Evidence map›Paper›PMID 30998893›Full record

ArticleNeuron2019

The Evolution of Phase-Separated TDP-43 in Stress.

Benjamin Wolozin

Open access · bronzeAbstract readComment
In one paragraph

Article in Neuron, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

15 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Small molecule JRMS modulating importin-β1 chaperone activity as a therapeutic strategy reducing TDP-43 pathology.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2026
    Article
  4. [Heterogeneity in the regulation of cellular stress responses byZhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences · 2025
    Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Protein Aggregation in the Pathogenesis of Ischemic Stroke.Cellular and molecular neurobiology · 2021
    Review
  12. Review
  13. Article
  14. Article
  15. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

Benjamin WolozinBoston University School of Medicine, Boston, MA, USA. Electronic address: bwolozin@bu.edu.
Boston University · US

Funding

Capturing the molecular complexity of Alzheimer's disease through the lens of RNA binding proteinsRF1AG056318 · NIA · BOSTON UNIVERSITY MEDICAL CAMPUS · PI LI, HU, WOLOZIN, BENJAMIN L · 2018 to 2020
$4.4M
Systems-level functional proteomics analysis assemblies in Alzheimer's disease and mouse models of tauopathyRF1AG061706 · NIA · BOSTON UNIVERSITY MEDICAL CAMPUS · PI EMILI, ANDREW, WOLOZIN, BENJAMIN L · 2019 to 2019
$3.9M
Genetic Modifiers of Protein Interaction Networks in TauopathyR01AG064932 · NIA · BOSTON UNIVERSITY MEDICAL CAMPUS · PI EMILI, ANDREW, WOLOZIN, BENJAMIN L · 2019 to 2023
$3.2M
RNA binding proteins as novel targets in Alzheimer's diseaseR01AG050471 · NIA · BOSTON UNIVERSITY MEDICAL CAMPUS · PI WOLOZIN, BENJAMIN L · 2015 to 2019
$2.9M
The role of acetylation in regulating pathophysiology of tauR01NS089544 · NINDS · MAYO CLINIC JACKSONVILLE · PI PETRUCELLI, LEONARD, WOLOZIN, BENJAMIN L · 2014 to 2018
$1.9M
Regulation of APP Processing by PresenilinsR01AG017485 · NIA · LOYOLA UNIVERSITY CHICAGO · PI WOLOZIN, BENJAMIN L · 2001 to 2004
$1.1M
Regulation of brain neuroprotection and inflammation by TIA1R21AG059925 · NIA · BOSTON UNIVERSITY MEDICAL CAMPUS · PI WOLOZIN, BENJAMIN L · 2018 to 2019
$454k
NIA NIH HHS R01 AG017485NIA NIH HHS R01 AG050471NIA NIH HHS R01 AG064932NIA NIH HHS R21 AG059925NIA NIH HHS RF1 AG056318NIA NIH HHS RF1 AG061706NINDS NIH HHS R01 NS089544
6 · The paper itself

Abstract

In this issue of Neuron, Gasset-Rosa et al. (2019) and Mann et al. (2019) demonstrate that cytoplasmic inclusions containing aggregated phosphorylated TDP-43 can evolve through three pathways: direct aggregation or phase-separated intermediates involving ejection from stress granules or seeding with exogenous fibrils. Interestingly, seeding with exogenous fibrils also induces cytoplasmic aggregates of nuclear pore proteins.

Indexed as

Amyotrophic Lateral SclerosisNeurotoxicity SyndromesDNA-Binding ProteinsHumansInclusion BodiesRNADNA-Binding ProteinsRNATARDBP protein, human

Identifiers

PMID30998893
PMCPMC6816464
OpenAlexW2936462840

What OpenQuestion holds

Textmetadata
LicenceTDM
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.