Evidence map›Paper›PMID 25053494›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2014

Analyzing the nuclear complexes of Notch signaling by electrophoretic mobility shift assay.

Kelly L Arnett, Stephen C Blacklow

Abstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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.

Kelly L ArnettDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 45 Shattuck St., Boston, MA, 02115, USA.
Stephen C Blacklow

Funding

Protein CoreP01CA119070 · NCI · BRIGHAM AND WOMEN'S HOSPITAL · PI ASTER, JON C. · 2006 to 2016
$10.3M
Structure and Function in Notch SignalingR01CA092433 · NCI · HARVARD MEDICAL SCHOOL · PI BLACKLOW, STEPHEN C. · 2002 to 2016
$5.0M
Structure and Function in Notch SignalingR56CA092433 · NCI · BRIGHAM AND WOMEN'S HOSPITAL · PI BLACKLOW, STEPHEN C. · 2008 to 2008
$392k
NCI NIH HHS CA-092433NCI NIH HHS CA-119070NCI NIH HHS P01 CA119070NCI NIH HHS R01 CA092433NCI NIH HHS R56 CA092433
6 · The paper itself

Abstract

An electrophoretic mobility shift assay (EMSA) is a sensitive technique for detecting protein-DNA and protein-protein interactions in which complexes are separated by native (non-denaturing) gel electrophoresis. EMSAs can provide evidence for specific binding between components prepared from a wide range of sources, including not only highly purified proteins but also components of crude cellular extracts. EMSA experiments were critical in identifying the minimal protein requirements for assembly of transcriptionally active nuclear Notch complexes as well as the DNA sequence specificity of Notch transcription complexes. Here, we describe a radioactive EMSA protocol for detection of Notch transcription complexes.

Indexed as

Cell NucleusDNAElectrophoretic Mobility Shift AssayEscherichia coliGene ExpressionHumansProtein BindingReceptors, NotchSignal TransductionTranscription, GeneticDNAReceptors, Notch

Identifiers

PMID25053494
PMCPMC4410701

What OpenQuestion holds

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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.