Evidence map›Paper›PMID 22941596›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2012

Electrophoretic mobility shift assays for protein-DNA complexes involved in DNA repair.

Chun Tsai, Vaughn Smider, Byung Joon Hwang, Gilbert Chu

Abstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2012. 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
0.5field-weighted citation impact, top 31% 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, 6 citations in OpenAlex.

  1. Article
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  5. Review
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 at 3 institutions in 2 countries.

Chun TsaiDepartments of Medicine and Biochemistry, Stanford University Medical Center, Stanford, CA, USA.
Vaughn Smider
Byung Joon Hwang
Gilbert Chu
Stanford Medicine · USKangwon National University · KRScripps Research Institute · US

Funding

Molecular basis for ligation of mismatched DNA endsR01GM086579 · NIGMS · STANFORD UNIVERSITY · PI CHU, GILBERT · 2009 to 2012
$1.2M
NIGMS NIH HHS R01 GM086579
6 · The paper itself

Abstract

The electrophoretic mobility shift assay (EMSA) can be used to study proteins that bind to DNA structures created by DNA-damaging agents. UV-damaged DNA-binding protein (UV-DDB), which is involved in nucleotide excision repair, binds to DNA damaged by ultraviolet radiation or the anticancer drug cisplatin. Ku, XRCC4/Ligase IV, and DNA-PKcs, which are involved in the repair of DNA double-strand breaks by nonhomologous end joining, assemble in complexes at DNA ends. This chapter will describe several EMSA protocols for detecting different DNA repair protein-DNA complexes. To obtain additional information, one can apply variations of the EMSA, which include the reverse EMSA to detect binding of (35)S-labeled protein to damaged DNA, and the antibody supershift assay to detect the presence of a specific protein in the protein-DNA complex.

Indexed as

DNA RepairBuffersCell LineCell Line, TumorCell NucleusCisplatinCytoplasmDNADNA-Binding ProteinsDNA DamageDNA ProbesElectrophoretic Mobility Shift AssayExodeoxyribonucleasesHumansPolynucleotide 5'-Hydroxyl-KinaseUltraviolet RaysBuffersCisplatinDNADNA-Binding ProteinsDNA ProbesExodeoxyribonucleasesPolynucleotide 5'-Hydroxyl-Kinase

Identifiers

PMID22941596
PMCPMC4204632
OpenAlexW136956811

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.