Evidence map›Paper›PMID 31147924›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2019

Purification and Biophysical Characterization of the Mre11-Rad50-Nbs1 Complex.

Logan R Myler, Michael M Soniat, Xiaoming Zhang, Rajashree A Deshpande, Tanya T Paull, Ilya J Finkelstein

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
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.

Logan R MylerDepartment of Molecular Biosciences and Institute for Cellular and Molecular Biology, The University of Texas at Austin, Austin, TX, USA.
Michael M SoniatDepartment of Molecular Biosciences and Institute for Cellular and Molecular Biology, The University of Texas at Austin, Austin, TX, USA.
Xiaoming ZhangDepartment of Molecular Biosciences and Institute for Cellular and Molecular Biology, The University of Texas at Austin, Austin, TX, USA.
Rajashree A DeshpandeDepartment of Molecular Biosciences and Institute for Cellular and Molecular Biology, The University of Texas at Austin, Austin, TX, USA.
Tanya T PaullDepartment of Molecular Biosciences and Institute for Cellular and Molecular Biology, The University of Texas at Austin, Austin, TX, USA.
Ilya J FinkelsteinDepartment of Molecular Biosciences and Institute for Cellular and Molecular Biology, The University of Texas at Austin, Austin, TX, USA. ifinkelstein@cm.utexas.edu.

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI WALTER J. CHAZIN · 2001 to 2026
$89.6M
Mechanistic Characterization of the First Steps of Human DNA Break RepairR01GM120554 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI FINKELSTEIN, ILYA J · 2016 to 2020
$1.5M
Single-Molecule Studies of Human DNA Double Strand Break RepairK00CA212452 · NCI · ROCKEFELLER UNIVERSITY · PI MYLER, LOGAN ROSS · 2018 to 2021
$376k
Single-Molecule Studies of Human DNA Double Strand Break RepairF99CA212452 · NCI · UNIVERSITY OF TEXAS AT AUSTIN · PI MYLER, LOGAN ROSS · 2016 to 2017
$69k
NCI NIH HHS F99 CA212452NCI NIH HHS K00 CA212452NCI NIH HHS P01 CA092584NIGMS NIH HHS R01 GM120554
6 · The paper itself

Abstract

The Mre11-Rad50-Nbs1 (MRN) complex coordinates the repair of DNA double-strand breaks, replication fork restart, meiosis, class-switch recombination, and telomere maintenance. As such, MRN is an essential molecular machine that has homologs in all organisms of life, from bacteriophage to humans. In human cells, MRN is a >500 kDa multifunctional complex that encodes DNA binding, ATPase, and both endonuclease and exonuclease activities. MRN also forms larger assemblies and interacts with multiple DNA repair and replication factors. The enzymatic properties of MRN have been the subject of intense research for over 20 years, and more recently, single-molecule biophysics studies are beginning to probe its many biochemical activities. Here, we describe the methods used to overexpress, fluorescently label, and visualize MRN and its activities on single molecules of DNA.

Indexed as

Acid Anhydride HydrolasesAdenosine TriphosphatasesCell Cycle ProteinsDNADNA-Binding ProteinsDNA Breaks, Double-StrandedDNA RepairDNA ReplicationHumansMeiosisMRE11 Homologue ProteinNuclear ProteinsAcid Anhydride HydrolasesAdenosine TriphosphatasesCell Cycle ProteinsDNADNA-Binding ProteinsMRE11 Homologue ProteinMRE11 protein, humanNBN protein, humanNuclear ProteinsRAD50 protein, humanDNA curtainsDNA repairHomologous recombinationMRNSingle-molecule imaging

Identifiers

PMID31147924
PMCPMC6667175

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Registered trials

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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.