Evidence map›Paper›PMID 31911437›Full record

ArticleThe Journal of biological chemistry2020

Granulins modulate liquid-liquid phase separation and aggregation of the prion-like C-terminal domain of the neurodegeneration-associated protein TDP-43.

Anukool A Bhopatkar, Vladimir N Uversky, Vijayaraghavan Rangachari

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.5field-weighted citation impact, top 8% 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

23 citing papers in PubMed, 40 citations in OpenAlex.

  1. Reversible Redox-Responsive Peptide Condensates With RNA.Chembiochem : a European journal of chemical biology · 2026
    Article
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  6. In silico design ofHeliyon · 2024
    Article
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  8. Review
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  10. Article
  11. Identifying and Diagnosing TDP-43 Neurodegenerative Diseases in Psychiatry.The American journal of geriatric psychiatry : official journal of the American Association for Geriatric Psychiatry · 2024
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Peptide-based coacervates in therapeutic applications.Frontiers in bioengineering and biotechnology · 2022
    Review
  17. Article
  18. Review
  19. Liquid-liquid phase separation of tau: From molecular biophysics to physiology and disease.Protein science : a publication of the Protein Society · 2021
    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 at 2 institutions in 2 countries.

Anukool A BhopatkarDepartment of Chemistry and Biochemistry, School of Mathematics and Natural Sciences, University of Southern Mississippi, Hattiesburg, Mississippi 39406.
Vladimir N UverskyDepartment of Molecular Medicine and Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, Florida 33620; Laboratory of New Methods in Biology, Institute for Biological Instrumentation, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia.
Vijayaraghavan RangachariDepartment of Chemistry and Biochemistry, School of Mathematics and Natural Sciences, University of Southern Mississippi, Hattiesburg, Mississippi 39406. Electronic address: vijay.rangachari@usm.edu.
University of Southern Mississippi · USInstitute for Biological Instrumentation · RU

Funding

Training and Mentoring Core P20GM103476 · NIGMS · UNIVERSITY OF SOUTHERN MISSISSIPPI · PI MICHAEL R GARRETT · 2012 to 2026
$60.2M
Controlling tau toxicity from inside and outside of neuronsRF1AG055088 · NIA · UNIVERSITY OF SOUTH FLORIDA · PI BICKFORD, PAULA C, BLAIR, LAURA J · 2017 to 2017
$2.3M
Structural Transitions in Proteins and Protein AssembliesR01GM120634 · NIGMS · UNIVERSITY OF OKLAHOMA · PI HANSMANN, ULRICH H.E. · 2017 to 2020
$1.2M
Role of Lipid-derived Oligomer Strains in AD PhenotypesR56AG062292 · NIA · UNIVERSITY OF SOUTHERN MISSISSIPPI · PI RANGACHARI, VIJAY · 2018 to 2018
$671k
NIA NIH HHS R56 AG062292NIA NIH HHS RF1 AG055088NIGMS NIH HHS P20 GM103476NIGMS NIH HHS R01 GM120634
6 · The paper itself

Abstract

TAR DNA-binding protein 43 (TDP-43) has emerged as a key player in many neurodegenerative pathologies, including frontotemporal lobar degeneration (FTLD) and amyotrophic lateral sclerosis (ALS). Hallmarks of both FTLD and ALS are the toxic cytoplasmic inclusions of the prion-like C-terminal fragments of TDP-43 CTD (TDP-43 C-terminal domain), formed upon proteolytic cleavage of full-length TDP-43 in the nucleus and subsequent transport to the cytoplasm. Both full-length TDP-43 and its CTD are also known to form stress granules by coacervating with RNA in the cytoplasm during stress and may be involved in these pathologies. Furthermore, mutations in the

Indexed as

Protein AggregatesBenzothiazolesDNA-Binding ProteinsGranulinsModels, BiologicalNerve DegenerationOxidation-ReductionPrionsProtein DomainsRNABenzothiazolesDNA-Binding ProteinsGranulinsPrionsProtein AggregatesRNAthioflavin TALSALS (Lou Gehrig disease)FTLDGranulinsintrinsically disordered proteinliquid–liquid phase separationprogranulinprotein dynamicprotein–protein interactionstress granuleTAR DNA-binding protein 43 (TDP-43, TARDBP)

Identifiers

PMID31911437
PMCPMC7039568
OpenAlexW2998775495

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.