ArticleNature2011
Structure of the membrane domain of respiratory complex I.
Article in Nature, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 175 papers, 1 of them a synthesis that pooled it.
What it found
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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.
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.
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Who cites it
175 citing papers in PubMed, 1 synthesis or guideline pooled it, 365 citations in OpenAlex.
- Meta-analysis identifies mitochondrial DNA sequence variants associated with walking speed.GeroScience · 2018Pooled it
- Mitochondrial complex I as a master regulator of redox signaling: From structural architecture to directionality of electron transport.Free radical biology & medicine · 2026Review
- Mitochondrial complex I deficiency-associated diseases and models.Cellular and molecular life sciences : CMLS · 2026Review
- Selective inhibition of respiratory complex I reveals a bioenergetic vulnerability inbioRxiv : the preprint server for biology · 2026Article
- Review
- Mammalian Respiratory Chain Complex Assemblies and Their Links to Mitochondria Stress-Induced Human Diseases.Advances in experimental medicine and biology · 2026Review
- Cellular function of the GndA microprotein during heat shock.bioRxiv : the preprint server for biology · 2025Article
- Cryo-EM structure of the NDH-PSI-LHCI supercomplex from Spinacia oleracea.Nature structural & molecular biology · 2025Article
- A cyanobacteria-derived intermolecular salt bridge stabilizes photosynthetic NDH-1 and prevents oxidative stress.Communications biology · 2025Article
- Graph-Theoretical Prediction and Analysis of Biologically Relevant Substructures in an Open and Closed Conformation of Respiratory Complex I.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Proton-Translocating NADH-Ubiquinone Oxidoreductase: Interaction with Artificial Electron Acceptors, Inhibitors, and Potential Medicines.International journal of molecular sciences · 2024Review
- Bismuth-based drugs sensitize Pseudomonas aeruginosa to multiple antibiotics by disrupting iron homeostasis.Nature microbiology · 2024Article
- Likelihood-based interactive local docking into cryo-EM maps in ChimeraX.Acta crystallographica. Section D, Structural biology · 2024Article
- Asgard archaea modulate potential methanogenesis substrates in wetland soil.Nature communications · 2024Article
- Vitamin C as Scavenger of Reactive Oxygen Species during Healing after Myocardial Infarction.International journal of molecular sciences · 2024Review
- Using cryo-EM to understand the assembly pathway of respiratory complex I.Acta crystallographica. Section D, Structural biology · 2024Article
- Mitochondria at the Nanoscale: Physics Meets Biology-What Does It Mean for Medicine?International journal of molecular sciences · 2024Review
- Investigation of hydrated channels and proton pathways in a high-resolution cryo-EM structure of mammalian complex I.Science advances · 2023Article
- Likelihood-based docking of models into cryo-EM maps.Acta crystallographica. Section D, Structural biology · 2023Article
- A primordial target: Mitochondria mediate both primary and collateral anesthetic effects of volatile anesthetics.Experimental biology and medicine (Maywood, N.J.) · 2023Review
115 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
Complex I is the first and largest enzyme of the respiratory chain, coupling electron transfer between NADH and ubiquinone to the translocation of four protons across the membrane. It has a central role in cellular energy production and has been implicated in many human neurodegenerative diseases. The L-shaped enzyme consists of hydrophilic and membrane domains. Previously, we determined the structure of the hydrophilic domain. Here we report the crystal structure of the Esherichia coli complex I membrane domain at 3.0 Å resolution. It includes six subunits, NuoL, NuoM, NuoN, NuoA, NuoJ and NuoK, with 55 transmembrane helices. The fold of the homologous antiporter-like subunits L, M and N is novel, with two inverted structural repeats of five transmembrane helices arranged, unusually, face-to-back. Each repeat includes a discontinuous transmembrane helix and forms half of a channel across the membrane. A network of conserved polar residues connects the two half-channels, completing the proton translocation pathway. Unexpectedly, lysines rather than carboxylate residues act as the main elements of the proton pump in these subunits. The fourth probable proton-translocation channel is at the interface of subunits N, K, J and A. The structure indicates that proton translocation in complex I, uniquely, involves coordinated conformational changes in six symmetrical structural elements.
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Registered trials
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.