Evidence map›Paper›PMID 32029762›Full record

ArticleScientific reports2020

A combined Far-FTIR, FTIR Spectromicroscopy, and DFT Study of the Effect of DNA Binding on the [4Fe4S] Cluster Site in EndoIII.

Ayaz Hassan, Lucyano J A Macedo, João C P de Souza, Filipe C D A Lima, Frank N Crespilho

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.2field-weighted citation impact, top 10% 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

12 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
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  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. On the Weak Binding and Spectroscopic Signature of SARS-CoV-2 nsp14 Interaction with RNA.Chembiochem : a European journal of chemical biology · 2021
    Article
  10. Review
  11. Article
  12. Effects of Ionic Liquids on Metalloproteins.Molecules (Basel, Switzerland) · 2021
    Review
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 3 institutions in 3 countries.

Ayaz HassanSão Carlos Institute of Chemistry, University of São Paulo, 13560-970, São Paulo, Brazil. ahasan333@yahoo.com.ORCID http://orcid.org/0000-0003-3842-5883
Lucyano J A MacedoSão Carlos Institute of Chemistry, University of São Paulo, 13560-970, São Paulo, Brazil.ORCID http://orcid.org/0000-0002-7949-5397
João C P de SouzaGoiano Federal Institute of Education, Science and Technology, Campus Rio Verde, 75901-970, Goiás, Brazil.ORCID http://orcid.org/0000-0001-9962-3889
Filipe C D A LimaFederal Institute of Education, Science, and Technology of São Paulo, Campus Matão, 15991-502, São Paulo, Brazil.ORCID http://orcid.org/0000-0001-7062-5450
Frank N CrespilhoSão Carlos Institute of Chemistry, University of São Paulo, 13560-970, São Paulo, Brazil. frankcrespilho@iqsc.usp.br.ORCID http://orcid.org/0000-0003-4830-652X
Universidade de São Paulo · BRFederal Institute of São Paulo · BRInstituto Federal Goiano · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Endonuclease III (EndoIII) is a DNA glycosylase that contains the [4Fe4S] cluster, which is essential for the protein to bind to damaged DNA in a process called base excision repair (BER). Here we propose that the change in the covalency of Fe-S bonds of the [4Fe4S] cluster caused by double-stranded (ds)-DNA binding is accompanied by a change in their strength, which is due to alterations of the electronic structure of the cluster. Micro-FTIR spectroscopy in the mid-IR region and FTIR spectroscopy in the far IR (450 and 300 cm

Indexed as

Binding SitesDeoxyribonuclease (Pyrimidine Dimer)DNADNA-Binding ProteinsDNA DamageDNA GlycosylasesDNA RepairEscherichia coliEscherichia coli ProteinsIron-Sulfur ProteinsOxidation-ReductionSpectroscopy, Fourier Transform InfraredDeoxyribonuclease (Pyrimidine Dimer)DNADNA-Binding ProteinsDNA GlycosylasesEscherichia coli ProteinsIron-Sulfur ProteinsNTH protein, E coli

Identifiers

PMID32029762
PMCPMC7005299
OpenAlexW3004567170

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.