Evidence map›Paper›PMID 25774876›Full record

ArticleThe Biochemical journal2015

RECQ1 interacts with FEN-1 and promotes binding of FEN-1 to telomeric chromatin.

Furqan Sami, Xing Lu, Swetha Parvathaneni, Rabindra Roy, Ronald K Gary, Sudha Sharma

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed, 1 pooled it
1.7field-weighted citation impact, top 16% 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

14 citing papers in PubMed, 1 synthesis or guideline pooled it, 19 citations in OpenAlex.

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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 3 institutions in 1 country.

Furqan Sami*Department of Biochemistry and Molecular Biology, College of Medicine, Howard University, 520 W Street NW, Washington, DC 20059, U.S.A.
Xing Lu*Department of Biochemistry and Molecular Biology, College of Medicine, Howard University, 520 W Street NW, Washington, DC 20059, U.S.A.
Swetha Parvathaneni*Department of Biochemistry and Molecular Biology, College of Medicine, Howard University, 520 W Street NW, Washington, DC 20059, U.S.A.
Rabindra Roy†Department of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University Medical Center, 3800 Reservoir Road NW, Washington, DC 20057, U.S.A.
Ronald K Gary‡Department of Chemistry, University of Nevada, Las Vegas 4505 Maryland Parkway, Las Vegas, NV 89154-4003, U.S.A.
Sudha Sharma*Department of Biochemistry and Molecular Biology, College of Medicine, Howard University, 520 W Street NW, Washington, DC 20059, U.S.A.
Howard University · USGeorgetown University · USUniversity of Nevada, Las Vegas · US

Funding

PROTEOMICS CORE FACILITYG12MD007597 · NIMHD · HOWARD UNIVERSITY · PI SOUTHERLAND, WILLIAM M. · 2012 to 2018
$14.8M
Molecular Analysis of RECQ1 Functions in Genome MaintenanceSC1GM093999 · NIGMS · HOWARD UNIVERSITY · PI SHARMA, SUDHA · 2010 to 2019
$3.0M
Regulations of DNA Alkylation/Deamination Damage RepairR01CA092306 · NCI · INSTITUTE FOR CANCER PREVENTION · PI ROY, RABINDRA · 2003 to 2013
$2.8M
Interaction of BER proteins with DNA adducts in live human cellsR03ES022857 · NIEHS · GEORGETOWN UNIVERSITY · PI ROY, RABINDRA · 2014 to 2015
$151k
NCI NIH HHS R01 CA092306NIEHS NIH HHS R03 ES022857NIGMS NIH HHS 5SC1 GM093999-05NIGMS NIH HHS SC1 GM093999NIMHD NIH HHS G12 MD007597
6 · The paper itself

Abstract

RecQ helicases are a family of highly conserved proteins that maintain genomic stability through their important roles in replication restart mechanisms. Cellular phenotypes of RECQ1 deficiency are indicative of aberrant repair of stalled replication forks, but the molecular functions of RECQ1, the most abundant of the five known human RecQ homologues, have remained poorly understood. We show that RECQ1 associates with FEN-1 (flap endonuclease-1) in nuclear extracts and exhibits direct protein interaction in vitro. Recombinant RECQ1 significantly stimulated FEN-1 endonucleolytic cleavage of 5'-flap DNA substrates containing non-telomeric or telomeric repeat sequence. RECQ1 and FEN-1 were constitutively present at telomeres and their binding to the telomeric chromatin was enhanced following DNA damage. Telomere residence of FEN-1 was dependent on RECQ1 since depletion of RECQ1 reduced FEN-1 binding to telomeres in unperturbed cycling cells. Our results confirm a conserved collaboration of human RecQ helicases with FEN-1 and suggest both overlapping and specialized roles of RECQ1 in the processing of DNA structure intermediates proposed to arise during replication, repair and recombination.

Indexed as

ChromatinChromatin ImmunoprecipitationDNA DamageDNA ReplicationFlap EndonucleasesHeLa CellsHumansProtein BindingRecQ HelicasesTelomereChromatinFEN1 protein, humanFlap EndonucleasesRecQ HelicasesRECQL protein, human

Identifiers

PMID25774876
PMCPMC4441847
OpenAlexW2135911824

What OpenQuestion holds

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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.