Evidence map›Paper›PMID 33420071›Full record

ArticleNature communications2021

Structures of human dual oxidase 1 complex in low-calcium and high-calcium states.

Jing-Xiang Wu, Rui Liu, Kangcheng Song, Lei Chen

Open access · goldAbstract readVideo-Audio Media
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 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
5.3field-weighted citation impact, top 3% 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

32 citing papers in PubMed, 80 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Expression, localization and regulation of NADPH oxidases in pancreatic beta cells.Redox report : communications in free radical research · 2025
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  8. Enhancing Selectivity and Potency of SJournal of medicinal chemistry · 2025
    Article
  9. Review
  10. Article
  11. Article
  12. To activate NAD(P)H oxidase with a brief pulse of photodynamic action.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    Article
  13. Article
  14. Structural basis of human NOX5 activation.Nature communications · 2024
    Article
  15. Article
  16. Article
  17. Article
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  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Jing-Xiang WuState Key Laboratory of Membrane Biology, College of Future Technology, Institute of Molecular Medicine, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Peking University, 100871, Beijing, China.
Rui LiuState Key Laboratory of Membrane Biology, College of Future Technology, Institute of Molecular Medicine, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Peking University, 100871, Beijing, China.
Kangcheng SongState Key Laboratory of Membrane Biology, College of Future Technology, Institute of Molecular Medicine, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Peking University, 100871, Beijing, China.
Lei ChenState Key Laboratory of Membrane Biology, College of Future Technology, Institute of Molecular Medicine, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Peking University, 100871, Beijing, China. chenlei2016@pku.edu.cn.ORCID http://orcid.org/0000-0002-7619-8311
Peking University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations. Here, we report the cryo-EM structures of human DUOX1-DUOXA1 complex in both high-calcium and low-calcium states. These structures reveal the DUOX1 complex is a symmetric 2:2 hetero-tetramer stabilized by extensive inter-subunit interactions. Substrate NADPH and cofactor FAD are sandwiched between transmembrane domain and the cytosolic dehydrogenase domain of DUOX. In the presence of calcium ions, intracellular EF-hand modules might enhance the catalytic activity of DUOX by stabilizing the dehydrogenase domain in a conformation that allows electron transfer.

Indexed as

CalciumCell MembraneCryoelectron MicroscopyDual OxidasesEnzyme ActivationEnzyme AssaysFlavin-Adenine DinucleotideHEK293 CellsHumansMembrane ProteinsModels, MolecularNADPProtein DomainsRecombinant ProteinsCalciumDual OxidasesDUOX1 protein, humanDUOXA1 protein, humanFlavin-Adenine DinucleotideMembrane ProteinsNADPRecombinant Proteins

Identifiers

PMID33420071
PMCPMC7794343
OpenAlexW3121080120

What Socratic holds

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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 Socratic graph.