Evidence map›Paper›PMID 38397158›Full record

ReviewGenes2024

The Intriguing Mystery of RPA Phosphorylation in DNA Double-Strand Break Repair.

Valerie J Fousek-Schuller, Gloria E O Borgstahl

Open access · goldAbstract readReview
In one paragraph

Review in Genes, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

7 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. DNA repair-associated nucleases induce double-strand breaks following sequential exposure to UVA1 and UVB.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2026
    Article
  3. RPA-independent activation of the ATR/CHK1 pathway.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Review
  6. Review
  7. 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

2 authors.

Valerie J Fousek-SchullerImmunology, Pathology, and Infectious Diseases, UNMC, Omaha, NE 68198-6805, USA.ORCID 0000-0001-6343-2343
Gloria E O BorgstahlEppley Institute for Research in Cancer & Allied Diseases, UNMC, Omaha, NE 68198-6805, USA.ORCID 0000-0001-8070-0258

Funding

UNMC Structural Biology CoreP20GM103427 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI Heather Colleen Jensen-Smith · 2012 to 2026
$59.2M
UNMC/EPPLEY CANCER CENTER SUPPORT GRANTP30CA036727 · NCI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI James Eudy · 1985 to 2026
$55.0M
NCI NIH HHS P30 CA036727NCI NIH HHS P30CA036727NIGMS NIH HHS P20 GM103427
6 · The paper itself

Abstract

Human Replication Protein A (RPA) was historically discovered as one of the six components needed to reconstitute simian virus 40 DNA replication from purified components. RPA is now known to be involved in all DNA metabolism pathways that involve single-stranded DNA (ssDNA). Heterotrimeric RPA comprises several domains connected by flexible linkers and is heavily regulated by post-translational modifications (PTMs). The structure of RPA has been challenging to obtain. Various structural methods have been applied, but a complete understanding of RPA's flexible structure, its function, and how it is regulated by PTMs has yet to be obtained. This review will summarize recent literature concerning how RPA is phosphorylated in the cell cycle, the structural analysis of RPA, DNA and protein interactions involving RPA, and how PTMs regulate RPA activity and complex formation in double-strand break repair. There are many holes in our understanding of this research area. We will conclude with perspectives for future research on how RPA PTMs control double-strand break repair in the cell cycle.

Indexed as

DNADNA Breaks, Double-StrandedDNA RepairReplication Protein ADNA, Single-StrandedHumansPhosphorylationDNADNA, Single-StrandedReplication Protein ARPA1 protein, humanAlphaFoldcell cycleDNA metabolismdouble-strand break repairhomologous recombinationphosphorylationprotein-ssDNA interactionsReplication Protein A (RPA)

Identifiers

PMID38397158
PMCPMC10888239
OpenAlexW4391314332

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.