Evidence map›Paper›PMID 27372763›Full record

ArticleMethods in enzymology2016

Characterization of How DNA Modifications Affect DNA Binding by C2H2 Zinc Finger Proteins.

A Patel, H Hashimoto, X Zhang, X Cheng

Open access · greenAbstract read
In one paragraph

Article in Methods in enzymology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
8.1field-weighted citation impact, top 2% 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

24 citing papers in PubMed, 35 citations in OpenAlex.

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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 1 institution in 1 country.

A PatelEmory University School of Medicine, Atlanta, GA, United States.
H HashimotoEmory University School of Medicine, Atlanta, GA, United States.
X ZhangEmory University School of Medicine, Atlanta, GA, United States. Electronic address: xzhan02@emory.edu.
X ChengEmory University School of Medicine, Atlanta, GA, United States. Electronic address: xcheng@emory.edu.
Emory University · US

Funding

THREE-DIMENSIONAL STRUCTURE OF HHAI METHYLASER01GM049245 · NIGMS · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI CHENG, XIAODONG · 1993 to 2017
$6.6M
NIGMS NIH HHS R01 GM049245
6 · The paper itself

Abstract

Much is known about vertebrate DNA methylation and oxidation; however, much less is known about how modified cytosine residues within particular sequences are recognized. Among the known methylated DNA-binding domains, the Cys2-His2 zinc finger (ZnF) protein superfamily is the largest with hundreds of members, each containing tandem ZnFs ranging from 3 to >30 fingers. We have begun to biochemically and structurally characterize these ZnFs not only on their sequence specificity but also on their sensitivity to various DNA modifications. Rather than following published methods of refolding insoluble ZnF arrays, we have expressed and purified soluble forms of ZnFs, ranging in size from a tandem array of two to six ZnFs, from seven different proteins. We also describe a fluorescence polarization assay to measure ZnFs affinity with oligonucleotides containing various modifications and our approaches for cocrystallization of ZnFs with oligonucleotides.

Indexed as

CYS2-HIS2 Zinc FingersAnimalsBase SequenceCloning, MolecularCrystallizationDNADNA-Binding ProteinsDNA MethylationEscherichia coliHumansOligonucleotidesProtein BindingSpectrometry, FluorescenceDNADNA-Binding ProteinsOligonucleotidesC2H2 zinc fingerDNA methylationDNA modificationEpigeneticsIonic strengthPolyethylenimine

Identifiers

PMID27372763
PMCPMC4941819
OpenAlexW2488189578

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.