Evidence map›Paper›PMID 33504804›Full record

ArticleNature communications2021

APE1 distinguishes DNA substrates in exonucleolytic cleavage by induced space-filling.

Tung-Chang Liu, Chun-Ting Lin, Kai-Cheng Chang, Kai-Wei Guo, Shuying Wang, Jhih-Wei Chu, Yu-Yuan Hsiao

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.2field-weighted citation impact, top 4% 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

30 citing papers in PubMed, 69 citations in OpenAlex.

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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

7 authors at 2 institutions in 1 country.

Tung-Chang LiuInstitute of Molecular Medicine and Bioengineering, National Chiao Tung University, Hsinchu, 30068, Taiwan.
Chun-Ting LinMaster's and Doctoral Degree Program for Science and Technology of Accelerator Light Sources, National Chiao Tung University, Hsinchu, 30068, Taiwan.
Kai-Cheng ChangDepartment of Biological Science and Technology, National Chiao Tung University, Hsinchu, 30068, Taiwan.
Kai-Wei GuoDepartment of Biological Science and Technology, National Chiao Tung University, Hsinchu, 30068, Taiwan.
Shuying WangDepartment of Microbiology and Immunology, College of Medicine, National Cheng Kung University, Tainan, Taiwan.ORCID 0000-0003-3339-8070
Jhih-Wei ChuInstitute of Molecular Medicine and Bioengineering, National Chiao Tung University, Hsinchu, 30068, Taiwan.
Yu-Yuan HsiaoInstitute of Molecular Medicine and Bioengineering, National Chiao Tung University, Hsinchu, 30068, Taiwan. mike0617@nctu.edu.tw.ORCID 0000-0002-9648-5879
National Yang Ming Chiao Tung University · TWNational Cheng Kung University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The exonuclease activity of Apurinic/apyrimidinic endonuclease 1 (APE1) is responsible for processing matched/mismatched terminus in various DNA repair pathways and for removing nucleoside analogs associated with drug resistance. To fill in the gap of structural basis for exonucleolytic cleavage, we determine the APE1-dsDNA complex structures displaying end-binding. As an exonuclease, APE1 does not show base preference but can distinguish dsDNAs with different structural features. Integration with assaying enzyme activity and binding affinity for a variety of substrates reveals for the first time that both endonucleolytic and exonucleolytic cleavage can be understood by an induced space-filling model. Binding dsDNA induces RM (Arg176 and Met269) bridge that defines a long and narrow product pocket for exquisite machinery of substrate selection. Our study paves the way to comprehend end-processing of dsDNA in the cell and the drug resistance relating to APE1.

Indexed as

AnimalsBiocatalysisCatalytic DomainDNADNA-(Apurinic or Apyrimidinic Site) LyaseDNA DamageExonucleasesMiceModels, MolecularSubstrate SpecificityApex1 protein, mouseDNADNA-(Apurinic or Apyrimidinic Site) LyaseExonucleases

Identifiers

PMID33504804
PMCPMC7841161
OpenAlexW3122836537

What OpenQuestion holds

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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.