Evidence map›Paper›PMID 37098072›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2023

Structure of the human respiratory complex II.

Zhanqiang Du, Xiaoting Zhou, Yuezheng Lai, Jinxu Xu, Yuying Zhang, Shan Zhou, Ziyan Feng, Long Yu, Yanting Tang, Weiwei Wang and 9 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed, 1 pooled it
7.8field-weighted citation impact, top 2% 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

28 citing papers in PubMed, 1 synthesis or guideline pooled it, 49 citations in OpenAlex.

  1. [Advances in the molecular genetics of nuclear gene mutations causing pediatric mitochondrial cardiomyopathy].Zhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics · 2026
    Pooled it
  2. Review
  3. Article
  4. Review
  5. Triclabendazole disrupts mitochondrial electron transportAntimicrobial agents and chemotherapy · 2026
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Cryo-EM single-particle analysis expanding towards increasingly native samples.Acta crystallographica. Section D, Structural biology · 2025
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  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

19 authors at 6 institutions in 2 countries.

Zhanqiang DuState Key Laboratory of Medicinal Chemical Biology, Frontiers Science Center for Cell Responses, College of Life Sciences, Nankai University, Tianjin 300353, China.ORCID 0009-0003-2668-8333
Xiaoting ZhouState Key Laboratory of Reproductive Regulation and Breeding of Grassland Livestock, School of Life Sciences, Inner Mongolia University, Hohhot 010070, China.
Yuezheng LaiState Key Laboratory of Medicinal Chemical Biology, Frontiers Science Center for Cell Responses, College of Life Sciences, Nankai University, Tianjin 300353, China.
Jinxu XuState Key Laboratory of Medicinal Chemical Biology, Frontiers Science Center for Cell Responses, College of Life Sciences, Nankai University, Tianjin 300353, China.
Yuying ZhangState Key Laboratory of Medicinal Chemical Biology, Frontiers Science Center for Cell Responses, College of Life Sciences, Nankai University, Tianjin 300353, China.ORCID 0009-0009-7646-7903
Shan ZhouState Key Laboratory of Medicinal Chemical Biology, Frontiers Science Center for Cell Responses, College of Life Sciences, Nankai University, Tianjin 300353, China.
Ziyan FengState Key Laboratory of Medicinal Chemical Biology, Frontiers Science Center for Cell Responses, College of Life Sciences, Nankai University, Tianjin 300353, China.
Long YuState Key Laboratory of Medicinal Chemical Biology, Frontiers Science Center for Cell Responses, College of Life Sciences, Nankai University, Tianjin 300353, China.
Yanting TangState Key Laboratory of Medicinal Chemical Biology, Frontiers Science Center for Cell Responses, College of Life Sciences, Nankai University, Tianjin 300353, China.ORCID 0000-0002-8656-3220
Weiwei WangShanghai Institute for Advanced Immunochemical Studies and School of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.
Lu YuHigh Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei 230031, China.ORCID 0000-0002-2581-4612
Changlin TianHigh Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei 230031, China.
Ting RanInnovative Center For Pathogen Research, Guangzhou Laboratory, Guangzhou 510005, China.
Hongming ChenInnovative Center For Pathogen Research, Guangzhou Laboratory, Guangzhou 510005, China.
Luke W GuddatSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD 4072, Australia.ORCID 0000-0002-8204-8408
Fengjiang LiuInnovative Center For Pathogen Research, Guangzhou Laboratory, Guangzhou 510005, China.
Yan GaoShanghai Institute for Advanced Immunochemical Studies and School of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.ORCID 0000-0002-0364-6427
Zihe RaoState Key Laboratory of Medicinal Chemical Biology, Frontiers Science Center for Cell Responses, College of Life Sciences, Nankai University, Tianjin 300353, China.ORCID 0000-0001-9866-2384
Hongri GongState Key Laboratory of Medicinal Chemical Biology, Frontiers Science Center for Cell Responses, College of Life Sciences, Nankai University, Tianjin 300353, China.ORCID 0000-0002-2596-7635
Nankai University · CNChinese Academy of Sciences · CNGuangzhou Experimental Station · CNShanghaiTech University · CNThe University of Queensland · AUInner Mongolia University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human complex II is a key protein complex that links two essential energy-producing processes: the tricarboxylic acid cycle and oxidative phosphorylation. Deficiencies due to mutagenesis have been shown to cause mitochondrial disease and some types of cancers. However, the structure of this complex is yet to be resolved, hindering a comprehensive understanding of the functional aspects of this molecular machine. Here, we have determined the structure of human complex II in the presence of ubiquinone at 2.86 Å resolution by cryoelectron microscopy, showing it comprises two water-soluble subunits, SDHA and SDHB, and two membrane-spanning subunits, SDHC and SDHD. This structure allows us to propose a route for electron transfer. In addition, clinically relevant mutations are mapped onto the structure. This mapping provides a molecular understanding to explain why these variants have the potential to produce disease.

Indexed as

Protein Structure, QuaternaryCryoelectron MicroscopyElectron Transport Complex IIHumansModels, MolecularMutationElectron Transport Complex IIrespiratory complex IIcryoelectron microscopyelectron transport chainhuman complex II

Identifiers

PMID37098072
PMCPMC10161127
OpenAlexW4366981282

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.