Evidence map›Paper›PMID 30355979›Full record

ReviewMolecules (Basel, Switzerland)2018

Thermodynamic Model for B-Z Transition of DNA Induced by Z-DNA Binding Proteins.

Ae-Ree Lee, Na-Hyun Kim, Yeo-Jin Seo, Seo-Ree Choi, Joon-Hwa Lee

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

15 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Deciphering the Biological Significance of ADAR1-Z-RNA Interactions.International journal of molecular sciences · 2021
    Review
  12. Review
  13. Article
  14. Dynamics Studies of DNA with Non-canonical Structure Using NMR Spectroscopy.International journal of molecular sciences · 2020
    Review
  15. 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

5 authors at 1 institution in 1 country.

Ae-Ree LeeDepartment of Chemistry and RINS, Gyeongsang National University, Gyeongnam 52828, Korea. dldofl24@naver.com.
Na-Hyun KimDepartment of Chemistry and RINS, Gyeongsang National University, Gyeongnam 52828, Korea. nahoney31@gmail.com.
Yeo-Jin SeoDepartment of Chemistry and RINS, Gyeongsang National University, Gyeongnam 52828, Korea. darkfntlvj@naver.com.
Seo-Ree ChoiDepartment of Chemistry and RINS, Gyeongsang National University, Gyeongnam 52828, Korea. csr2915@nate.com.
Joon-Hwa LeeDepartment of Chemistry and RINS, Gyeongsang National University, Gyeongnam 52828, Korea. joonhwa@gnu.ac.kr.ORCID 0000-0003-3137-4585
Gyeongsang National University · KR

Funding

National Research Foundation of Korea 2017R1A2B2001832Samsung Science and Technology Foundation SSTF-BA1701-10
6 · The paper itself

Abstract

Z-DNA is stabilized by various Z-DNA binding proteins (ZBPs) that play important roles in RNA editing, innate immune response, and viral infection. In this review, the structural and dynamics of various ZBPs complexed with Z-DNA are summarized to better understand the mechanisms by which ZBPs selectively recognize d(CG)-repeat DNA sequences in genomic DNA and efficiently convert them to left-handed Z-DNA to achieve their biological function. The intermolecular interaction of ZBPs with Z-DNA strands is mediated through a single continuous recognition surface which consists of an α3 helix and a β-hairpin. In the ZBP-Z-DNA complexes, three identical, conserved residues (N173, Y177, and W195 in the Zα domain of human ADAR1) play central roles in the interaction with Z-DNA. ZBPs convert a 6-base DNA pair to a Z-form helix via the B-Z transition mechanism in which the ZBP first binds to B-DNA and then shifts the equilibrium from B-DNA to Z-DNA, a conformation that is then selectively stabilized by the additional binding of a second ZBP molecule. During B-Z transition, ZBPs selectively recognize the alternating d(CG)

Indexed as

Models, MolecularThermodynamicsAlgorithmsBinding SitesDNADNA-Binding ProteinsDNA, Z-FormMacromolecular SubstancesProtein ConformationStructure-Activity RelationshipDNADNA-Binding ProteinsDNA, Z-FormMacromolecular SubstancesB-Z transitionDNA-protein interactionZ-DNAZ-DNA binding protein

Identifiers

PMID30355979
PMCPMC6278649
OpenAlexW2898323765

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.