Evidence map›Paper›PMID 39286502›Full record

ArticleiScience2024

Redox-dependent condensation and cytoplasmic granulation by human ssDNA-binding protein-1 delineate roles in oxidative stress response.

Gábor M Harami, János Pálinkás, Zoltán J Kovács, Bálint Jezsó, Krisztián Tárnok, Hajnalka Harami-Papp, József Hegedüs, Lamiya Mahmudova, Nóra Kucsma, Szilárd Tóth and 2 more

Abstract read
In one paragraph

Article in iScience, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Review
  2. Protein oxidation in crowded environments.The Biochemical journal · 2026
    Review
  3. Article
  4. 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

12 authors.

Gábor M HaramiELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Pázmány P. s. 1/c, 1117 Budapest, Hungary.
János PálinkásELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Pázmány P. s. 1/c, 1117 Budapest, Hungary.
Zoltán J KovácsELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Pázmány P. s. 1/c, 1117 Budapest, Hungary.
Bálint JezsóELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Pázmány P. s. 1/c, 1117 Budapest, Hungary.
Krisztián TárnokDepartment of Physiology and Neurobiology, Eötvös Loránd University, Pázmány P. s. 1/c, 1117 Budapest, Hungary.
Hajnalka Harami-PappELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Pázmány P. s. 1/c, 1117 Budapest, Hungary.
József HegedüsELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Pázmány P. s. 1/c, 1117 Budapest, Hungary.
Lamiya MahmudovaELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Pázmány P. s. 1/c, 1117 Budapest, Hungary.
Nóra KucsmaHUN-REN Institute of Molecular Life Sciences, Research Centre for Natural Sciences, Magyar Tudósok körútja 2, 1117 Budapest, Hungary.
Szilárd TóthHUN-REN Institute of Molecular Life Sciences, Research Centre for Natural Sciences, Magyar Tudósok körútja 2, 1117 Budapest, Hungary.
Gergely SzakácsHUN-REN Institute of Molecular Life Sciences, Research Centre for Natural Sciences, Magyar Tudósok körútja 2, 1117 Budapest, Hungary.
Mihály KovácsELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Pázmány P. s. 1/c, 1117 Budapest, Hungary.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human single-stranded DNA binding protein 1 (hSSB1/NABP2/OBFC2B) plays central roles in DNA repair. Here, we show that purified hSSB1 undergoes redox-dependent liquid-liquid phase separation (LLPS) in the presence of single-stranded DNA or RNA, features that are distinct from those of LLPS by bacterial SSB. hSSB1 nucleoprotein droplets form under physiological ionic conditions in response to treatment modeling cellular oxidative stress. hSSB1's intrinsically disordered region is indispensable for LLPS, whereas all three cysteine residues of the oligonucleotide/oligosaccharide-binding fold are necessary to maintain redox-sensitive droplet formation. Proteins interacting with hSSB1 show selective enrichment inside hSSB1 droplets, suggesting tight content control and recruitment functions for the condensates. While these features appear instrumental for genome repair, we detected cytoplasmic hSSB1 condensates in various cell lines colocalizing with stress granules upon oxidative stress, implying extranuclear function in cellular stress response. Our results suggest condensation-linked roles for hSSB1, linking genome repair and cytoplasmic defense.

Indexed as

Cell biologyMolecular biology

Identifiers

PMID39286502
PMCPMC11403420

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.