ArticleScientific reports2017
Structural and Functional insights into the catalytic mechanism of the Type II NADH:quinone oxidoreductase family.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed, 40 citations in OpenAlex.
- Quinone-transporting filaments expand bioenergetic capacity in Gram-positive Bacillota.Nature microbiology · 2026Article
- Mechanistic insights into redox activity and catalytic determinants of the haloarchaeal flavin-dependent oxidoreductasebioRxiv : the preprint server for biology · 2026Article
- Revealing interactions between microbes, metabolites, and dietary compounds using genome-scale analysis.Microbiome · 2026Article
- Article
- FSP1 and CoQ10 have the potential to serve as biomarkers for severe preeclampsia.BMC pregnancy and childbirth · 2025Article
- Low-complexity regions in fungi display functional groups and are depleted in positively charged amino acids.NAR genomics and bioinformatics · 2025Article
- Article
- Inhibitors of Type II NADH Dehydrogenase Enzyme: A Review.Current protein & peptide science · 2025Review
- Scrutinizing aApplied and environmental microbiology · 2024Article
- Integrated chemical and genetic screens unveil FSP1 mechanisms of ferroptosis regulation.Nature structural & molecular biology · 2023Article
- Structural insights into FSP1 catalysis and ferroptosis inhibition.Nature communications · 2023Article
- Mutations in the Second Alternative Oxidase Gene: A New Approach to GroupJournal of fungi (Basel, Switzerland) · 2023Article
- Recent Advances in Chemotherapeutics for Leishmaniasis: Importance of the Cellular Biochemistry of the Parasite and Its Molecular Interaction with the Host.Pathogens (Basel, Switzerland) · 2023Review
- Molecular characterization of AIFM2/FSP1 inhibition by iFSP1-like molecules.Cell death & disease · 2023Article
- Development of Novel Anti-Leishmanials: The Case for Structure-Based Approaches.Pathogens (Basel, Switzerland) · 2022Review
- Thylakoid Localized Type 2 NAD(P)H Dehydrogenase NdbA Optimizes Light-Activated Heterotrophic Growth of Synechocystis sp. PCC 6803.Plant & cell physiology · 2019Article
- Regulation of the mechanism of Type-II NADH: Quinone oxidoreductase from S. aureus.Redox biology · 2018Article
- In Silico Discovery of a Substituted 6-Methoxy-quinalidine with Leishmanicidal Activity in Leishmania infantum.Molecules (Basel, Switzerland) · 2018Article
- Ubiquinone binding site of yeast NADH dehydrogenase revealed by structures binding novel competitive- and mixed-type inhibitors.Scientific reports · 2018Article
- Chemoinformatics Strategies for Leishmaniasis Drug Discovery.Frontiers in pharmacology · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Type II NADH:quinone oxidoreductases (NDH-2s) are membrane proteins involved in respiratory chains. These proteins contribute indirectly to the establishment of the transmembrane difference of electrochemical potential by catalyzing the reduction of quinone by oxidation of NAD(P)H. NDH-2s are widespread enzymes being present in the three domains of life. In this work, we explored the catalytic mechanism of NDH-2 by investigating the common elements of all NDH-2s, based on the rationale that conservation of such elements reflects their structural/functional importance. We observed conserved sequence motifs and structural elements among 1762 NDH-2s. We identified two proton pathways possibly involved in the protonation of the quinone. Our results led us to propose the first catalytic mechanism for NDH-2 family, in which a conserved glutamate residue, E
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.