Evidence map›Paper›PMID 21908891›Full record

ArticleThe Journal of biological chemistry2011

The multi-zinc finger protein ZNF217 contacts DNA through a two-finger domain.

Noelia Nunez, Molly M K Clifton, Alister P W Funnell, Crisbel Artuz, Samantha Hallal, Kate G R Quinlan, Josep Font, Marylène Vandevenne, Surya Setiyaputra, Richard C M Pearson and 2 more

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
0.5field-weighted citation impact, top 35% 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

26 citing papers in PubMed, 36 citations in OpenAlex.

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  11. Structural Evaluation and Conformational Dynamics ofBioengineering (Basel, Switzerland) · 2022
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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

12 authors at 2 institutions in 1 country.

Noelia NunezSchool of Molecular Bioscience, University of Sydney, New South Wales 2006, Australia.
Molly M K CliftonSchool of Molecular Bioscience, University of Sydney, New South Wales 2006, Australia.
Alister P W FunnellSchool of Molecular Bioscience, University of Sydney, New South Wales 2006, Australia; School of Biotechnology and Biomolecular Sciences, University of New South Wales, New South Wales 2052, Australia.
Crisbel ArtuzSchool of Biotechnology and Biomolecular Sciences, University of New South Wales, New South Wales 2052, Australia.
Samantha HallalSchool of Molecular Bioscience, University of Sydney, New South Wales 2006, Australia.
Kate G R QuinlanSchool of Molecular Bioscience, University of Sydney, New South Wales 2006, Australia.
Josep FontSchool of Molecular Bioscience, University of Sydney, New South Wales 2006, Australia.
Marylène VandevenneSchool of Molecular Bioscience, University of Sydney, New South Wales 2006, Australia.
Surya SetiyaputraSchool of Molecular Bioscience, University of Sydney, New South Wales 2006, Australia.
Richard C M PearsonSchool of Molecular Bioscience, University of Sydney, New South Wales 2006, Australia; School of Biotechnology and Biomolecular Sciences, University of New South Wales, New South Wales 2052, Australia.
Joel P MackaySchool of Molecular Bioscience, University of Sydney, New South Wales 2006, Australia.
Merlin CrossleySchool of Molecular Bioscience, University of Sydney, New South Wales 2006, Australia; School of Biotechnology and Biomolecular Sciences, University of New South Wales, New South Wales 2052, Australia. Electronic address: m.crossley@unsw.edu.au.
University of Sydney · AUUNSW Sydney · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Classical C2H2 zinc finger proteins are among the most abundant transcription factors found in eukaryotes, and the mechanisms through which they recognize their target genes have been extensively investigated. In general, a tandem array of three fingers separated by characteristic TGERP links is required for sequence-specific DNA recognition. Nevertheless, a significant number of zinc finger proteins do not contain a hallmark three-finger array of this type, raising the question of whether and how they contact DNA. We have examined the multi-finger protein ZNF217, which contains eight classical zinc fingers. ZNF217 is implicated as an oncogene and in repressing the E-cadherin gene. We show that two of its zinc fingers, 6 and 7, can mediate contacts with DNA. We examine its putative recognition site in the E-cadherin promoter and demonstrate that this is a suboptimal site. NMR analysis and mutagenesis is used to define the DNA binding surface of ZNF217, and we examine the specificity of the DNA binding activity using fluorescence anisotropy titrations. Finally, sequence analysis reveals that a variety of multi-finger proteins also contain two-finger units, and our data support the idea that these may constitute a distinct subclass of DNA recognition motif.

Indexed as

Amino Acid MotifsBinding SitesCell NucleusDNAGene Expression RegulationHEK293 CellsHumansMagnetic Resonance SpectroscopyModels, MolecularProtein BindingProtein Interaction MappingProtein Structure, TertiaryTrans-ActivatorsTranscription, GeneticZinc FingersDNATrans-ActivatorsZNF217 protein, human

Identifiers

PMID21908891
PMCPMC3207412
OpenAlexW2003218490

What OpenQuestion holds

Textmetadata
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.