Affinage

COX17

Cytochrome c oxidase copper chaperone · UniProt Q14061

Length
63 aa
Mass
6.9 kDa
Annotated
2026-04-28
40 papers in source corpus 20 papers cited in narrative 20 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

COX17 is a mitochondrial intermembrane space (IMS) copper chaperone essential for the assembly of cytochrome c oxidase (complex IV). Fully reduced Cox17 enters the IMS from the cytoplasm and is oxidized by Mia40 to the functional Cox17(2S-S) form—a coiled-coil-helix-coiled-coil-helix domain stabilized by two disulfide bonds—which binds a single Cu(I) ion via the Cys22-Cys23 motif and is thereby trapped in the IMS (PMID:18093982, PMID:8662933, PMID:15893662). Cu(I)-loaded Cox17(2S-S) transfers copper directly to Sco1 (for the CuA site of CoxII) through a redox-coupled mechanism that simultaneously delivers two electrons to oxidized Sco1, and independently to Cox11 (for the CuB site), with specificity enforced by transient protein–protein interactions (PMID:15199057, PMID:18458339). Beyond copper delivery, Cox17 interacts with the MICOS component Mic60 in a copper-regulated manner to maintain mitochondrial inner membrane architecture, and is acetylated by the MOF-KANSL complex to sustain complex IV integrity and cristae organization (PMID:25918166, PMID:37813994).

Mechanistic history

Synthesis pass · year-by-year structured walk · 15 steps
  1. 1996 High

    The identification of COX17 as a gene required for cytochrome c oxidase assembly whose null phenotype is rescued by exogenous copper established that a dedicated protein exists for copper delivery to mitochondria, rather than copper trafficking being a passive process.

    Evidence Yeast null mutant analysis with copper supplementation rescue and subcellular fractionation

    PMID:8662933

    Open questions at the time
    • Copper-binding stoichiometry and mechanism unknown
    • Whether Cox17 acts inside or outside mitochondria unresolved
    • No mammalian homolog characterized
  2. 1997 High

    Functional complementation of yeast cox17Δ by human COX17 cDNA established evolutionary conservation of this copper chaperone, validating yeast studies for understanding the human pathway.

    Evidence Heterologous complementation of yeast cox17 mutant with human cDNA library

    PMID:9050918

    Open questions at the time
    • Human Cox17 biochemical properties uncharacterized
    • Downstream copper acceptors unknown
  3. 1998 High

    Spectroscopic characterization revealed that Cox17 binds Cu(I) as a labile binuclear cuprous-thiolate cluster, explaining its chaperone function: tight enough to sequester copper yet labile enough to donate it.

    Evidence EXAFS and luminescence spectroscopy on purified Cox17

    PMID:9585572

    Open questions at the time
    • Copper transfer targets not identified
    • Redox states of Cox17 not distinguished
    • Oligomeric state not defined
  4. 2000 High

    Mutagenesis of the conserved Cys-Cys-X-Cys motif identified three cysteines (C23, C24, C26 in yeast) as essential for function, pinpointing the critical copper-binding and/or structural determinants; the C57Y mutant dissociated copper binding from mitochondrial retention.

    Evidence Site-directed mutagenesis with respiratory growth and cytochrome oxidase activity assays in yeast

    PMID:10970896

    Open questions at the time
    • Whether defect is in binding, transfer, or localization not fully separated
    • Structural basis for cysteine requirements unknown
  5. 2001 High

    Discovery that Cox17 forms oligomers (dimer–tetramer equilibrium) with the tetramer predominating in mitochondria revealed that oligomeric state correlates with subcellular function, with the essential Cys residues required for tetramerization.

    Evidence Analytical ultracentrifugation, XAS, mutagenesis, and subcellular fractionation in yeast

    PMID:11170391

    Open questions at the time
    • Whether tetramer is the active copper-donating species unclear
    • Role of oligomerization in copper transfer untested
  6. 2003 High

    Tethering Cox17 to the mitochondrial inner membrane fully rescued cox17Δ, resolving the long-standing question of where Cox17 acts: its essential function is confined to the IMS, and a C-terminal amphipathic helix mediates import independently of the copper-binding motif.

    Evidence Sco2-transmembrane domain fusion rescue, respiratory growth, and cytochrome oxidase activity in yeast

    PMID:14615477

    Open questions at the time
    • Import mechanism (Mia40 involvement) not yet demonstrated
    • Downstream IMS acceptors not biochemically identified
  7. 2004 High

    Reconstituted copper transfer from Cox17 to both Sco1 and Cox11 in vitro identified the two direct downstream acceptors, defining the branching pathway for CuA and CuB site assembly; structural studies and redox-state characterization revealed three distinct oxidation states (0S-S, 2S-S, 3S-S) with different copper-binding capacities.

    Evidence In vitro copper transfer assays with purified proteins, yeast cytoplasmic co-expression, NMR structure, ESI-MS, and redox analysis

    PMID:15142040 PMID:15199057 PMID:15465825

    Open questions at the time
    • Which oxidation state is the physiological copper donor in the IMS not established
    • Mechanism of copper release during transfer unknown
    • How Mia40 connects to Cox17 redox states untested
  8. 2005 High

    NMR structure of oxidized apoCox17 revealed a coiled-coil fold stabilized by two disulfide bonds with a disulfide isomerization step required before Cu(I) binding, providing the first structural model for how redox switching gates copper loading.

    Evidence NMR structure determination with disulfide bond mapping and copper-binding assays

    PMID:15893662

    Open questions at the time
    • Kinetics of disulfide isomerization in the IMS unknown
    • Coupling to Mia40-dependent oxidative folding not shown
  9. 2007 High

    NMR structure of human Cox17(2S-S) and full redox thermodynamic characterization established that Cox17(2S-S)—with Cu(I) coordinated by the unique Cys22-Cys23 motif—is the functional IMS species, and that fully reduced Cox17 imported from the cytoplasm is oxidized by Mia40 to generate this form.

    Evidence NMR structure, redox potential measurements, ESI-MS, and XAS on human and mammalian Cox17

    PMID:17672825 PMID:18093982

    Open questions at the time
    • Direct demonstration of Mia40-dependent trapping in vivo pending
    • Whether Cox17(0S-S) has any IMS role unclear
  10. 2008 High

    The discovery that Cu(I) transfer from Cox17(2S-S) to oxidized Sco1 is coupled to simultaneous two-electron transfer revealed a thermodynamically driven redox-metallation mechanism, explaining how copper insertion into the CuA site is directional and irreversible under IMS conditions.

    Evidence In vitro reconstitution with purified human proteins, NMR monitoring, and thermodynamic analysis

    PMID:18458339

    Open questions at the time
    • Structural details of the transient Cox17–Sco1 complex unresolved
    • Whether analogous redox coupling occurs for Cox11 transfer unknown
    • Specificity against Sco2 not structurally explained
  11. 2009 Medium

    siRNA knockdown in human cells demonstrated that COX17 depletion specifically blocks Cox2 incorporation and supercomplex formation, providing the first mammalian cell-based evidence that Cox17 is rate-limiting for CuA site assembly in complex IV.

    Evidence COX17 siRNA in HeLa cells with BN-PAGE and cytochrome oxidase activity

    PMID:19393246

    Open questions at the time
    • Whether CuB assembly is also affected not assessed
    • Long-term vs. acute effects not separated
    • Single cell line tested
  12. 2011 High

    Structural dissection of the two disulfide bonds in human Cox17 showed that the inner disulfide stabilizes the coiled-coil fold while the outer disulfide organizes the copper-binding site, explaining how stepwise oxidation simultaneously achieves structural maturation and functional competence.

    Evidence NMR structures and dynamics of single-disulfide Cox17 mutants

    PMID:21816817

    Open questions at the time
    • Order of disulfide formation during Mia40-catalyzed folding not determined
    • Whether partially oxidized intermediates are physiologically relevant unknown
  13. 2015 Medium

    Discovery of a copper-regulated interaction between Cox17 and the MICOS component Mic60 revealed an unexpected role for Cox17 in maintaining mitochondrial inner membrane architecture beyond its canonical copper chaperone function.

    Evidence Co-immunoprecipitation and genetic interaction analysis with copper modulation in yeast

    PMID:25918166

    Open questions at the time
    • No reciprocal structural validation of the Cox17–Mic60 interface
    • Functional consequence on cristae morphology not directly measured
    • Whether this interaction requires Cu(I)-loaded or apo Cox17 unclear
  14. 2016 Medium

    Identification of cisplatin binding at the Cox17 Cu(I)-binding cysteines demonstrated competitive coordination between the drug and copper, suggesting a molecular basis for cisplatin-induced mitochondrial toxicity through complex IV copper delivery disruption.

    Evidence Top-down FT-ICR tandem mass spectrometry on human Cox17(2S-S) treated with cisplatin

    PMID:27539433

    Open questions at the time
    • Functional consequence of cisplatin binding on copper transfer activity not tested
    • In vivo relevance at pharmacological cisplatin concentrations unknown
  15. 2023 High

    Identification of MOF-KANSL-mediated acetylation of COX17 as required for complex IV integrity and cristae maintenance revealed a previously unknown post-translational regulatory layer controlling COX17 function, with acetylation-mimetic COX17 sufficient to bypass MOF requirement.

    Evidence Mass spectrometry acetylation mapping, acetyltransferase assays, non-acetylatable/mimetic mutants, mitochondrial morphology imaging, and complex IV activity in mammalian cells

    PMID:37813994

    Open questions at the time
    • Specific acetylation site on Cox17 and its effect on copper binding not structurally characterized
    • Whether acetylation affects Cox17–Sco1 or Cox17–Mic60 interactions unknown
    • Deacetylase identity not established

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include: the structure of the transient Cox17–Sco1 and Cox17–Cox11 transfer complexes; whether redox-coupled copper transfer also occurs during Cox11 metallation; the mechanistic link between Cox17 acetylation and its copper chaperone or MICOS-related functions; and how the Cox17–Mic60 interaction remodels cristae architecture.
  • No structural model of any Cox17–partner transfer complex
  • Redox coupling to Cox11 untested
  • Acetylation–copper binding interplay unexplored

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140104 molecular carrier activity 4 GO:0098772 molecular function regulator activity 2
Localization
GO:0005739 mitochondrion 4 GO:0005829 cytosol 2
Pathway
R-HSA-1852241 Organelle biogenesis and maintenance 4 R-HSA-382551 Transport of small molecules 3
Partners
COX11MIA40MIC60MOFSCO1

Evidence

Reading pass · 20 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1996 COX17 encodes a cysteine-rich cytoplasmic protein required for cytochrome c oxidase assembly in yeast; cox17 null mutants are rescued by copper supplementation, indicating Cox17p functions specifically in copper delivery to mitochondria for cytochrome oxidase, not in general copper metabolism. Genetic complementation, null mutant rescue with copper supplementation, subcellular fractionation The Journal of biological chemistry High 8662933
1997 A human COX17 cDNA was isolated that functionally complements the yeast cox17 null mutant, establishing that the human homolog encodes a conserved copper recruitment factor for cytochrome oxidase. Heterologous complementation of yeast cox17 mutant with human cDNA expression library Human genetics High 9050918
1998 Cox17 binds Cu(I) ions as a binuclear cuprous-thiolate cluster with trigonal coordination by thiolate ligands (Cu-S bonds at 2.26 Å, Cu-Cu distance 2.7 Å); the cluster is more labile than metallothionein clusters, consistent with a copper chaperone role. X-ray absorption spectroscopy (EXAFS), UV-visible absorption and emission spectroscopy Biochemistry High 9585572
2000 Mutational analysis of yeast Cox17 identified three cysteines within a Cys-Cys-X-Cys motif (Cys23, Cys24, Cys26) as critical for function; single Cys→Ser substitution at any of these abolishes cytochrome oxidase activity. The C57Y mutation prevents mitochondrial accumulation of Cox17 but retains Cu(I) binding. Site-directed mutagenesis, growth assays on non-fermentable carbon, cytochrome oxidase activity in isolated mitochondria, Cu(I) binding assays The Journal of biological chemistry High 10970896
2001 Purified untagged Cox17 binds three Cu(I) ions per monomer in a polycopper cluster with predominantly trigonal coordination; the complex exists in a dimer/tetramer equilibrium (Kd ~20 µM). Cys→Ser substitutions at Cys23, Cys24, or Cys26 abolish tetramerization without abolishing Cu(I) binding, suggesting oligomeric state is important for function. Mitochondrial Cox17 is predominantly tetrameric; cytosolic Cox17 is primarily dimeric. X-ray absorption spectroscopy, analytical ultracentrifugation, site-directed mutagenesis, subcellular fractionation Biochemistry High 11170391
2003 Cox17 tethered to the mitochondrial inner membrane via fusion to the Sco2 transmembrane domain fully rescues respiratory growth and cytochrome oxidase activity in cox17Δ yeast, demonstrating that Cox17 function is confined to the mitochondrial intermembrane space. The C-terminal amphipathic helix of Cox17 is required for mitochondrial uptake and retention, independently of the N-terminal copper-binding motif. Fusion protein complementation, respiratory growth assays, cytochrome oxidase activity, subcellular localization by fractionation The Journal of biological chemistry High 14615477
2004 Cox17 directly transfers Cu(I) to both Sco1 and Cox11 in vitro; transfer is specific (no transfer to BSA or carbonic anhydrase). The C57Y mutant of Cox17 transfers copper to Cox11 but not to Sco1. Soluble domains of Sco1 and Cox11 expressed in the yeast cytoplasm are metallated only when Cox17 is co-expressed. In vitro copper transfer assays with purified proteins, yeast cytoplasm expression system, metal analysis The Journal of biological chemistry High 15199057
2004 NMR solution structure of yeast Cox17 reveals two α-helices with an unstructured N-terminal region; Cu(I) is modeled as two-coordinate, ligated by Cys23 and Cys26. ITC shows fully reduced Cox17 binds one Cu(I) with Ka ~6×10^6 M−1. NMR structure determination, isothermal titration calorimetry The Journal of biological chemistry High 15465825
2004 Porcine Cox17 binds cooperatively four Cu(I) ions as a Cu4S6-type cluster; ESI-MS shows three oxidative states with distinct metal-binding: Cox17(0S-S) binds four Cu(I), Cox17(2S-S) binds one Cu(I) or Zn(2+), and Cox17(3S-S) binds no metals. Apparent copper dissociation constant KCu ~13 fM. Electrospray ionization mass spectrometry (ESI-MS), fluorescence spectroscopy The Biochemical journal High 15142040
2004 Cox23p, a homolog of Cox17p, is required for cytochrome oxidase expression and is found in the mitochondrial intermembrane space; rescue of cox23 null mutant by copper requires overexpression of Cox17p. Cox23p and Cox17p are not part of a complex, suggesting they act in a common pathway with Cox17p downstream of Cox23p. Genetic epistasis, null mutant analysis, copper rescue, subcellular fractionation, co-immunoprecipitation The Journal of biological chemistry Medium 15145942
2005 NMR solution structure of oxidized apoCox17 reveals a coiled-coil fold stabilized by two disulfide bonds (Cys26/Cys57 and Cys36/Cys47). Isomerization of the Cys26/Cys57 disulfide to Cys24/Cys57 is required prior to Cu(I) binding. A fully reduced form is a molten globule that can bind up to four Cu(I) ions in a polycopper cluster and is oligomeric. NMR structure determination, disulfide bond mapping, copper-binding assays Structure High 15893662
2006 The P174L mutation in human Sco1 severely compromises Cox17-dependent copper transfer both in vitro and in a yeast cytoplasmic assay, but the mutant protein retains normal Cu(I) and Cu(II) binding. This indicates the P174L mutation attenuates a transient Cox17–Sco1 interaction required for copper transfer, not metal binding per se. In vitro copper transfer assays, yeast cytoplasmic metallation assay, pulse-chase labeling of mitochondrial translation products The Journal of biological chemistry High 16520371
2007 NMR solution structure of human Cox17(2S-S) shows a coiled-coil-helix-coiled-coil-helix domain stabilized by disulfide bonds involving Cys25-Cys54 and Cys35-Cys44, with an unstructured N-terminal tail. Cu(I) is coordinated by Cys22 and Cys23 (a Cys-Cys motif unique among copper proteins). Cox17(2S-S) is the functional IMS species that binds one Cu(I). Redox properties support import of fully reduced Cox17 into IMS where Mia40 oxidizes it to Cox17(2S-S), trapping it. NMR structure determination, redox potential measurements, backbone dynamics analysis The Journal of biological chemistry High 18093982
2007 Mammalian Cox17 exists in three oxidative states with distinct metal-binding: Cox17(0S-S) binds four Cu(I) cooperatively, Cox17(2S-S) binds one Cu(I) or Zn(2+), Cox17(3S-S) binds no metals. Midpoint redox potentials determined (Em1 = −197 mV for 3S-S↔2S-S; Em2 = −340 mV for 2S-S↔0S-S). XAS confirms Cu4Cox17 contains a Cu4S6-type cluster. IMS conditions shift equilibrium toward Cox17(2S-S). ESI-MS, X-ray absorption spectroscopy, redox potential measurements The Biochemical journal High 17672825
2008 Cu(I)-loaded human Cox17(2S-S) transfers Cu(I) and two electrons simultaneously to oxidized human Sco1 (HSco1 with disulfide at metal-binding cysteines), yielding Cu(I)HSco1 and fully oxidized apoHCox17(3S-S). This redox-coupled metallation is thermodynamically driven by copper transfer. The same reaction does not occur with HSco2 due to lack of a specific metal-bridged protein-protein complex. In vitro copper transfer and redox assays with purified human proteins, NMR, thermodynamic analysis Proceedings of the National Academy of Sciences of the United States of America High 18458339
2009 COX17 siRNA knockdown in HeLa cells reduces cytochrome c oxidase activity and assembly; early response includes disappearance of COX-containing supercomplexes; a ~150 kDa complex accumulates containing Cox1 but not Cox2, suggesting Cox17 is specifically required for copper delivery to Cox2 (CuA site). siRNA knockdown, blue native gel electrophoresis, cytochrome oxidase activity assay Journal of molecular biology Medium 19393246
2011 Structural analysis of human Cox17 mutants with only one interhelical disulfide shows that the inner disulfide (Cys36-Cys45) stabilizes interhelical hydrophobic interactions and recapitulates mature Cox17 structural dynamics, while the outer disulfide (Cys26-Cys55) is required to structurally organize the copper-binding site region. NMR structure determination of Cox17 mutants, backbone mobility analysis The Journal of biological chemistry High 21816817
2015 Cox17 directly interacts with Mic60 of the MICOS complex, modulating MICOS integrity and mitochondrial inner membrane architecture. This interaction is regulated by copper ions and does not involve Sco1. Co-immunoprecipitation, genetic interaction analysis, copper modulation experiments The Journal of biological chemistry Medium 25918166
2023 MOF (a MYST family lysine acetyltransferase) acetylates COX17 via the MOF-KANSL complex; loss of this acetylation (non-acetylatable COX17 mutant) phenocopies MOF depletion (mitochondrial fragmentation, reduced cristae density, impaired complex IV integrity), while acetylation-mimetic COX17 rescues complex IV activity even without MOF. Mass spectrometry identification of acetylation site, acetyltransferase assay, non-acetylatable and acetylation-mimetic mutants, mitochondrial morphology imaging, complex IV activity assays Nature metabolism High 37813994
2016 Cisplatin binds to Cys26 or Cys27 of human Cox17(2S-S) (the Cu(I)-binding site) as identified by top-down FT-ICR-MS/MS, providing direct evidence for competitive coordination between cisplatin and cuprous ions at the COX17 active site. High-resolution FT-ICR tandem mass spectrometry with electron capture dissociation Rapid communications in mass spectrometry Medium 27539433

Source papers

Stage 0 corpus · 40 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1996 Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase. The Journal of biological chemistry 393 8662933
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
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
1997 Isolation of a cDNA encoding the human homolog of COX17, a yeast gene essential for mitochondrial copper recruitment. Human genetics 126 9050918
2001 The mitochondrial copper metallochaperone Cox17 exists as an oligomeric, polycopper complex. Biochemistry 112 11170391
2005 Folding studies of Cox17 reveal an important interplay of cysteine oxidation and copper binding. Structure (London, England : 1993) 108 15893662
2003 Cox17 is functional when tethered to the mitochondrial inner membrane. The Journal of biological chemistry 97 14615477
1998 Characterization of the copper chaperone Cox17 of Saccharomyces cerevisiae. Biochemistry 93 9585572
2004 Yeast cox17 solution structure and Copper(I) binding. The Journal of biological chemistry 91 15465825
2007 A structural-dynamical characterization of human Cox17. The Journal of biological chemistry 86 18093982
2000 Mutational analysis of the mitochondrial copper metallochaperone Cox17. The Journal of biological chemistry 85 10970896
2004 Metal-binding mechanism of Cox17, a copper chaperone for cytochrome c oxidase. The Biochemical journal 81 15142040
2004 COX23, a homologue of COX17, is required for cytochrome oxidase assembly. The Journal of biological chemistry 70 15145942
2003 Identification of COX17 as a therapeutic target for non-small cell lung cancer. Cancer research 67 14612491
2023 Lead aggravates Alzheimer's disease pathology via mitochondrial copper accumulation regulated by COX17. Redox biology 57 38091880
2007 Oxidative switches in functioning of mammalian copper chaperone Cox17. The Biochemical journal 51 17672825
2009 Knockdown of human COX17 affects assembly and supramolecular organization of cytochrome c oxidase. Journal of molecular biology 49 19393246
2002 AtCOX17, an Arabidopsis homolog of the yeast copper chaperone COX17. Plant physiology 45 12177498
2023 COX17 restricts renal fibrosis development by maintaining mitochondrial copper homeostasis and restoring complex IV activity. Acta pharmacologica Sinica 42 37217601
2015 Cox17 Protein Is an Auxiliary Factor Involved in the Control of the Mitochondrial Contact Site and Cristae Organizing System. The Journal of biological chemistry 39 25918166
2000 Characterization and localization of human COX17, a gene involved in mitochondrial copper transport. Human genetics 31 10982038
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
2023 COX17 acetylation via MOF-KANSL complex promotes mitochondrial integrity and function. Nature metabolism 27 37813994
2019 Stable COX17 Downregulation Leads to Alterations in Mitochondrial Ultrastructure, Decreased Copper Content and Impaired Cytochrome c Oxidase Biogenesis in HEK293 Cells. Folia biologica 22 31903891
2002 Characterization and identification of promoter elements in the mouse COX17 gene. Biochimica et biophysica acta 21 11997103
2015 Glutathione selectively modulates the binding of platinum drugs to human copper chaperone Cox17. The Biochemical journal 16 26399480
2011 Functional role of two interhelical disulfide bonds in human Cox17 protein from a structural perspective. The Journal of biological chemistry 16 21816817
2022 Zebrafish cox17 modulates primitive erythropoiesis via regulation of mitochondrial metabolism to facilitate hypoxia tolerance. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 14 36208295
2006 Cox17, a copper chaperone for cytochrome c oxidase: expression, purification, and formation of mixed disulphide adducts with thiol reagents. Protein expression and purification 14 17208454
2019 Transcriptional profiles and copper stress responses in zebrafish cox17 mutants. Environmental pollution (Barking, Essex : 1987) 11 31662245
2014 Identification and initial characterisation of a Plasmodium falciparum Cox17 copper metallochaperone. Experimental parasitology 11 25447123
2018 The nonsense-mediated mRNA decay (NMD) pathway differentially regulates COX17, COX19 and COX23 mRNAs. Current genetics 10 30317392
2016 Identification of binding sites of cisplatin to human copper chaperone protein Cox17 by high-resolution FT-ICR-MS. Rapid communications in mass spectrometry : RCM 7 27539433
2009 Modulation of redox switches of copper chaperone Cox17 by Zn(II) ions determined by new ESI MS-based approach. Antioxidants & redox signaling 6 19018666
2001 Genomic structure of mouse copper chaperone, COX17. DNA sequence : the journal of DNA sequencing and mapping 4 11913776
2016 A comparative study on the interactions of human copper chaperone Cox17 with anticancer organoruthenium(II) complexes and cisplatin by mass spectrometry. Journal of inorganic biochemistry 2 27235272
2026 COX17 Attenuates Diabetes-Associated Retinal Injury by Improving Mitochondrial Function. Clinical and experimental pharmacology & physiology 0 41347662
2026 Lysophosphatidylcholine acyltransferase 1 promotes head and neck squamous cell carcinoma progression by enhancing COX17-dependent oxidative phosphorylation. Cell death discovery 0 41792107
2025 Cisplatin transported by COX17 induces cochlear damage by binding Myosin IIA to regulate cell pyroptosis induced by mitochondrial dysfunction. Life sciences 0 40945651