citations in OpenAlex.

  1. Sticky interactions govern sequence-dependent dynamics in biomolecular condensates.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. The structural properties of full-length annexin A11.Frontiers in molecular biosciences · 2024
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. FUS and TDP-43 Phases in Health and Disease.Trends in biochemical sciences · 2021
    Review
  12. Review
  13. 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.

Michael FernandopulleCambridge Institute for Medical Research, Department of Clinical Neurosciences, University of Cambridge, Cambridge, UK, CB2 0XY.
GuoZhen WangCambridge Institute for Medical Research, Department of Clinical Neurosciences, University of Cambridge, Cambridge, UK, CB2 0XY.
Jonathon Nixon-AbellCambridge Institute for Medical Research, Department of Clinical Neurosciences, University of Cambridge, Cambridge, UK, CB2 0XY.
Seema QamarCambridge Institute for Medical Research, Department of Clinical Neurosciences, University of Cambridge, Cambridge, UK, CB2 0XY.
Varun BalajiTanz Centre for Research in Neurodegenerative Diseases, and Departments of Medicine, University of Toronto, Toronto, Ontario, Canada, M5S 3H2.
Ryuta MoriharaTanz Centre for Research in Neurodegenerative Diseases, and Departments of Medicine, University of Toronto, Toronto, Ontario, Canada, M5S 3H2.
Peter H St George-HyslopCambridge Institute for Medical Research, Department of Clinical Neurosciences, University of Cambridge, Cambridge, UK, CB2 0XY.
University of Cambridge · GBUniversity of Toronto · CA

Funding

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

Abstract

Recent work on the biophysics of proteins with low complexity, intrinsically disordered domains that have the capacity to form biological condensates has profoundly altered the concepts about the pathogenesis of inherited and sporadic neurodegenerative disorders associated with pathological accumulation of these proteins. In the present review, we use the FUS, TDP-43 and A11 proteins as examples to illustrate how missense mutations and aberrant post-translational modifications of these proteins cause amyotrophic lateral sclerosis (ALS) and fronto-temporal lobar degeneration (FTLD).

Indexed as

Amyotrophic Lateral SclerosisAnnexinsBiological TransportDNA-Binding ProteinsFrontotemporal Lobar DegenerationHumansIntracellular MembranesMutation, MissenseNeurodegenerative DiseasesNeuronsProtein Processing, Post-TranslationalRNA-Binding Protein FUSTemporal LobeAnnexinsDNA-Binding ProteinsRNA-Binding Protein FUSTARDBP protein, humanAmyotrophic lateral sclerosisANXA11biological condensatesfronto-temporal dementiaFUSgelationhydrogelslocal RNA translationneuronal transport granulesphase separationstress granulesTDP-43

Identifiers

PMID31595953
PMCPMC6872449
OpenAlexW2958983479

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.