Evidence map›Paper›PMID 16523492›Full record

ReviewJournal of cellular physiology2006

Functions of human replication protein A (RPA): from DNA replication to DNA damage and stress responses.

Yue Zou, Yiyong Liu, Xiaoming Wu, Steven M Shell

Open access · bronzeAbstract readReview
In one paragraph

Review in Journal of cellular physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 219 papers.

0numbers the graph read from it
0cells of the map it votes in
219citing papers in PubMed
7.6field-weighted citation impact, top 2% 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

219 citing papers in PubMed, 375 citations in OpenAlex.

  1. Article
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  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. PLK1 phosphorylates WRN at replication forks.The Journal of pharmacology and experimental therapeutics · 2025
    Article
  13. Article
  14. Article
  15. DNA repair and anti-cancer mechanisms in the long-lived bowhead whale.bioRxiv : the preprint server for biology · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. A perspective on tumor radiation resistance following high-LET radiation treatment.Journal of cancer research and clinical oncology · 2024
    Review

159 more citing papers are in PubMed but not listed here.

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.

Yue ZouDepartment of Biochemistry and Molecular Biology, James H. Quillen College of Medicine, East Tennessee State University, Johnson City, Tennessee 37614, USA. zouy@etsu.edu
Yiyong Liu
Xiaoming Wu
Steven M Shell
East Tennessee State University · US

Funding

RECOGNITION AND REPAIR OF UV DAMAGE TO HUMAN DNAR01CA086927 · NCI · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI ZOU, YUE · 2000 to 2011
$2.2M
Checkpoint Signaling and Repair of UV Damage to Human DNAR56CA086927 · NCI · EAST TENNESSEE STATE UNIVERSITY · PI ZOU, YUE · 2007 to 2007
$231k
NCI NIH HHS CA86927NCI NIH HHS R01 CA086927NCI NIH HHS R56 CA086927
6 · The paper itself

Abstract

Human replication protein A (RPA), a heterotrimeric protein complex, was originally defined as a eukaryotic single-stranded DNA binding (SSB) protein essential for the in vitro replication of simian virus 40 (SV40) DNA. Since then RPA has been found to be an indispensable player in almost all DNA metabolic pathways such as, but not limited to, DNA replication, DNA repair, recombination, cell cycle, and DNA damage checkpoints. Defects in these cellular reactions may lead to genome instability and, thus, the diseases with a high potential to evolve into cancer. This extensive involvement of RPA in various cellular activities implies a potential modulatory role for RPA in cellular responses to genotoxic insults. In support, RPA is hyperphosphorylated upon DNA damage or replication stress by checkpoint kinases including ataxia telangiectasia mutated (ATM), ATR (ATM and Rad3-related), and DNA-dependent protein kinase (DNA-PK). The hyperphosphorylation may change the functions of RPA and, thus, the activities of individual pathways in which it is involved. Indeed, there is growing evidence that hyperphosphorylation alters RPA-DNA and RPA-protein interactions. In addition, recent advances in understanding the molecular basis of the stress-induced modulation of RPA functions demonstrate that RPA undergoes a subtle structural change upon hyperphosphorylation, revealing a structure-based modulatory mechanism. Furthermore, given the crucial roles of RPA in a broad range of cellular processes, targeting RPA to inhibit its specific functions, particularly in DNA replication and repair, may serve a valuable strategy for drug development towards better cancer treatment.

Indexed as

DNA DamageDNA ReplicationCell Cycle ProteinsDNA, Single-StrandedHumansModels, BiologicalPhosphorylationProtein Structure, TertiaryRecombination, GeneticReplication Protein ACell Cycle ProteinsDNA, Single-StrandedReplication Protein A

Identifiers

PMID16523492
PMCPMC3107514
OpenAlexW2010869413

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.