Evidence map›Paper›PMID 34112944›Full record

ArticleCommunications biology2021

ATP biphasically modulates LLPS of TDP-43 PLD by specifically binding arginine residues.

Mei Dang, Liangzhong Lim, Jian Kang, Jianxing Song

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.9field-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

38 citing papers in PubMed, 63 citations in OpenAlex.

  1. Review
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  6. Protein oxidation in crowded environments.The Biochemical journal · 2026
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  7. Regulation of RNA-binding proteins by small biomolecules.Nature reviews. Molecular cell biology · 2026
    Review
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  9. Biomolecular Condensates Can Induce Local Membrane Potentials.Small (Weinheim an der Bergstrasse, Germany) · 2026
    Article
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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

4 authors at 1 institution in 1 country.

Mei DangDepartment of Biological Sciences, Faculty of Science, National University of Singapore, Singapore, Singapore.
Liangzhong LimDepartment of Biological Sciences, Faculty of Science, National University of Singapore, Singapore, Singapore.
Jian KangDepartment of Biological Sciences, Faculty of Science, National University of Singapore, Singapore, Singapore.ORCID 0000-0001-9935-4172
Jianxing SongDepartment of Biological Sciences, Faculty of Science, National University of Singapore, Singapore, Singapore. dbssjx@nus.edu.sg.ORCID 0000-0003-0224-6322
National University of Singapore · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mysteriously neurons maintain ATP concentrations of ~3 mM but whether ATP modulates TDP-43 LLPS remains completely unexplored. Here we characterized the effect of ATP on LLPS of TDP-43 PLD and seven mutants by DIC and NMR. The results revealed: 1) ATP induces and subsequently dissolves LLPS of TDP-43 PLD by specifically binding Arg saturated at 1:100. 2) ATP modifies the conformation-specific electrostatic property beyond just imposing screening effect. 3) Reversibility of LLPS of TDP-43 PLD and further exaggeration into aggregation appear to be controlled by a delicate network composed of both attractive and inhibitory interactions. Results together establish that ATP might be a universal but specific regulator for most, if not all, R-containing intrinsically-disordered regions by altering physicochemical properties, conformations, dynamics, LLPS and aggregation. Under physiological conditions, TDP-43 is highly bound with ATP and thus inhibited for LLPS, highlighting a central role of ATP in cell physiology, pathology and aging.

Indexed as

Adenosine TriphosphateArginineBinding SitesDNA-Binding ProteinsHumansMutationNeurodegenerative DiseasesPhase TransitionProtein AggregatesProtein BindingRecombinant ProteinsAdenosine TriphosphateArginineDNA-Binding ProteinsProtein AggregatesRecombinant ProteinsTARDBP protein, human

Identifiers

PMID34112944
PMCPMC8192790
OpenAlexW3165917655

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.