Evidence map›Paper›PMID 28257700›Full record

ArticleMolecular cell2017

Functions of Replication Protein A as a Sensor of R Loops and a Regulator of RNaseH1.

Hai Dang Nguyen, Tribhuwan Yadav, Sumanprava Giri, Borja Saez, Timothy A Graubert, Lee Zou

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 198 papers.

0numbers the graph read from it
0cells of the map it votes in
198citing papers in PubMed
11.2field-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

198 citing papers in PubMed, 267 citations in OpenAlex.

  1. Article
  2. Mechanisms and disease relevance of DNA break repair pathway choice.Nature reviews. Molecular cell biology · 2026
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138 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

6 authors at 1 institution in 1 country.

Hai Dang NguyenMassachusetts General Hospital Cancer Center, Harvard Medical School, Charlestown, MA 02129, USA.
Tribhuwan YadavMassachusetts General Hospital Cancer Center, Harvard Medical School, Charlestown, MA 02129, USA.
Sumanprava GiriMassachusetts General Hospital Cancer Center, Harvard Medical School, Charlestown, MA 02129, USA.
Borja SaezMassachusetts General Hospital Cancer Center, Harvard Medical School, Charlestown, MA 02129, USA.
Timothy A GraubertMassachusetts General Hospital Cancer Center, Harvard Medical School, Charlestown, MA 02129, USA.
Lee ZouMassachusetts General Hospital Cancer Center, Harvard Medical School, Charlestown, MA 02129, USA; Department of Pathology, Massachusetts General Hospital, Harvard Medical School, Boston, MA 02114, USA. Electronic address: zou.lee@mgh.harvard.edu.
Harvard University · US

Funding

XRAY CRYSTALLOGRAPHIC STRUCTURE ANALYSIS: PROTEIN SORTINGP41RR001081 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 1985 to 2011
$17.6M
TRAINING IN CELL STRUCTURE AND FUNCTION IN NEPHROLOGYT32DK007540 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI BROWN, DENNIS, SOBERMAN, ROY · 1986 to 2021
$7.2M
Regulation of the ATR Checkpoint Kinase by DNA DamageR01GM076388 · NIGMS · MASSACHUSETTS GENERAL HOSPITAL · PI ZOU, LEE · 2006 to 2018
$4.3M
Implications of the ATR Checkpoint Kinase in Radiation and Targeted TherapiesR01CA197779 · NCI · MASSACHUSETTS GENERAL HOSPITAL · PI ZOU, LEE · 2015 to 2020
$2.4M
NCI NIH HHS R01 CA197779NCRR NIH HHS P41 RR001081NIDDK NIH HHS T32 DK007540NIGMS NIH HHS R01 GM076388
6 · The paper itself

Abstract

R loop, a transcription intermediate containing RNA:DNA hybrids and displaced single-stranded DNA (ssDNA), has emerged as a major source of genomic instability. RNaseH1, which cleaves the RNA in RNA:DNA hybrids, plays an important role in R loop suppression. Here we show that replication protein A (RPA), an ssDNA-binding protein, interacts with RNaseH1 and colocalizes with both RNaseH1 and R loops in cells. In vitro, purified RPA directly enhances the association of RNaseH1 with RNA:DNA hybrids and stimulates the activity of RNaseH1 on R loops. An RPA binding-defective RNaseH1 mutant is not efficiently stimulated by RPA in vitro, fails to accumulate at R loops in cells, and loses the ability to suppress R loops and associated genomic instability. Thus, in addition to sensing DNA damage and replication stress, RPA is a sensor of R loops and a regulator of RNaseH1, extending the versatile role of RPA in suppression of genomic instability.

Indexed as

Genomic InstabilityTranscription, GeneticBinding SitesDNAHEK293 CellsHeLa CellsHumansNucleic Acid ConformationProtein BindingProtein Interaction Domains and MotifsReplication Protein ARibonuclease HRNARNA InterferenceStructure-Activity RelationshipTime FactorsDNAReplication Protein ARibonuclease Hribonuclease HIRNARPA1 protein, humangenome instabilityR loopRNase H1RPAsplicing inhibitorsplicing mutationssDNA

Identifiers

PMID28257700
PMCPMC5507214
OpenAlexW2594603678

What OpenQuestion holds

Textmetadata
LicenceTDM
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.