Evidence map›Paper›PMID 16935876›Full record

ReviewNucleic acids research2006

A dynamic model for replication protein A (RPA) function in DNA processing pathways.

Ellen Fanning, Vitaly Klimovich, Andrew R Nager

Open access · goldAbstract readReview
In one paragraph

Review in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 370 papers.

0numbers the graph read from it
0cells of the map it votes in
370citing papers in PubMed
13.6field-weighted citation impact, top 1% 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

370 citing papers in PubMed, 568 citations in OpenAlex.

  1. Article
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  7. Slippage reconfiguration of trinucleotide repeat hairpins impedes resolution by human replication protein A.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  12. Review
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  20. The canonical RPA complex interacts with Est3 to regulate yeast telomerase activity.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article

310 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

3 authors at 1 institution in 1 country.

Ellen FanningDepartment of Biological Sciences, Vanderbilt University, VU Station B 351634, Nashville, TN 37235-1634, USA. ellen.fanning@vanderbilt.edu
Vitaly Klimovich
Andrew R Nager
Vanderbilt University · US

Funding

CONTROL OF SIMIAN VIRUS 40 AND CELLULAR DNA REPLICATIONR01GM052948 · NIGMS · VANDERBILT UNIVERSITY · PI FRIEDMAN, KATHERINE LOUISE · 1995 to 2013
$6.1M
NIGMS NIH HHS GM52948NIGMS NIH HHS R01 GM052948
6 · The paper itself

Abstract

Processing of DNA in replication, repair and recombination pathways in cells of all organisms requires the participation of at least one major single-stranded DNA (ssDNA)-binding protein. This protein protects ssDNA from nucleolytic damage, prevents hairpin formation and blocks DNA reannealing until the processing pathway is successfully completed. Many ssDNA-binding proteins interact physically and functionally with a variety of other DNA processing proteins. These interactions are thought to temporally order and guide the parade of proteins that 'trade places' on the ssDNA, a model known as 'hand-off', as the processing pathway progresses. How this hand-off mechanism works remains poorly understood. Recent studies of the conserved eukaryotic ssDNA-binding protein replication protein A (RPA) suggest a novel mechanism by which proteins may trade places on ssDNA by binding to RPA and mediating conformation changes that alter the ssDNA-binding properties of RPA. This article reviews the structure and function of RPA, summarizes recent studies of RPA in DNA replication and other DNA processing pathways, and proposes a general model for the role of RPA in protein-mediated hand-off.

Indexed as

DNADNA-Binding ProteinsDNA ReplicationDNA, Single-StrandedModels, BiologicalProtein ConformationReplication Protein ASaccharomyces cerevisiaeDNADNA-Binding ProteinsDNA, Single-StrandedReplication Protein A

Identifiers

PMID16935876
PMCPMC1616954
OpenAlexW2135453449

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.