Evidence map›Paper›PMID 38372588›Full record

ArticleActa crystallographica. Section D, Structural biology2024

Using cryo-EM to understand the assembly pathway of respiratory complex I.

Eike Laube, Jonathan Schiller, Volker Zickermann, Janet Vonck

Open access · hybridAbstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

5 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
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  5. 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 2 institutions in 1 country.

Eike LaubeDepartment of Structural Biology, Max Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany.ORCID 0000-0002-1096-5178
Jonathan SchillerInstitute of Biochemistry II, University Hospital, Goethe University, 60590 Frankfurt am Main, Germany.ORCID 0000-0002-0098-7787
Volker ZickermannInstitute of Biochemistry II, University Hospital, Goethe University, 60590 Frankfurt am Main, Germany.ORCID 0000-0001-8461-8817
Janet VonckDepartment of Structural Biology, Max Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany.ORCID 0000-0001-5659-8863
Goethe University Frankfurt · DEMax Planck Institute of Biophysics · DE

Funding

Deutsche Forschungsgemeinschaft CRC1507 P14
6 · The paper itself

Abstract

Complex I (proton-pumping NADH:ubiquinone oxidoreductase) is the first component of the mitochondrial respiratory chain. In recent years, high-resolution cryo-EM studies of complex I from various species have greatly enhanced the understanding of the structure and function of this important membrane-protein complex. Less well studied is the structural basis of complex I biogenesis. The assembly of this complex of more than 40 subunits, encoded by nuclear or mitochondrial DNA, is an intricate process that requires at least 20 different assembly factors in humans. These are proteins that are transiently associated with building blocks of the complex and are involved in the assembly process, but are not part of mature complex I. Although the assembly pathways have been studied extensively, there is limited information on the structure and molecular function of the assembly factors. Here, the insights that have been gained into the assembly process using cryo-EM are reviewed.

Indexed as

Electron Transport Complex IMitochondriaCryoelectron MicroscopyHumansElectron Transport Complex Iassembly factorscomplex I assemblyproton-pumping NADH ubiquinone oxidoreductaserespiratory complex Isingle-particle cryo-EM

Identifiers

PMID38372588
PMCPMC10910544
OpenAlexW4391948871

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.