Evidence map›Paper›PMID 21325134›Full record

ArticleGenes & development2011

BLM-DNA2-RPA-MRN and EXO1-BLM-RPA-MRN constitute two DNA end resection machineries for human DNA break repair.

Amitabh V Nimonkar, Jochen Genschel, Eri Kinoshita, Piotr Polaczek, Judith L Campbell, Claire Wyman, Paul Modrich, Stephen C Kowalczykowski

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 481 papers.

0numbers the graph read from it
0cells of the map it votes in
481citing papers in PubMed
–field-weighted citation impact
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

481 citing papers in PubMed, 731 citations in OpenAlex.

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421 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

8 authors at 5 institutions in 2 countries.

Amitabh V NimonkarDepartment of Microbiology, University of California at Davis, Davis, California 95616, USA.
Jochen Genschel
Eri Kinoshita
Piotr Polaczek
Judith L Campbell
Claire Wyman
Paul Modrich
Stephen C Kowalczykowski
California Institute of Technology · USErasmus MC · NLUniversity of California, Davis · USDuke Medical Center · USDuke University Hospital · US

Funding

Biochemical Mechanisms and Function of DNA HelicasesR01GM041347 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI KOWALCZYKOWSKI, STEPHEN CHARLES · 1989 to 2018
$7.6M
Enzymology Of Eukaryotic Mismatch RepairR01GM045190 · NIGMS · DUKE UNIVERSITY · PI MODRICH, PAUL LAWRENCE · 1991 to 2018
$6.8M
Mechanistic Studies of Genetic RecombinationR01GM062653 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI KOWALCZYKOWSKI, STEPHEN CHARLES · 2010 to 2018
$4.4M
MECHANISTIC STUDIES OF GENETIC RECOMBINATIONR37GM062653 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI KOWALCZYKOWSKI, STEPHEN CHARLES · 2000 to 2009
$3.6M
Enzyme Interactions at the DNA Replication ForkR01GM078666 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI CAMPBELL, JUDITH L · 2006 to 2009
$1.5M
Howard Hughes Medical InstituteNCI NIH HHS 5P01CA092548NIGMS NIH HHS GM-45190NIGMS NIH HHS GM-62653NIGMS NIH HHS GM-78666NIGMS NIH HHS R01 GM041347NIGMS NIH HHS R01 GM045190NIGMS NIH HHS R01 GM062653NIGMS NIH HHS R01 GM078666NIGMS NIH HHS R37 GM062653
6 · The paper itself

Abstract

Repair of dsDNA breaks requires processing to produce 3'-terminated ssDNA. We biochemically reconstituted DNA end resection using purified human proteins: Bloom helicase (BLM); DNA2 helicase/nuclease; Exonuclease 1 (EXO1); the complex comprising MRE11, RAD50, and NBS1 (MRN); and Replication protein A (RPA). Resection occurs via two routes. In one, BLM and DNA2 physically and specifically interact to resect DNA in a process that is ATP-dependent and requires BLM helicase and DNA2 nuclease functions. RPA is essential for both DNA unwinding by BLM and enforcing 5' → 3' resection polarity by DNA2. MRN accelerates processing by recruiting BLM to the end. In the other, EXO1 resects the DNA and is stimulated by BLM, MRN, and RPA. BLM increases the affinity of EXO1 for ends, and MRN recruits and enhances the processivity of EXO1. Our results establish two of the core machineries that initiate recombinational DNA repair in human cells.

Indexed as

DNA Breaks, Double-StrandedAcid Anhydride HydrolasesCell Cycle ProteinsDNA-Binding ProteinsDNA Breaks, Single-StrandedDNA HelicasesDNA RepairDNA Repair EnzymesExodeoxyribonucleasesHumansIn Vitro TechniquesModels, BiologicalMRE11 Homologue ProteinMultiprotein ComplexesNuclear ProteinsProtein BindingAcid Anhydride HydrolasesBloom syndrome proteinCell Cycle ProteinsDNA2 protein, humanDNA-Binding ProteinsDNA HelicasesDNA Repair Enzymesexodeoxyribonuclease IExodeoxyribonucleasesMRE11 Homologue ProteinMRE11 protein, humanMultiprotein ComplexesNBN protein, humanNuclear ProteinsRAD50 protein, humanRecQ HelicasesReplication Protein A

Identifiers

PMID21325134
PMCPMC3042158
OpenAlexW2117602431

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.