Evidence map›Paper›PMID 30260704›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2019

PML-like subnuclear bodies, containing XRCC1, juxtaposed to DNA replication-based single-strand breaks.

Magdalena M Kordon, Aleksander Szczurek, Krzysztof Berniak, Oskar Szelest, Kamil Solarczyk, Magdalena Tworzydło, Sebastian Wachsmann-Hogiu, Anne Vaahtokari, Christoph Cremer, Thoru Pederson and 1 more

Open access · greenAbstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

10 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. USP7 at PML Nuclear Bodies: A Protein Interaction Network Perspective.International journal of molecular sciences · 2026
    Article
  4. Poly (ADP-Ribose) Glycohydrolase-Dependent dePARylation of PCNA Is Essential for DNA Replication.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. The cell nucleus. A study in Burgundy.Nucleus (Austin, Tex.) · 2019
    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

11 authors at 5 institutions in 4 countries.

Magdalena M KordonDepartment of Cell Biophysics, Faculty of Biochemistry, Biophysics, and Biotechnology, Jagiellonian University, Kraków, Poland.
Aleksander SzczurekDepartment of Cell Biophysics, Faculty of Biochemistry, Biophysics, and Biotechnology, Jagiellonian University, Kraków, Poland.
Krzysztof BerniakDepartment of Cell Biophysics, Faculty of Biochemistry, Biophysics, and Biotechnology, Jagiellonian University, Kraków, Poland.
Oskar SzelestDepartment of Cell Biophysics, Faculty of Biochemistry, Biophysics, and Biotechnology, Jagiellonian University, Kraków, Poland.
Kamil SolarczykDepartment of Cell Biophysics, Faculty of Biochemistry, Biophysics, and Biotechnology, Jagiellonian University, Kraków, Poland.
Magdalena TworzydłoDepartment of Physical Biochemistry, Faculty of Biochemistry, Biophysics, and Biotechnology, Jagiellonian University, Kraków, Poland.
Sebastian Wachsmann-HogiuDepartment of Pathology and Laboratory Medicine, University of California at Davis, Davis, California, USA.
Anne VaahtokariThe Francis Crick Institute, Cancer Research UK, London, United Kingdom; and.
Christoph CremerSuperresolution Microscopy Group, Institute of Molecular Biology, Mainz, Germany.
Thoru PedersonDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts, USA.
Jurek W DobruckiDepartment of Cell Biophysics, Faculty of Biochemistry, Biophysics, and Biotechnology, Jagiellonian University, Kraków, Poland.
Jagiellonian University · PLCancer Research UK · GBInstitute of Molecular Biology · DEUniversity of California, Davis · USUniversity of Massachusetts Chan Medical School · US

Funding

Nucleolar Genomics During Early Mammalian DevelopmentU01DA040588 · NIDA · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI KAUFMAN, PAUL D., PEDERSON, THORU · 2015 to 2019
$2.2M
NIDA NIH HHS U01 DA040588
6 · The paper itself

Abstract

DNA lesions induce recruitment and accumulation of various repair factors, resulting in formation of discrete nuclear foci. Using superresolution fluorescence microscopy as well as live cell and quantitative imaging, we demonstrate that X-ray repair cross-complementing protein 1 (XRCC1), a key factor in single-strand break and base excision repair, is recruited into nuclear bodies formed in response to replication-related single-strand breaks. Intriguingly, these bodies are assembled immediately in the vicinity of these breaks and never fully colocalize with replication foci. They are structurally organized, containing canonical promyelocytic leukemia (PML) nuclear body protein SP100 concentrated in a peripheral layer, and XRCC1 in the center. They also contain other factors, including PML, poly(ADP-ribose) polymerase 1 (PARP1), ligase IIIα, and origin recognition complex subunit 5. The breast cancer 1 and -2 C terminus domains of XRCC1 are essential for formation of these repair foci. These results reveal that XRCC1-contaning foci constitute newly recognized PML-like nuclear bodies that accrete and locally deliver essential factors for repair of single-strand DNA breaks in replication regions.-Kordon, M. M., Szczurek, A., Berniak, K., Szelest, O., Solarczyk, K., Tworzydło, M., Wachsmann-Hogiu, S., Vaahtokari, A., Cremer, C., Pederson, T., Dobrucki, J. W. PML-like subnuclear bodies, containing XRCC1, juxtaposed to DNA replication-based single-strand breaks.

Indexed as

DNA Breaks, Single-StrandedDNA ReplicationAntigens, NuclearAutoantigensCell NucleusCells, CulturedDNA RepairHeLa CellsHumansOrigin Recognition ComplexPoly (ADP-Ribose) Polymerase-1Promyelocytic Leukemia ProteinProtein DomainsX-ray Repair Cross Complementing Protein 1Antigens, NuclearAutoantigensORC5 protein, humanOrigin Recognition ComplexPARP1 protein, humanPML protein, humanPoly (ADP-Ribose) Polymerase-1Promyelocytic Leukemia ProteinSP100 protein, humanX-ray Repair Cross Complementing Protein 1XRCC1 protein, humanDNA damagePML nuclear bodiessuperresolution microscopy

Identifiers

PMID30260704
PMCPMC6993927
OpenAlexW2894525431

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.