Evidence map›Paper›PMID 28668119›Full record

ArticleMethods in enzymology2017

DNA-PKcs, Allostery, and DNA Double-Strand Break Repair: Defining the Structure and Setting the Stage.

Dimitri Y Chirgadze, David B Ascher, Tom L Blundell, Bancinyane L Sibanda

Abstract read
In one paragraph

Article in Methods in enzymology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Dimers of DNA-PK create a stage for DNA double-strand break repair.Nature structural & molecular biology · 2021
    Article
  3. Article
  4. 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

4 authors.

Dimitri Y ChirgadzeUniversity of Cambridge, Cambridge, United Kingdom.
David B AscherUniversity of Cambridge, Cambridge, United Kingdom.
Tom L BlundellUniversity of Cambridge, Cambridge, United Kingdom. Electronic address: tlb20@cam.ac.uk.
Bancinyane L SibandaUniversity of Cambridge, Cambridge, United Kingdom.

Funding

Wellcome TrustWellcome Trust 093167/Z/10/Z
6 · The paper itself

Abstract

DNA-dependent protein kinase catalytic subunit (DNA-PKcs) is central to the regulation of the DNA damage response and repair through nonhomologous end joining. The structure has proved challenging due to its large size and multiple HEAT repeats. We have recently reported crystals of selenomethionine-labeled DNA-PKcs complexed with native KU80ct

Indexed as

Allosteric RegulationAmino Acid SequenceCrystallography, X-RayDNA-Activated Protein KinaseDNA Breaks, Double-StrandedDNA End-Joining RepairHeLa CellsHumansModels, MolecularNuclear ProteinsProtein ConformationRepetitive Sequences, Amino AcidSelenomethionineSequence AlignmentDNA-Activated Protein KinaseNuclear ProteinsPRKDC protein, humanSelenomethionineAnomalous scatteringDNA-dependent protein kinaseSelenomethinione labelingStage for assembly of NHEJ

Identifiers

PMID28668119
PMCPMC5495172

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.