Evidence map›Paper›PMID 36820987›Full record

ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2023

Zinc binding of a Cys2His2-type zinc finger protein is enhanced by the interaction with DNA.

Bálint Hajdu, Éva Hunyadi-Gulyás, Kohsuke Kato, Atsushi Kawaguchi, Kyosuke Nagata, Béla Gyurcsik

Open access · hybridFull text read
In one paragraph

Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

7 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Review
  3. International journal of molecular sciences · 2025
    Article
  4. Article
  5. Review
  6. Article
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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

6 authors at 3 institutions in 2 countries.

Bálint HajduDepartment of Inorganic and Analytical Chemistry, University of Szeged, Dóm Tér 7, 6720, Szeged, Hungary.ORCID 0000-0003-4024-116X
Éva Hunyadi-GulyásLaboratory of Proteomics Research, Biological Research Centre, Eötvös Loránd Research Network (ELKH), Temesvári Krt. 62, 6726, Szeged, Hungary.ORCID 0000-0003-2089-1499
Kohsuke KatoDepartment of Infection Biology, Faculty of Medicine, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, 305-8575, Japan.
Atsushi KawaguchiDepartment of Infection Biology, Faculty of Medicine, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, 305-8575, Japan.ORCID 0000-0002-5485-1578
Kyosuke NagataDepartment of Infection Biology, Faculty of Medicine, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, 305-8575, Japan.ORCID 0000-0003-2522-3561
Béla GyurcsikDepartment of Inorganic and Analytical Chemistry, University of Szeged, Dóm Tér 7, 6720, Szeged, Hungary. gyurcsik@chem.u-szeged.hu.ORCID 0000-0003-1894-7414
University of Tsukuba · JPUniversity of Szeged · HUHUN-REN Szegedi Biológiai Kutatóközpont · HU

Funding

EU Horizon 2020 730872EU Horizon 2020 739593Hungarian National Research, Development and Innovation Office 2019-2.1111-TÉT-2019-00089Hungarian National Research, Development and Innovation Office GINOP-2.3.2-15-2016-00001Hungarian National Research, Development and Innovation Office GINOP-2.3.2-15-2016-00020Hungarian National Research, Development and Innovation Office GINOP-2.3.2-15-2016-00038Hungarian National Research, Development and Innovation Office K_16/120130
6 · The paper itself

Abstract

Zinc finger proteins specifically recognize DNA sequences and, therefore, play a crucial role in living organisms. In this study the Zn(II)-, and DNA-binding of 1MEY#, an artificial zinc finger protein consisting of three finger units was characterized by multiple methods. Fluorimetric, circular dichroism and isothermal calorimetric titrations were applied to determine the accurate stability constant of a zinc finger protein. Assuming that all three zinc finger subunits behave identically, the obtained thermodynamic data for the Zn(II) binding were ΔH

Indexed as

PeptidesZinc FingersBinding SitesDNAProtein BindingZincDNAPeptidesZincDNA bindingElectrophoretic mobility shift assayIsothermal titration calorimetryMass spectrometryZinc finger proteinZn(II)-affinity

Identifiers

PMID36820987
PMCPMC10036435
OpenAlexW4321600617

What Socratic holds

Textfull text, public
LicenceCC BY
measurements read58
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 Socratic graph.