Evidence map›Paper›PMID 35653932›Full record

ArticleRedox biology2022

Rhodaneses minimize the accumulation of cellular sulfane sulfur to avoid disulfide stress during sulfide oxidation in bacteria.

Mingxue Ran, Qingbin Li, Yufeng Xin, Shaohua Ma, Rui Zhao, Min Wang, Luying Xun, Yongzhen Xia

Open access · goldAbstract read
In one paragraph

Article in Redox biology, 2022. 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
2.7field-weighted citation impact, top 11% 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, 23 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Mechanism of Intracellular Elemental Sulfur Oxidation inInternational journal of molecular sciences · 2024
    Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. 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

8 authors at 3 institutions in 2 countries.

Mingxue RanState Key Laboratory of Microbial Technology, Shandong University, Qingdao, 266237, People's Republic of China.
Qingbin LiState Key Laboratory of Microbial Technology, Shandong University, Qingdao, 266237, People's Republic of China.
Yufeng XinCollege of Life Sciences, Qufu Normal University, Qufu, 273165, China.
Shaohua MaState Key Laboratory of Microbial Technology, Shandong University, Qingdao, 266237, People's Republic of China.
Rui ZhaoState Key Laboratory of Microbial Technology, Shandong University, Qingdao, 266237, People's Republic of China.
Min WangState Key Laboratory of Microbial Technology, Shandong University, Qingdao, 266237, People's Republic of China.
Luying XunState Key Laboratory of Microbial Technology, Shandong University, Qingdao, 266237, People's Republic of China; School of Molecular Biosciences, Washington State University, Pullman, WA, 99164-7520, USA. Electronic address: luying_xun@vetmed.edu.edu.
Yongzhen XiaState Key Laboratory of Microbial Technology, Shandong University, Qingdao, 266237, People's Republic of China. Electronic address: xiayongzhen2002@sdu.edu.cn.
Shandong University · CNQingdao University · CNQufu Normal University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heterotrophic bacteria and human mitochondria often use sulfide: quinone oxidoreductase (SQR) and persulfide dioxygenase (PDO) to oxidize sulfide to sulfite and thiosulfate. Bioinformatic analysis showed that the genes encoding RHOD domains were widely presented in annotated sqr-pdo operons and grouped into three types: fused with an SQR domain, fused with a PDO domain, and dissociated proteins. Biochemical evidence suggests that RHODs facilitate the formation of thiosulfate and promote the reaction between inorganic polysulfide and glutathione to produce glutathione polysulfide. However, the physiological roles of RHODs during sulfide oxidation by SQR and PDO could only be tested in an RHOD-free host. To test this, 8 genes encoding RHOD domains in Escherichia coli MG1655 were deleted to produce E. coli RHOD-8K. The sqr

Indexed as

Hydrogen SulfideQuinone ReductasesBacterial ProteinsDisulfidesEscherichia coliGlutathioneHumansOxidation-ReductionSulfidesSulfurThiosulfatesThiosulfate SulfurtransferaseBacterial ProteinsDisulfidesGlutathioneHydrogen SulfideQuinone ReductasesSulfidesSulfursulfur-32ThiosulfatesThiosulfate SulfurtransferaseGlutathione persulfidePersulfide dioxygenaseRhodaneseSulfane sulfurSulfide oxidationSulfide: quinone oxidoreductase

Identifiers

PMID35653932
PMCPMC9163753
OpenAlexW4281552315

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.