Evidence map›Paper›PMID 35780107›Full record

ArticleMicrobial cell factories2022

Sequence, structure, and function of the Dps DNA-binding protein from Deinococcus wulumuqiensis R12.

Yao Chen, Zhihan Yang, Xue Zhou, Mengmeng Jin, Zijie Dai, Dengming Ming, Zhidong Zhang, Liying Zhu, Ling Jiang

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

7 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Physiological Changes and Transposition of Insertion Sequences in theInternational journal of molecular sciences · 2026
    Article
  3. Article
  4. Review
  5. Review
  6. Review
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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

9 authors at 1 institution in 1 country.

Yao ChenCollege of Food Science and Light Industry, State Key Laboratory of Materials-Oriented Chemical Engineering, Nanjing Tech University, Nanjing, 211816, China.
Zhihan YangCollege of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing, 211816, China.
Xue ZhouCollege of Food Science and Light Industry, State Key Laboratory of Materials-Oriented Chemical Engineering, Nanjing Tech University, Nanjing, 211816, China.
Mengmeng JinCollege of Food Science and Light Industry, State Key Laboratory of Materials-Oriented Chemical Engineering, Nanjing Tech University, Nanjing, 211816, China.
Zijie DaiCollege of Food Science and Light Industry, State Key Laboratory of Materials-Oriented Chemical Engineering, Nanjing Tech University, Nanjing, 211816, China.
Dengming MingCollege of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing, 211816, China.
Zhidong ZhangCollege of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing, 211816, China. zhangzheedong@sohu.com.
Liying ZhuSchool of Chemistry and Molecular Engineering, Nanjing Tech University, Nanjing, 211816, China. zlyhappy@njtech.edu.cn.
Ling JiangCollege of Food Science and Light Industry, State Key Laboratory of Materials-Oriented Chemical Engineering, Nanjing Tech University, Nanjing, 211816, China. jiangling@njtech.edu.cn.ORCID http://orcid.org/0000-0001-6625-5557
Nanjing Tech University · CN

Funding

Fundamental Research Funds for the Central Universities 0214-14380502National Natural Science Foundation of China 31922070National Natural Science Foundation of China 32060004National Natural Science Foundation of China U2106228Postgraduate Research & Practice Innovation Program of Jiangsu Province KYCX19_0872
6 · The paper itself

Abstract

Deinococcus wulumuqiensis R12, which was isolated from arid irradiated soil in Xinjiang province of China, belongs to a genus that is well-known for its extreme resistance to ionizing radiation and oxidative stress. The DNA-binding protein Dps has been studied for its great contribution to oxidative resistance. To explore the role of Dps in D. wulumuqiensis R12, the Dps sequence and homology-modeled structure were analyzed. In addition, the dps gene was knocked out and proteomics was used to verify the functions of Dps in D. wulumuqiensis R12. Docking data and DNA binding experiments in vitro showed that the R12 Dps protein has a better DNA binding ability than the Dps1 protein from D. radiodurans R1. When the dps gene was deleted in D. wulumuqiensis R12, its resistance to H

Indexed as

DNA-Binding ProteinsHydrogen PeroxideBacterial ProteinsDeinococcusDNABacterial ProteinsDNADNA-Binding ProteinsHydrogen PeroxideDeinococcus wulumuqiensis R12DNA-binding proteinOxidative stressProteomics

Identifiers

PMID35780107
PMCPMC9250271
OpenAlexW4283774697

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.