ArticleThe Journal of biological chemistry2016
Purification of Ovine Respiratory Complex I Results in a Highly Active and Stable Preparation.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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.
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.
Who cites it
19 citing papers in PubMed.
- Targeted Delivery and ROS-Responsive Release of Lutein Nanoassemblies Inhibit Myocardial Ischemia-Reperfusion Injury by Improving Mitochondrial Function.International journal of nanomedicine · 2024Article
- Structure of mycobacterial respiratory complex I.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Resting mitochondrial complex I fromeLife · 2023Article
- Making the leap from structure to mechanism: are the open states of mammalian complex I identified by cryoEM resting states or catalytic intermediates?Current opinion in structural biology · 2022Review
- Cardiac-specific overexpression of Ndufs1 ameliorates cardiac dysfunction after myocardial infarction by alleviating mitochondrial dysfunction and apoptosis.Experimental & molecular medicine · 2022Article
- Structure of respiratory complex I - An emerging blueprint for the mechanism.Current opinion in structural biology · 2022Review
- Article
- The Mysterious Multitude: Structural Perspective on the Accessory Subunits of Respiratory Complex I.Frontiers in molecular biosciences · 2021Review
- Cryo-EM structure of the entire mammalian F-type ATP synthase.Nature structural & molecular biology · 2020Article
- Mutations inCells · 2019Article
- Structures of Respiratory Supercomplex I+IIIMolecular cell · 2019Article
- Article
- Exploring the quinone/inhibitor-binding pocket in mitochondrial respiratory complex I by chemical biology approaches.The Journal of biological chemistry · 2019Article
- Suppression of reactive oxygen species generation in heart mitochondria from anoxic turtles: the role of complex IThe Journal of experimental biology · 2018Article
- Structure of the Deactive State of Mammalian Respiratory Complex I.Structure (London, England : 1993) · 2018Article
- Clarifying the supercomplex: the higher-order organization of the mitochondrial electron transport chain.Nature structural & molecular biology · 2017Review
- Spatial Organization of Metabolic Enzyme Complexes in Cells.Biochemistry · 2017Review
- Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
NADH-ubiquinone oxidoreductase (complex I) is the largest (∼1 MDa) and the least characterized complex of the mitochondrial electron transport chain. Because of the ease of sample availability, previous work has focused almost exclusively on bovine complex I. However, only medium resolution structural analyses of this complex have been reported. Working with other mammalian complex I homologues is a potential approach for overcoming these limitations. Due to the inherent difficulty of expressing large membrane protein complexes, screening of complex I homologues is limited to large mammals reared for human consumption. The high sequence identity among these available sources may preclude the benefits of screening. Here, we report the characterization of complex I purified from Ovis aries (ovine) heart mitochondria. All 44 unique subunits of the intact complex were identified by mass spectrometry. We identified differences in the subunit composition of subcomplexes of ovine complex I as compared with bovine, suggesting differential stability of inter-subunit interactions within the complex. Furthermore, the 42-kDa subunit, which is easily lost from the bovine enzyme, remains tightly bound to ovine complex I. Additionally, we developed a novel purification protocol for highly active and stable mitochondrial complex I using the branched-chain detergent lauryl maltose neopentyl glycol. Our data demonstrate that, although closely related, significant differences exist between the biochemical properties of complex I prepared from ovine and bovine mitochondria and that ovine complex I represents a suitable alternative target for further structural studies.
Indexed as
Identifiers
What OpenQuestion holds
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.