Affinage

SCO1

Cytochrome c oxidase assembly factor SCO1 · UniProt O75880

Length
301 aa
Mass
33.8 kDa
Annotated
2026-04-28
50 papers in source corpus 27 papers cited in narrative 26 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

SCO1 is a mitochondrial inner-membrane copper metallochaperone essential for the assembly of cytochrome c oxidase (Complex IV) and for systemic copper homeostasis. It possesses a thioredoxin-like fold and binds one Cu(I) ion through a conserved CXXXC motif and a histidine residue in a trigonal coordination geometry; Cu(I) is received from Cox17 via a coupled copper-electron transfer mechanism, and SCO2 acts upstream as a thiol-disulfide oxidoreductase to regulate the redox state of SCO1's copper-coordinating cysteines during maturation of the CuA site of COX subunit II (PMID:18458339, PMID:19336478, PMID:11546815). Beyond COX assembly, SCO1 participates in a mitochondria-to-cytoplasm signaling pathway that post-translationally controls CTR1-dependent copper import in a tissue-specific manner—stabilizing CTR1 protein levels in liver and maintaining its plasma-membrane localization in heart—and copper-loaded SCO1 bridges LKB1 to AMPK to activate fatty acid oxidation (PMID:25683716, PMID:28973536, PMID:36261001). Biallelic loss-of-function mutations in human SCO1 cause isolated COX deficiency presenting with neonatal hepatic failure and cardiomyopathy (PMID:11013136, PMID:28973536).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 1988 High

    Established that Sco1 is required post-transcriptionally for cytochrome c oxidase subunit II accumulation, defining its entry point in COX biogenesis.

    Evidence Northern blot and mitochondrial translation analysis in yeast sco1 mutants

    PMID:2835635

    Open questions at the time
    • Mechanism of action unknown
    • Whether Sco1 functions directly on CoxII or on an upstream factor unclear
  2. 1991 High

    Demonstrated that Sco1 is anchored to the mitochondrial inner membrane via an N-terminal hydrophobic segment, and this membrane association is essential for function.

    Evidence Subcellular fractionation, alkaline extraction, sucrose gradient centrifugation, and truncation mutagenesis in yeast

    PMID:1944230 PMID:2543907

    Open questions at the time
    • Topology relative to the inner membrane not fully resolved
    • No structural information yet available
  3. 1996 High

    Genetic suppressor analysis placed Sco1 in the mitochondrial copper delivery pathway downstream of Cox17, revealing that Sco1 mediates copper supply to COX.

    Evidence Multicopy suppressor screen and respiratory rescue assays in cox17 and sco1 null yeast

    PMID:8702795

    Open questions at the time
    • Direct copper binding by Sco1 not yet demonstrated
    • Relationship between Sco1 and Sco2 only partially defined
  4. 2001 High

    Biochemical and spectroscopic studies showed Sco1 binds one Cu(I) per monomer via two cysteines of the CXXXC motif and a histidine in trigonal coordination, and each ligand is essential for COX activity.

    Evidence X-ray absorption spectroscopy of purified yeast Sco1 combined with site-directed mutagenesis and in vivo respiratory assays

    PMID:11546815

    Open questions at the time
    • Mechanism of copper transfer from Cox17 to Sco1 unknown
    • Whether Cu(II) binding is physiologically relevant unclear
  5. 2003 High

    Structural determination revealed that Sco1 adopts a thioredoxin-like fold, and assembly intermediate analysis in patient cells showed that SCO1 loss blocks CuA maturation of COX2, arresting a specific subassembly.

    Evidence NMR structure of B. subtilis Sco1; blue-native PAGE of COX subassemblies in human SCO1-deficient fibroblasts

    PMID:14604533 PMID:14607829

    Open questions at the time
    • How Sco1 physically engages COX2 to deliver copper not resolved
    • Role of redox state transitions during assembly unclear
  6. 2004 High

    Reconstituted in vitro copper transfer demonstrated that Cox17 directly and specifically delivers Cu(I) to Sco1, and cooperative but non-overlapping roles of SCO1 and SCO2 in human COX assembly were established.

    Evidence Purified protein copper-transfer assays, yeast co-expression, overexpression/rescue experiments in human SCO-patient fibroblasts

    PMID:15199057 PMID:15229189

    Open questions at the time
    • Nature of the SCO1–SCO2 physical interaction unclear
    • Whether electron transfer accompanies copper transfer not yet shown
  7. 2006 High

    NMR and crystallographic structures of human Sco1 in apo, Cu(I), and Cu(II) states showed that copper binding converts the protein from a flexible open conformation to a rigid closed state; the P174L pathogenic mutation was shown to reduce Cu(I) affinity ~10,000-fold and impair Cox17-to-Sco1 copper transfer.

    Evidence NMR and X-ray crystallography of human and yeast Sco1, copper-binding KD measurements, in vitro transfer assays

    PMID:16520371 PMID:16570183 PMID:16735468 PMID:17182746

    Open questions at the time
    • Structural basis of Cox17–Sco1 complex not resolved
    • Mechanism linking P174L to hepatic failure vs. other tissue phenotypes unknown
  8. 2008 High

    A coupled copper-electron transfer mechanism was demonstrated: partially oxidized Cox17 simultaneously delivers Cu(I) and two electrons to disulfide-form Sco1, yielding Cu(I)-Sco1 and fully oxidized Cox17—a reaction specific to Sco1 and not Sco2.

    Evidence In vitro assays with purified human proteins monitored by NMR and ESI-MS

    PMID:18458339

    Open questions at the time
    • Whether this mechanism operates the same way within the lipid bilayer in vivo not confirmed
    • How Sco1 subsequently donates copper to COX2 CuA site unknown
  9. 2009 High

    Epistatic ordering was refined: SCO2 acts upstream of SCO1 as a thiol-disulfide oxidoreductase that oxidizes SCO1's copper-coordinating cysteines, and both form a complex during COX2 CuA maturation.

    Evidence Pulse-labeling of mitochondrial translation products, RNAi, and cysteine redox-state analysis in human patient and control cells

    PMID:19336478

    Open questions at the time
    • Stoichiometry and structure of the SCO1–SCO2 complex undefined
    • Whether additional redox partners participate unknown
  10. 2014 High

    COX20 was identified as an early chaperone that presents newly synthesized COX2 to the SCO1/SCO2 metallochaperone module, placing COX20 upstream in the assembly pathway.

    Evidence siRNA/TALEN knockouts, FLAG-IP, and assembly intermediate analysis in human cells

    PMID:24403053

    Open questions at the time
    • Whether SCO1 contacts COX20 directly or only COX20-bound COX2 not resolved
    • Kinetics of handoff from COX20 to SCO module unknown
  11. 2015 High

    A role for SCO1 beyond COX assembly was established: SCO1 maintains CTR1 protein stability in liver by preventing its proteasomal degradation, linking mitochondrial copper signaling to cellular copper import.

    Evidence Liver-specific Sco1 knockout mouse, CTR1 immunoblot, proteasome-inhibitor rescue in MEFs

    PMID:25683716

    Open questions at the time
    • Identity of the mitochondria-to-cytoplasm signal unknown
    • Whether a direct SCO1-CTR1 interaction occurs undetermined
  12. 2017 High

    Tissue-specificity of the copper-homeostasis function was delineated: in cardiomyocytes, SCO1 maintains CTR1 at the plasma membrane rather than protecting its stability, and loss causes dilated cardiomyopathy.

    Evidence Heart-specific Sco1 knockout and G115S knockin mice, CTR1 immunofluorescence, echocardiography

    PMID:28973536

    Open questions at the time
    • Mechanism by which mitochondrial SCO1 status influences CTR1 trafficking in heart unknown
    • Whether the CTR1-regulatory and COX-assembly functions are separable in vivo undetermined
  13. 2022 Medium

    Copper-loaded SCO1 was found to bridge LKB1 to AMPK, activating AMPK to promote fatty acid oxidation, revealing a copper-sensing signaling function for SCO1 independent of COX assembly.

    Evidence Co-immunoprecipitation, mouse liver ceruloplasmin knockout model, AMPK activity and fatty acid oxidation assays

    PMID:36261001

    Open questions at the time
    • Ternary complex not reconstituted with purified components in vitro
    • Structural basis for copper-dependent AMPK recruitment unknown
    • Whether this function operates in tissues beyond liver not established

Open questions

Synthesis pass · forward-looking unresolved questions
  • Major open questions include the identity of the signal linking mitochondrial SCO1 to cytoplasmic CTR1 regulation, the structural basis of SCO1–COX2 copper transfer, and whether the COX-assembly and copper-homeostasis functions of SCO1 are genetically separable.
  • No structure of a SCO1–COX2 or SCO1–SCO2 complex
  • Mitochondria-to-cytoplasm retrograde signal mediating CTR1 regulation unidentified
  • Relative contributions of COX-assembly vs. copper-homeostasis roles to human disease phenotypes not delineated

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 4 GO:0140104 molecular carrier activity 4
Localization
GO:0005739 mitochondrion 3 GO:0043226 organelle 2
Pathway
R-HSA-1852241 Organelle biogenesis and maintenance 6 R-HSA-382551 Transport of small molecules 5 R-HSA-1643685 Disease 2 R-HSA-1430728 Metabolism 1
Partners
COX17COX2COX20CTR1LKB1PRKAA1SCO2
Complex memberships
SCO1-LKB1-AMPK signaling complexSCO1-SCO2 metallochaperone module

Evidence

Reading pass · 26 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1988 Yeast SCO1 gene is required for a post-transcriptional step in the accumulation of mitochondrially synthesized cytochrome c oxidase subunit II (CoxII), as CoxII mRNA levels are normal but protein accumulation is lost in sco1 mutants. Northern blot hybridization and mitochondrial translation analysis in sco1-1 mutant yeast Molecular & general genetics : MGG High 2835635
1989 Yeast Sco1 protein is imported into mitochondria and is tightly associated with the mitochondrial inner membrane; a 33 kDa precursor is processed to a 30 kDa mature form. In vitro transcription/translation combined with mitochondrial import assay and protease protection Molecular & general genetics : MGG High 2543907
1990 Yeast SCO1 is required for a post-translational step involving protection of newly synthesized COX subunits I and II from proteolytic degradation, not for their translation. Pulse-chase labeling of mitochondrial translation products in sco1 deletion yeast Current genetics High 2173976
1991 Yeast Sco1 protein localizes to the inner mitochondrial membrane; membrane anchoring via a stretch of 17 hydrophobic amino acids in the N-terminal region is required for its biological function. Immunoblot of subcellular fractions, alkaline extraction, isopycnic sucrose gradient centrifugation, digitonin treatment, and truncation mutagenesis Molecular & general genetics : MGG High 1944230
1996 Yeast SCO1 and SCO2 suppress a mitochondrial copper recruitment defect in cox17 mutants, and SCO1 overexpression compensates for absence of COX17, indicating Sco1 functions in mitochondrial copper transport or insertion into the COX active site; SCO2 cannot suppress sco1 null mutants, showing overlapping but non-identical functions. Multicopy suppressor screen, respiratory growth rescue assays, genetic epistasis in S. cerevisiae The Journal of biological chemistry High 8702795
2000 Compound heterozygous mutations in human SCO1 (frameshift ΔGA and P174L missense adjacent to the CxxxC copper-binding domain) cause isolated COX deficiency with neonatal hepatic failure, establishing SCO1 as essential for COX assembly in humans. Chromosomal mapping, mutation screening by sequencing, mRNA stability analysis in patient cells American journal of human genetics High 11013136
2001 Yeast Sco1 binds one Cu(I) per monomer via a CXXXC motif and a conserved histidine (trigonal coordination); mutation of any of these three ligands abolishes Sco1 function and cytochrome c oxidase activity; Sco1 may be oligomeric in vivo. X-ray absorption spectroscopy of purified protein, site-directed mutagenesis with in vivo functional assay, size-exclusion chromatography of mitochondrial lysates The Journal of biological chemistry High 11546815
2003 The solution NMR structure of Sco1 from Bacillus subtilis shows a thioredoxin-like fold with the CXXXCP copper-binding motif and His135 as ligands; the protein can bind Cu(I) and Cu(II) in vitro, establishing Sco1 as a distinct subgroup within the thioredoxin superfamily. NMR solution structure determination, in vitro copper-binding assays Structure High 14604533
2003 SCO1-deficient fibroblasts accumulate a COX subassembly containing MTCO1, COX4, and COX5A but lacking MTCO2, indicating SCO1 is required for Cu(A) center formation in MTCO2 prior to its incorporation into this subassembly. Blue native PAGE immunoblot analysis of COX subassemblies in patient fibroblasts The Journal of biological chemistry High 14607829
2004 Cox17 directly and specifically transfers copper to both Sco1 and Cox11 in vitro; the C57Y mutant of Cox17 transfers copper to Cox11 but not to Sco1; metallation of soluble Sco1 in the yeast cytoplasm is strictly dependent on co-expression of Cox17. In vitro copper transfer assays with purified proteins, yeast cytoplasmic co-expression system The Journal of biological chemistry High 15199057
2004 Human SCO1 and SCO2 have non-overlapping, cooperative functions in mitochondrial copper delivery to COX; overexpression of COX17 rescues COX deficiency in SCO2 but not SCO1 patient cells; overexpression of either SCO protein in the reciprocal patient background produces a dominant-negative phenotype, implying a physical SCO1-SCO2 interaction; both proteins function as homodimers by size exclusion chromatography. Immunoblot analysis, COX17 overexpression rescue assays, chimeric protein complementation, size exclusion chromatography of patient cell lysates Human molecular genetics High 15229189
2005 Human Sco1 and Sco2 bind both Cu(I) (trigonal geometry via two conserved cysteines and a histidine) and Cu(II) (type II site); an aspartate residue (Asp238 in human Sco1) is required for Cu(II) binding and in vivo function; the Cu(II) state is resistant to weak reductants. Purified protein expression in bacteria and yeast, X-ray absorption spectroscopy, UV-visible spectroscopy, site-directed mutagenesis with functional assays in yeast The Journal of biological chemistry High 16091356
2005 Crystal structure of human SCO1 (apo form, 2.8 Å) reveals a thioredoxin/peroxiredoxin-like fold with putative copper-binding ligands at the positions of catalytic residues; human SCO1 and a yeast sco1 null exhibit extreme sensitivity to hydrogen peroxide, suggesting a redox signaling role. X-ray crystallography, hydrogen peroxide sensitivity assay in yeast and human cells The Journal of biological chemistry High 15659396
2006 The pathogenic P174L mutation in human Sco1 reduces the affinity of the protein for Cu(I) by ~10,000-fold and impairs copper transfer from Cox17 to Sco1, without abolishing copper binding; it also causes conformational changes around the metal-binding site and slower redox kinetics. NMR solution structure of mutant Cu(I)-Sco1, KD measurements, in vitro Cox17-to-Sco1 copper transfer assays, yeast cytoplasmic complementation assay, pulse-chase labeling of mitochondrial translation products in patient fibroblasts Proceedings of the National Academy of Sciences of the United States of America High 16520371 17182746
2006 Solution structures of apo, Cu(I), and Ni(II) human Sco1 show that metal binding converts the protein from an open, conformationally mobile state to a closed, rigid conformation; Cu(I) is coordinated by two Cys of the CPXXCP motif and a His residue; an additional ligand (possibly Asp) completes the Ni(II) coordination sphere, suggesting the oxidized Cys form may also be competent for metal binding. NMR solution structure determination, electrospray ionization mass spectrometry, X-ray crystallography of Ni(II) derivative Proceedings of the National Academy of Sciences of the United States of America High 16735468
2006 Crystal structures of yeast apo-Sco1 (1.8 Å) and copper-soaked Sco1 (2.3 Å) reveal a thioredoxin-like fold; the conserved CXXXC cysteines (Cys148/Cys152) undergo redox chemistry; an essential His239 on a flexible 'Sco loop' can adopt positions proximal to two pairs of cysteines; complementary electrostatic surfaces suggest COX17 and COX2 interaction sites. X-ray crystallography Journal of biological inorganic chemistry High 16570183
2007 Human SCO1 and SCO2 have additional roles in cellular copper homeostasis beyond COX assembly; mutations in either SCO cause a tissue- and allele-specific cellular copper deficiency driven by increased copper efflux rather than reduced uptake; SCO2, but not SCO1, overexpression suppresses the copper-deficiency phenotype, suggesting a mitochondrial signaling pathway through SCO1 and SCO2 regulating cellular copper content. Copper efflux/uptake assays, shRNA knockdown and overexpression in patient fibroblasts, immunoblot analysis Cell metabolism High 17189203
2008 Human Cox17 in its partially oxidized form (two S-S bonds, two reduced Cys) simultaneously transfers Cu(I) and two electrons to oxidized human Sco1 (disulfide form), yielding Cu(I)-Sco1 and fully oxidized Cox17; the same coupled electron-copper transfer does not occur with human Sco2, due to absence of a specific metal-bridged protein-protein complex between Cox17 and Sco2. In vitro biochemical assays with purified recombinant proteins, NMR, electrospray ionization MS Proceedings of the National Academy of Sciences of the United States of America High 18458339
2009 SCO2 acts upstream of SCO1 and is indispensable for COX II synthesis; SCO2 functions as a thiol-disulfide oxidoreductase that oxidizes the copper-coordinating cysteines in SCO1 during COX II maturation; both SCO proteins form a complex and each fulfills distinct stage-specific functions in COX II synthesis and CuA site maturation. Pulse-labeling of mitochondrial translation products, RNAi knockdown of SCO proteins, redox state analysis of SCO1 cysteines in patient and control cells Human molecular genetics High 19336478
2009 A fraction of Sco1 physically associates with the assembled COX complex in human muscle mitochondria, as demonstrated by co-immunoprecipitation and blue native immunoblot; a G132S mutation in the Sco1 juxtamembrane region impairs protein stability and abolishes Sco1 oligomerization. Blue native PAGE, co-immunoprecipitation, immunoblot of patient muscle mitochondria American journal of physiology. Cell physiology Medium 19295170
2011 Despite global cellular copper deficiency in SCO1 and SCO2 patient fibroblasts, total copper and exchangeable mitochondrial Cu(+) pools are maintained at near-normal levels, revealing that cells prioritize mitochondrial copper homeostasis even when overall copper is limiting. Mitochondria-targeted fluorescent Cu(+) sensor (Mito-CS1) imaging in living cells combined with biochemical copper measurements Journal of the American Chemical Society High 21563821
2014 COX20 acts as an early chaperone for newly synthesized COX2, stabilizing it and presenting it to the SCO1/SCO2 metallochaperone module; SCO1 and SCO2 act on COX20-bound COX2 to mature the CuA site; absence of COX20 causes COX2 instability and accumulation of COX subassemblies similar to those in SCO1/SCO2 patient cells. siRNA knockdown, TALEN knockout, immunoprecipitation of COX20-FLAG in stable cell lines, mitochondrial subassembly analysis Human molecular genetics High 24403053
2015 SCO1 is required to maintain CTR1 (the high-affinity copper importer) at steady-state levels; in Sco1-/- mouse embryonic fibroblasts, CTR1 protein is rapidly degraded and its levels are restored by proteasome inhibition, establishing a post-translational mechanism by which mitochondrial SCO1 signaling regulates CTR1-dependent copper import. Liver-specific Sco1 knockout mouse model, immunoblot of CTR1, proteasome inhibitor rescue experiment in MEFs Cell reports High 25683716
2017 In the heart, SCO1 maintains CTR1 at the plasma membrane rather than controlling its total protein level; deletion or functional mutation of Sco1 in cardiomyocytes causes mislocalization of CTR1 to the cytosol and a resulting copper deficiency leading to dilated cardiomyopathy; this is distinct from the liver mechanism where SCO1 loss leads to CTR1 protein degradation. Heart/striated muscle-specific Sco1 knockout and G115S knockin mouse models, immunofluorescence microscopy of CTR1 localization, copper measurements, echocardiography Human molecular genetics High 28973536
2022 Copper-loaded SCO1 forms a complex with LKB1 and AMPK; copper-loaded SCO1 directly tethers LKB1 to AMPK, thereby activating AMPK and promoting mitochondrial biogenesis and fatty acid oxidation; SCO1 constitutively interacts with LKB1 even without copper, but copper loading is required to recruit AMPK. Co-immunoprecipitation, mouse liver Cp knockout model, AMPK activity assays, fatty acid oxidation measurements Cell reports Medium 36261001
1998 Human SCO1 protein contains a mitochondrial targeting sequence and is imported into mitochondria, as confirmed by in vitro import and protease-protection assay, consistent with a role in respiratory chain biogenesis. In vitro import assay with protease protection on isolated mitochondria Genomics High 9878253

Source papers

Stage 0 corpus · 50 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2000 Mutations of the SCO1 gene in mitochondrial cytochrome c oxidase deficiency with neonatal-onset hepatic failure and encephalopathy. American journal of human genetics 289 11013136
1996 SCO1 and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae. The Journal of biological chemistry 278 8702795
2004 Specific copper transfer from the Cox17 metallochaperone to both Sco1 and Cox11 in the assembly of yeast cytochrome C oxidase. The Journal of biological chemistry 243 15199057
2011 A targetable fluorescent sensor reveals that copper-deficient SCO1 and SCO2 patient cells prioritize mitochondrial copper homeostasis. Journal of the American Chemical Society 206 21563821
2004 Human SCO1 and SCO2 have independent, cooperative functions in copper delivery to cytochrome c oxidase. Human molecular genetics 203 15229189
2007 The human cytochrome c oxidase assembly factors SCO1 and SCO2 have regulatory roles in the maintenance of cellular copper homeostasis. Cell metabolism 178 17189203
2008 Mitochondrial copper(I) transfer from Cox17 to Sco1 is coupled to electron transfer. Proceedings of the National Academy of Sciences of the United States of America 160 18458339
2001 Yeast Sco1, a protein essential for cytochrome c oxidase function is a Cu(I)-binding protein. The Journal of biological chemistry 159 11546815
2005 Human Sco1 and Sco2 function as copper-binding proteins. The Journal of biological chemistry 136 16091356
2009 Human SCO2 is required for the synthesis of CO II and as a thiol-disulphide oxidoreductase for SCO1. Human molecular genetics 134 19336478
1998 Identification and characterization of human cDNAs specific to BCS1, PET112, SCO1, COX15, and COX11, five genes involved in the formation and function of the mitochondrial respiratory chain. Genomics 122 9878253
2003 Cytochrome c oxidase subassemblies in fibroblast cultures from patients carrying mutations in COX10, SCO1, or SURF1. The Journal of biological chemistry 115 14607829
2003 Solution structure of Sco1: a thioredoxin-like protein Involved in cytochrome c oxidase assembly. Structure (London, England : 1993) 105 14604533
2006 Human Sco1 functional studies and pathological implications of the P174L mutant. Proceedings of the National Academy of Sciences of the United States of America 101 17182746
1988 SCO1, a yeast nuclear gene essential for accumulation of mitochondrial cytochrome c oxidase subunit II. Molecular & general genetics : MGG 100 2835635
2005 Crystal structure of human SCO1: implications for redox signaling by a mitochondrial cytochrome c oxidase "assembly" protein. The Journal of biological chemistry 99 15659396
2016 Transcriptome analysis of copper homeostasis genes reveals coordinated upregulation of SLC31A1,SCO1, and COX11 in colorectal cancer. FEBS open bio 88 27516958
2014 Human COX20 cooperates with SCO1 and SCO2 to mature COX2 and promote the assembly of cytochrome c oxidase. Human molecular genetics 85 24403053
2009 Loss of function of Sco1 and its interaction with cytochrome c oxidase. American journal of physiology. Cell physiology 83 19295170
2006 A hint for the function of human Sco1 from different structures. Proceedings of the National Academy of Sciences of the United States of America 83 16735468
1989 Accumulation of the cytochrome c oxidase subunits I and II in yeast requires a mitochondrial membrane-associated protein, encoded by the nuclear SCO1 gene. Molecular & general genetics : MGG 80 2543907
1991 Immunological identification of yeast SCO1 protein as a component of the inner mitochondrial membrane. Molecular & general genetics : MGG 71 1944230
1990 Yeast SCO1 protein is required for a post-translational step in the accumulation of mitochondrial cytochrome c oxidase subunits I and II. Current genetics 66 2173976
2006 Crystal structure of yeast Sco1. Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry 62 16570183
2022 Downregulation of hepatic ceruloplasmin ameliorates NAFLD via SCO1-AMPK-LKB1 complex. Cell reports 50 36261001
2015 The Mitochondrial Metallochaperone SCO1 Is Required to Sustain Expression of the High-Affinity Copper Transporter CTR1 and Preserve Copper Homeostasis. Cell reports 40 25683716
2007 Identification of the novel narrow-spectrum beta-lactamase SCO-1 in Acinetobacter spp. from Argentina. Antimicrobial agents and chemotherapy 40 17420213
1999 Human members of the SCO1 gene family: complementation analysis in yeast and intracellular localization. FEBS letters 36 10218584
2010 HCC1, the Arabidopsis homologue of the yeast mitochondrial copper chaperone SCO1, is essential for embryonic development. Journal of experimental botany 33 21041373
1994 The complete sequence of a 33 kb fragment on the right arm of chromosome II from Saccharomyces cerevisiae reveals 16 open reading frames, including ten new open reading frames, five previously identified genes and a homologue of the SCO1 gene. Yeast (Chichester, England) 31 8091864
2000 Characterization of human SCO1 and COX17 genes in mitochondrial cytochrome-c-oxidase deficiency. Biochemical and biophysical research communications 30 11027508
2006 The P174L mutation in human Sco1 severely compromises Cox17-dependent metallation but does not impair copper binding. The Journal of biological chemistry 29 16520371
2017 The mitochondrial metallochaperone SCO1 maintains CTR1 at the plasma membrane to preserve copper homeostasis in the murine heart. Human molecular genetics 28 28973536
2011 Pleiotropic role of the Sco1/SenC family copper chaperone in the physiology of Streptomyces. Microbial biotechnology 26 22117562
2010 Genetic, functional and evolutionary characterization of scox, the Drosophila melanogaster ortholog of the human SCO1 gene. Mitochondrion 19 20388558
2010 Unexpected vascular enrichment of SCO1 over SCO2 in mammalian tissues: implications for human mitochondrial disease. The American journal of pathology 14 20864674
2010 The cardiac copper chaperone proteins Sco1 and CCS are up-regulated, but Cox 1 and Cox4 are down-regulated, by copper deficiency. Biological trace element research 14 20878365
2003 Purification, crystallization and preliminary X-ray analysis of a Sco1-like protein from Bacillus subtilis, a copper-binding protein involved in the assembly of cytochrome c oxidase. Acta crystallographica. Section D, Biological crystallography 11 12832793
2019 Mitochondrial Disease Caused by a Novel Homozygous Mutation (Gly106del) in the SCO1 Gene. Neonatology 10 31352446
2017 Synthesis of cytochrome c oxidase 1 (SCO1) inhibits insulin sensitivity by decreasing copper levels in adipocytes. Biochemical and biophysical research communications 9 28647369
1991 AUG codons in the RNA leader sequences of the yeast PET genes CBS1 and SCO1 have no influence on translation efficiency. Current genetics 9 1782674
2010 Demethyl fruticulin A (SCO-1) causes apoptosis by inducing reactive oxygen species in mitochondria. Journal of cellular biochemistry 8 20683904
2021 Expression of SCO1 and SCO2 after form-deprivation myopia in Guinea pigs. European journal of ophthalmology 7 34962434
2003 Let's Sco1, Oxidase! Let's Sco! Structure (London, England : 1993) 3 14604519
2025 Lymphopoiesis is attenuated upon hepatocyte-specific deletion of the cytochrome c oxidase assembly factor Sco1. iScience 2 40177634
2025 Heart is the most susceptible organ in an isogenic background to loss of function mutations in the mitochondrial metallochaperone SCO1. Human molecular genetics 2 40679281
2024 Endocrinological features and epileptic encephalopathy in COX deficiency due to SCO1 mutations: case series and review of literature. Endocrine connections 2 39214134
2012 Evaluation of SCO1 deletion on Saccharomyces cerevisiae metabolism through a proteomic approach. Proteomics 2 22623105
2025 Detection of rare β-lactamase bla SCO-1 from a Klebsiella pneumoniae high-risk clone in Peru. JAC-antimicrobial resistance 1 40421127
2025 [Role of SCO1 in regulating microglial mitochondrial copper accumulation in neurological damage of mice exposed to lead and high-glucose diet]. Wei sheng yan jiu = Journal of hygiene research 0 40695768