Evidence map›Paper›PMID 33805331›Full record

ArticleInternational journal of molecular sciences2021

Systematic Approach to Find the Global Minimum of Relaxation Dispersion Data for Protein-Induced B-Z Transition of DNA.

Kwang-Im Oh, Ae-Ree Lee, Seo-Ree Choi, Youyeon Go, Kyoung-Seok Ryu, Eun-Hee Kim, Joon-Hwa Lee

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 48% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. Biophysical Study of the Structure, Dynamics, and Function of Nucleic Acids.International journal of molecular sciences · 2022
    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

7 authors at 2 institutions in 1 country.

Kwang-Im OhDepartment of Chemistry and RINS, Gyeongsang National University, Gyeongnam 52828, Korea.ORCID 0000-0002-3304-2659
Ae-Ree LeeDepartment of Chemistry and RINS, Gyeongsang National University, Gyeongnam 52828, Korea.
Seo-Ree ChoiDepartment of Chemistry and RINS, Gyeongsang National University, Gyeongnam 52828, Korea.
Youyeon GoDepartment of Chemistry and RINS, Gyeongsang National University, Gyeongnam 52828, Korea.
Kyoung-Seok RyuDivision of Magnetic Resonance, Korea Basic Science Institute, Ochang, Chungbuk 28119, Korea.ORCID 0000-0002-8422-6669
Eun-Hee KimCenter for Research Equipment, Korea Basic Science Institute, Ochang, Chungbuk 28119, Korea.
Joon-Hwa LeeDepartment of Chemistry and RINS, Gyeongsang National University, Gyeongnam 52828, Korea.ORCID 0000-0003-3137-4585
Gyeongsang National University · KRKorea Basic Science Institute · KR

Funding

Korea Basic Science Institute C030440National Research Foundation of Korea 2020R1A2C1006909National Research Foundation of Korea 2020R1I1A1A01070690Samsung Science and Technology Foundation SSTF-BA1701-10
6 · The paper itself

Abstract

Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion spectroscopy is commonly used for quantifying conformational changes of protein in μs-to-ms timescale transitions. To elucidate the dynamics and mechanism of protein binding, parameters implementing CPMG relaxation dispersion results must be appropriately determined. Building an analytical model for multi-state transitions is particularly complex. In this study, we developed a new global search algorithm that incorporates a random search approach combined with a field-dependent global parameterization method. The robust inter-dependence of the parameters carrying out the global search for individual residues (GSIR) or the global search for total residues (GSTR) provides information on the global minimum of the conformational transition process of the Zα domain of human ADAR1 (hZα

Indexed as

Models, MolecularAdenosine DeaminaseAlgorithmsDNA, B-FormDNA-Binding ProteinsDNA, Z-FormHumansMagnetic Resonance SpectroscopyProtein ConformationRNA-Binding ProteinsThermodynamicsADAR protein, humanAdenosine DeaminaseDNA, B-FormDNA-Binding ProteinsDNA, Z-FormRNA-Binding ProteinsCPMGglobal searchhZαADAR1NMRrelaxation dispersionZ-DNA

Identifiers

PMID33805331
PMCPMC8037647
OpenAlexW3146526545

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.