Evidence map›Paper›PMID 37668474›Full record

ArticleeLife2023

Structural characterization of human RPA70N association with DNA damage response proteins.

Yeyao Wu, Wangmi Fu, Ning Zang, Chun Zhou

Open access · goldAbstract read
In one paragraph

Article in eLife, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

16 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. DNA Damage and Replication Stress Checkpoints.Annual review of biochemistry · 2025
    Review
  10. Review
  11. Rare SNP in theNAR molecular medicine · 2025
    Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Review
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.

Yeyao Wu *School of Public Health & Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Zhejiang, China.ORCID 0000-0003-1144-8508
Wangmi Fu *School of Public Health & Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Zhejiang, China.
Ning Zang *School of Public Health & Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Zhejiang, China.
Chun ZhouSchool of Public Health & Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Zhejiang, China.ORCID 0000-0002-9257-468X
Sir Run Run Shaw Hospital · CN

Funding

National Natural Science Foundation of China 31971125
6 · The paper itself

Abstract

The heterotrimeric Replication protein A (RPA) is the ubiquitous eukaryotic single-stranded DNA (ssDNA) binding protein and participates in nearly all aspects of DNA metabolism, especially DNA damage response. The N-terminal OB domain of the RPA70 subunit (RPA70N) is a major protein-protein interaction element for RPA and binds to more than 20 partner proteins. Previous crystallography studies of RPA70N with p53, DNA2 and PrimPol fragments revealed that RPA70N binds to amphipathic peptides that mimic ssDNA. NMR chemical-shift studies also provided valuable information on the interaction of RPA70N residues with target sequences. However, it is still unclear how RPA70N recognizes and distinguishes such a diverse group of target proteins. Here, we present high-resolution crystal structures of RPA70N in complex with peptides from eight DNA damage response proteins. The structures show that, in addition to the ssDNA mimicry mode of interaction, RPA70N employs multiple ways to bind its partners. Our results advance the mechanistic understanding of RPA70N-mediated recruitment of DNA damage response proteins.

Indexed as

DNA-Binding ProteinsDNA, Single-StrandedReplication Protein ACrystallographyDNA DamageDNA-Directed DNA PolymeraseDNA PrimaseEukaryotaHumansMultifunctional EnzymesDNA-Binding ProteinsDNA-Directed DNA PolymeraseDNA PrimaseDNA, Single-StrandedMultifunctional EnzymesPrimPol protein, humanReplication Protein ARPA1 protein, humanATRIPbiochemistryBLMchemical biologyHelBhumanmolecular biophysicsRMI1RPAstructural biologyWRN

Identifiers

PMID37668474
PMCPMC10479964
OpenAlexW4386437858

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.