Evidence map›Paper›PMID 34226550›Full record

ArticleNature communications2021

DNA repair glycosylase hNEIL1 triages damaged bases via competing interaction modes.

Menghao Liu, Jun Zhang, Chenxu Zhu, Xiaoxue Zhang, Weide Xiao, Yongchang Yan, Lulu Liu, Hu Zeng, Yi Qin Gao, Chengqi Yi

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 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

11 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Review
  6. Deciphering the crystal structure of a novel nanobody against the NEIL1 DNA glycosylase.Acta crystallographica. Section D, Structural biology · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. 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.

Menghao Liu *Peking-Tsinghua Center for Life Sciences, Peking University, Beijing, China.ORCID 0000-0002-5284-0146
Jun Zhang *Beijing National Laboratory for Molecular Sciences, College of Chemistry and Molecular Engineering, Peking University, Beijing, China.ORCID 0000-0002-8760-6747
Chenxu Zhu *State Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking University, Beijing, China.ORCID 0000-0003-4216-6562
Xiaoxue ZhangPeking-Tsinghua Center for Life Sciences, Peking University, Beijing, China.
Weide XiaoState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking University, Beijing, China.
Yongchang YanPeking-Tsinghua Center for Life Sciences, Peking University, Beijing, China.
Lulu LiuPeking-Tsinghua Center for Life Sciences, Peking University, Beijing, China.
Hu ZengState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking University, Beijing, China.ORCID 0000-0003-4773-205X
Yi Qin GaoBeijing National Laboratory for Molecular Sciences, College of Chemistry and Molecular Engineering, Peking University, Beijing, China. gaoyq@pku.edu.cn.ORCID 0000-0002-4309-9376
Chengqi YiPeking-Tsinghua Center for Life Sciences, Peking University, Beijing, China. chengqi.yi@pku.edu.cn.ORCID 0000-0003-2540-9729
Peking University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA glycosylases must distinguish the sparse damaged sites from the vast expanse of normal DNA bases. However, our understanding of the nature of nucleobase interrogation is still limited. Here, we show that hNEIL1 (human endonuclease VIII-like 1) captures base lesions via two competing states of interaction: an activated state that commits catalysis and base excision repair, and a quarantine state that temporarily separates and protects the flipped base via auto-inhibition. The relative dominance of the two states depends on key residues of hNEIL1 and chemical properties (e.g. aromaticity and hydrophilicity) of flipped bases. Such a DNA repair mechanism allows hNEIL1 to recognize a broad spectrum of DNA damage while keeps potential gratuitous repair in check. We further reveal the molecular basis of hNEIL1 activity regulation mediated by post-transcriptional modifications and provide an example of how exquisite structural dynamics serves for orchestrated enzyme functions.

Indexed as

TriageAmino Acid SequenceBinding SitesCatalytic DomainDeoxyribonuclease (Pyrimidine Dimer)DNADNA DamageDNA GlycosylasesDNA RepairHumansMolecular Dynamics SimulationMutationProtein ConformationSubstrate SpecificityDeoxyribonuclease (Pyrimidine Dimer)DNADNA GlycosylasesNEIL1 protein, human

Identifiers

PMID34226550
PMCPMC8257757
OpenAlexW3182805786

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.