Evidence map›Paper›PMID 26792893›Full record

ArticleNucleic acids research2016

Solution structure of the Z-DNA binding domain of PKR-like protein kinase from Carassius auratus and quantitative analyses of the intermediate complex during B-Z transition.

Ae-Ree Lee, Chin-Ju Park, Hae-Kap Cheong, Kyoung-Seok Ryu, Jin-Wan Park, Mun-Young Kwon, Janghyun Lee, Kyeong Kyu Kim, Byong-Seok Choi, Joon-Hwa Lee

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

17 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. NMR Titration Studies in Z-DNA Dynamics.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  9. Review
  10. Salt Dependence of DNA Binding Activity of Human Transcription Factor Dlx3.International journal of molecular sciences · 2022
    Article
  11. Article
  12. Article
  13. Dynamics Studies of DNA with Non-canonical Structure Using NMR Spectroscopy.International journal of molecular sciences · 2020
    Review
  14. Base-pair Opening Dynamics of Nucleic Acids in Relation to Their Biological Function.Computational and structural biotechnology journal · 2019
    Review
  15. Review
  16. 2'-Molecules (Basel, Switzerland) · 2018
    Article
  17. 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

10 authors at 1 institution in 1 country.

Ae-Ree LeeDepartment of Chemistry and RINS, Gyeongsang National University, Gyeongnam 52828, Republic of Korea.
Chin-Ju ParkDivision of Liberal Arts and Sciences and Department of Chemistry, Gwangju Institute of Science and Technology, Gwangju 61005, Republic of Korea.
Hae-Kap CheongDivision of Magnetic Resonance, KBSI, Chungbuk 28119, Republic of Korea.
Kyoung-Seok RyuDivision of Magnetic Resonance, KBSI, Chungbuk 28119, Republic of Korea.
Jin-Wan ParkDepartment of Chemistry and RINS, Gyeongsang National University, Gyeongnam 52828, Republic of Korea Division of Magnetic Resonance, KBSI, Chungbuk 28119, Republic of Korea.
Mun-Young KwonDepartment of Chemistry and RINS, Gyeongsang National University, Gyeongnam 52828, Republic of Korea.
Janghyun LeeDepartment of Chemistry, Korea Advanced Institute of Science and Technology, Daejeon 34141, Republic of Korea.
Kyeong Kyu KimDepartment of Molecular Cell Biology, Sungkyunkwan University School of Medicine, Gyeonggi 16419, Republic of Korea.
Byong-Seok ChoiDepartment of Chemistry, Korea Advanced Institute of Science and Technology, Daejeon 34141, Republic of Korea.
Joon-Hwa LeeDepartment of Chemistry and RINS, Gyeongsang National University, Gyeongnam 52828, Republic of Korea joonhwa@gnu.ac.kr.
Korea Advanced Institute of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Z-DNA binding proteins (ZBPs) play important roles in RNA editing, innate immune response and viral infection. Structural and biophysical studies show that ZBPs initially form an intermediate complex with B-DNA for B-Z conversion. However, a comprehensive understanding of the mechanism of Z-DNA binding and B-Z transition is still lacking, due to the absence of structural information on the intermediate complex. Here, we report the solution structure of the Zα domain of the ZBP-containing protein kinase from Carassius auratus(caZαPKZ). We quantitatively determined the binding affinity of caZαPKZ for both B-DNA and Z-DNA and characterized its B-Z transition activity, which is modulated by varying the salt concentration. Our results suggest that the intermediate complex formed by caZαPKZ and B-DNA can be used as molecular ruler, to measure the degree to which DNA transitions to the Z isoform.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCloning, MolecularDNA, B-FormDNA-Binding ProteinsDNA, Z-FormEscherichia coliFish ProteinsGene ExpressionGoldfishKineticsModels, MolecularMolecular Sequence DataProtein BindingProtein KinasesDNA, B-FormDNA-Binding ProteinsDNA, Z-FormFish ProteinsProtein KinasesRecombinant ProteinsSodium Chloride

Identifiers

PMID26792893
PMCPMC4824103
OpenAlexW2271156822

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LicenceCC BY-NC
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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.