Evidence map›Paper›PMID 30374105›Full record

ArticleNature communications2018

Locking loop movement in the ubiquinone pocket of complex I disengages the proton pumps.

Alfredo Cabrera-Orefice, Etienne Galemou Yoga, Christophe Wirth, Karin Siegmund, Klaus Zwicker, Sergio Guerrero-Castillo, Volker Zickermann, Carola Hunte, Ulrich Brandt

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed, 1 pooled it
4.6field-weighted citation impact, top 4% 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

56 citing papers in PubMed, 1 synthesis or guideline pooled it, 97 citations in OpenAlex.

  1. Pooled it
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  11. Using cryo-EM to understand the assembly pathway of respiratory complex I.Acta crystallographica. Section D, Structural biology · 2024
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  16. HScientific reports · 2023
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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 3 institutions in 3 countries.

Alfredo Cabrera-OreficeRadboud Institute for Molecular Life Sciences, Department of Pediatrics, Radboud University Medical Center, Geert Grooteplein-Zuid 10, 6525, GA, Nijmegen, The Netherlands.
Etienne Galemou YogaInstitute of Biochemistry II, Medical School, Goethe University, Max von Laue Str. 9, 60438, Frankfurt am Main, Germany.
Christophe WirthInstitute for Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, BIOSS Centre for Biological Signalling Studies, University of Freiburg, Stefan-Meier-Str. 17, 79104, Freiburg im Breisgau, Germany.ORCID http://orcid.org/0000-0001-8864-6508
Karin SiegmundInstitute of Biochemistry II, Medical School, Goethe University, Max von Laue Str. 9, 60438, Frankfurt am Main, Germany.
Klaus ZwickerInstitute of Biochemistry I, Medical School, Goethe University, Theodor-Stern-Kai 7, 60590, Frankfurt am Main, Germany.ORCID http://orcid.org/0000-0003-2155-024X
Sergio Guerrero-CastilloRadboud Institute for Molecular Life Sciences, Department of Pediatrics, Radboud University Medical Center, Geert Grooteplein-Zuid 10, 6525, GA, Nijmegen, The Netherlands.
Volker ZickermannCluster of Excellence Macromolecular Complexes, Goethe-University, Max von Laue Str. 9, 60438, Frankfurt am Main, Germany.ORCID http://orcid.org/0000-0001-8461-8817
Carola HunteInstitute for Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, BIOSS Centre for Biological Signalling Studies, University of Freiburg, Stefan-Meier-Str. 17, 79104, Freiburg im Breisgau, Germany.ORCID http://orcid.org/0000-0002-0826-3986
Ulrich BrandtRadboud Institute for Molecular Life Sciences, Department of Pediatrics, Radboud University Medical Center, Geert Grooteplein-Zuid 10, 6525, GA, Nijmegen, The Netherlands. ulrich.brandt@radboudumc.nl.ORCID http://orcid.org/0000-0003-1869-6811
Goethe University Frankfurt · DEUniversity of Freiburg · DERadboud University Nijmegen · NL

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) BR1633/3-1Deutsche Forschungsgemeinschaft (German Research Foundation) CRC746Deutsche Forschungsgemeinschaft (German Research Foundation) EXC 115 CEFDeutsche Forschungsgemeinschaft (German Research Foundation) EXC115 CEFDeutsche Forschungsgemeinschaft (German Research Foundation) ZI552/4-1Nederlandse Organisatie voor Wetenschappelijk Onderzoek (Netherlands Organisation for Scientific Research) TOP 714.017.00.4
6 · The paper itself

Abstract

Complex I (proton-pumping NADH:ubiquinone oxidoreductase) is the largest enzyme of the mitochondrial respiratory chain and a significant source of reactive oxygen species (ROS). We hypothesized that during energy conversion by complex I, electron transfer onto ubiquinone triggers the concerted rearrangement of three protein loops of subunits ND1, ND3, and 49-kDa thereby generating the power-stoke driving proton pumping. Here we show that fixing loop TMH1-2

Indexed as

Crystallography, X-RayDisulfidesElectron TransportElectron Transport Complex IEnzyme ActivationEscherichia coliEscherichia coli ProteinsKineticsMitochondrial MembranesModels, MolecularMolecular Dynamics SimulationMutagenesis, Site-DirectedProtein ConformationProton PumpsReactive Oxygen SpeciesUbiquinoneDisulfidesElectron Transport Complex IEscherichia coli ProteinsProton PumpsReactive Oxygen SpeciesUbiquinone

Identifiers

PMID30374105
PMCPMC6206036
OpenAlexW2897708283

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.