Evidence map›Paper›PMID 33121960›Full record

ReviewProgress in biophysics and molecular biology2021

The dynamic nature of the Mre11-Rad50 DNA break repair complex.

Mahtab Beikzadeh, Michael P Latham

Open access · hybridAbstract readReview
In one paragraph

Review in Progress in biophysics and molecular biology, 2021. 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
0.3field-weighted citation impact, top 42% 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

5 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  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

2 authors at 1 institution in 1 country.

Mahtab BeikzadehDepartment of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX, USA.
Michael P LathamDepartment of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX, USA. Electronic address: michael.latham@ttu.edu.
Texas Tech University · US

Funding

Structural Biology Studies of a Large DNA Repair ComplexR35GM128906 · NIGMS · UNIVERSITY OF MINNESOTA · PI Michael Parker Latham · 2018 to 2026
$3.1M
NIGMS NIH HHS R35 GM128906
6 · The paper itself

Abstract

The Mre11-Rad50-Nbs1/Xrs2 protein complex plays a pivotal role in the detection and repair of DNA double strand breaks. Through traditional and emerging structural biology techniques, various functional structural states of this complex have been visualized; however, relatively little is known about the transitions between these states. Indeed, it is these structural transitions that are important for Mre11-Rad50-mediated DNA unwinding at a break and the activation of downstream repair signaling events. Here, we present a brief overview of the current understanding of the structure of the core Mre11-Rad50 complex. We then highlight our recent studies emphasizing the contributions of solution state NMR spectroscopy and other biophysical techniques in providing insight into the structures and dynamics associated with Mre11-Rad50 functions.

Indexed as

Cell Cycle ProteinsDNA-Binding ProteinsDNA RepairMRE11 Homologue ProteinDNA Breaks, Double-StrandedCell Cycle ProteinsDNA-Binding ProteinsMRE11 Homologue ProteinAllosteryDNA double Strand break repairDNA repairMethyl TROSYMre11-Rad50-Nbs1NMR spectroscopy

Identifiers

PMID33121960
PMCPMC8065065
OpenAlexW3094704720

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.