ArticleProceedings of the National Academy of Sciences of the United States of America2015
Loop recognition and copper-mediated disulfide reduction underpin metal site assembly of CuA in human cytochrome oxidase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 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
42 citing papers in PubMed, 66 citations in OpenAlex.
- Pathogenic variants of the mitochondrial copper chaperones SCO1 and SCO2 reshape their respective interactomes and disrupt cellular phospholipid metabolism.bioRxiv : the preprint server for biology · 2026Article
- Copper-instigated modulatory cell mortality mechanisms and progress in kidney diseases.Renal failure · 2025Review
- Heart is the most susceptible organ in an isogenic background to loss of function mutations in the mitochondrial metallochaperone SCO1.Human molecular genetics · 2025Article
- Metal Ion Signaling in Biomedicine.Chemical reviews · 2025Review
- Cysteine rich intestinal protein 2 links copper homeostasis to translational regulation in primary myoblasts.microPublication biology · 2025Article
- Cysteine Rich Intestinal Protein 2 is a copper-responsive regulator of skeletal muscle differentiation and metal homeostasis.PLoS genetics · 2024Article
- Copper homeostasis and cuproptosis in central nervous system diseases.Cell death & disease · 2024Review
- Copper in colorectal cancer: From copper-related mechanisms to clinical cancer therapies.Clinical and translational medicine · 2024Review
- Cysteine Rich Intestinal Protein 2 is a copper-responsive regulator of skeletal muscle differentiation.bioRxiv : the preprint server for biology · 2024Article
- More than Just Bread and Wine: Using Yeast to Understand Inherited Cytochrome Oxidase Deficiencies in Humans.International journal of molecular sciences · 2024Review
- Copper Metabolism and Cuproptosis: Molecular Mechanisms and Therapeutic Perspectives in Neurodegenerative Diseases.Current medical science · 2024Review
- Role of copper and its complexes in cardiovascular diseases.Zhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences · 2023Article
- Mitochondrial copper in human genetic disorders.Trends in endocrinology and metabolism: TEM · 2023Review
- A yeast suppressor screen links Coa4 to the mitochondrial copper delivery pathway for cytochrome c oxidase.Genetics · 2022Article
- Coordination of metal center biogenesis in human cytochrome c oxidase.Nature communications · 2022Article
- Reaction ofInternational journal of molecular sciences · 2022Article
- Mitochondrial COA7 is a heme-binding protein with disulfide reductase activity, which acts in the early stages of complex IV assembly.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The Role of COA6 in the Mitochondrial Copper Delivery Pathway to CytochromeBiomolecules · 2022Review
- Identification and Validation of a DNA Damage Repair-Related Signature for Diffuse Large B-Cell Lymphoma.BioMed research international · 2022Article
- The mitochondrial CuFrontiers in molecular biosciences · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Maturation of cytochrome oxidases is a complex process requiring assembly of several subunits and adequate uptake of the metal cofactors. Two orthologous Sco proteins (Sco1 and Sco2) are essential for the correct assembly of the dicopper CuA site in the human oxidase, but their function is not fully understood. Here, we report an in vitro biochemical study that shows that Sco1 is a metallochaperone that selectively transfers Cu(I) ions based on loop recognition, whereas Sco2 is a copper-dependent thiol reductase of the cysteine ligands in the oxidase. Copper binding to Sco2 is essential to elicit its redox function and as a guardian of the reduced state of its own cysteine residues in the oxidizing environment of the mitochondrial intermembrane space (IMS). These results provide a detailed molecular mechanism for CuA assembly, suggesting that copper and redox homeostasis are intimately linked in the mitochondrion.
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.