Affinage

ATOX1

Copper transport protein ATOX1 · UniProt O00244

Length
68 aa
Mass
7.4 kDa
Annotated
2026-06-09
100 papers in source corpus 40 papers cited in narrative 40 extracted findings
Cross-family judge vs UniProt: tie faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

ATOX1 (HAH1) is a small cytosolic copper(I) chaperone that delivers copper to the secretory pathway and coordinates intracellular copper distribution (PMID:9083055, PMID:19865834). It binds Cu(I) with sub-femtomolar affinity through a conserved Cys12-Cys15 (MTCXGC) motif in a near-linear bis-cysteinate geometry, and these cysteine ligands are obligatory for copper trafficking (PMID:9430722, PMID:12686548, PMID:21258123). ATOX1 acquires copper from the Cu-loaded C-terminal cytoplasmic tail of the importer Ctr1 in a strictly copper-dependent manner (PMID:26745413) and delivers it through direct, copper-dependent protein-protein contacts to the N-terminal metal-binding domains of the copper-transporting P-type ATPases ATP7A (Menkes) and ATP7B (Wilson), preferentially engaging domain 4 to route copper to downstream domains and thereby stimulating ATPase catalytic activity by altering inter-domain dynamics (PMID:10557326, PMID:12029094, PMID:16571664, PMID:28900031); disease-associated ATP7B N-terminal mutations weaken this interaction, linking impaired copper delivery to Wilson disease (PMID:10557326). Genetic loss of Atox1 causes intracellular copper accumulation, an efflux defect, and failure of copper-stimulated trafficking of ATP7A out of the Golgi, with loss of the normal perinuclear copper distribution (PMID:11391006, PMID:12538877, PMID:19865834). Beyond chaperone function, copper stimulates ATOX1 nuclear translocation via its C-terminal KKTGK motif, where it acts as a transcription factor binding the promoters of cyclin D1, SOD3, and MDC1 to drive proliferation, antioxidant responses, and DNA damage repair (PMID:18245776, PMID:29168020, PMID:35315340). ATOX1 redox state is governed by glutaredoxin 1 and the GSH/GSSG couple, coupling copper handling to cellular redox balance (PMID:24522867), and the protein contributes to copper-dependent cancer cell migration through an ATP7A-LOX axis (PMID:28027931, PMID:31932435). ATOX1 also binds platinum drugs such as cisplatin through the same cysteine motif and can shuttle platinum to ATP7B domains, implicating it in drug detoxification (PMID:21981264, PMID:23751120, PMID:23936210).

Mechanistic history

Synthesis pass · year-by-year structured walk · 24 steps
  1. 1997 High

    Established that ATOX1 is a bona fide copper chaperone for the secretory pathway, resolving whether the human gene had conserved metallochaperone function.

    Evidence Yeast atx1Δ complementation restoring Fet3p copper incorporation and high-affinity iron uptake

    PMID:9083055

    Open questions at the time
    • Did not identify the mammalian copper acceptor proteins
    • No structural basis for copper binding
  2. 1998 High

    Defined the molecular determinants of ATOX1's two functions, showing that the Cys12/Cys15 motif mediates copper trafficking while distinct C-terminal lysines mediate antioxidant activity.

    Evidence In vitro Cu(I) binding, site-directed mutagenesis, and yeast complementation (Fet3p and sod1Δ assays)

    PMID:9430722

    Open questions at the time
    • Mechanism of antioxidant function not defined
    • Copper acceptor still unidentified
  3. 1999 High

    Identified the physiological copper acceptors by demonstrating copper-dependent direct interaction with the Menkes and Wilson disease ATPases, linking ATOX1 to human copper disorders.

    Evidence GST pulldown and co-immunoprecipitation from human cells with mutagenesis of cysteine ligands and disease-associated ATP7B mutations

    PMID:10557326

    Open questions at the time
    • Did not establish directionality or kinetics of transfer
    • Which specific ATPase domains accept copper unresolved
  4. 2001 High

    Provided in vivo proof that ATOX1 is required for cellular copper efflux, showing its loss causes intracellular copper accumulation.

    Evidence Atox1-knockout mouse cells with metabolic copper efflux and accumulation measurements

    PMID:11391006

    Open questions at the time
    • Did not separate trafficking from transcriptional contributions to phenotype
  5. 2002 High

    Reconstituted directional copper transfer to ATP7B and demonstrated bidirectional regulation of ATPase activity, defining ATOX1 as a functional activator of the pump.

    Evidence In vitro copper transfer to N-WNDP, ATPase activity assays, and apo-Atox1 copper removal experiments

    PMID:12029094

    Open questions at the time
    • Domain-level acceptor preference not yet mapped
    • Coupling to ATP hydrolysis not structurally explained
  6. 2003 High

    Showed ATOX1 is essential for copper-stimulated Golgi-to-vesicle trafficking of ATP7A, distinguishing trafficking control from bulk copper content.

    Evidence Confocal trafficking time-course in Atox1+/+ vs Atox1−/− fibroblasts at matched copper levels

    PMID:12538877

    Open questions at the time
    • Did not address ATP7B trafficking dependence
  7. 2003 High

    Determined the Cu(I) coordination geometry and mapped chaperone binding across all six ATPase metal-binding sites, establishing the structural basis of transfer.

    Evidence XAS of Cu(I)-HAH1; yeast two-hybrid and SPR kinetics against MNK MBS1-6 with CXXC mutants

    PMID:12679332 PMID:12686548

    Open questions at the time
    • Did not resolve which MBS is the kinetically preferred acceptor
    • Functional consequence of binding all six sites unclear
  8. 2004 High

    Refined the transfer mechanism by identifying MBS2 of ATP7B as a preferential, copper-retaining acceptor and resolving the apo/holo conformational change driving transfer.

    Evidence Cysteine-protection labeling, MBS2 mutagenesis, chelator competition, XAS, and NMR of apo/Cu(I)-HAH1

    PMID:14754885 PMID:15476398

    Open questions at the time
    • Reconciliation of MBS2 preference with later domain-4 preference unresolved
    • In-cell relevance of single-domain preference not tested
  9. 2004 Medium

    Demonstrated copper-dependent ATOX1 homodimerization in vitro and in living cells, adding an oligomeric dimension to the transfer mechanism.

    Evidence Solid-phase binding, Biacore, and FRET in living cells

    PMID:15530404

    Open questions at the time
    • Functional role of dimer vs monomer in transfer not resolved here
  10. 2006 High

    Mapped the intramolecular copper routing within ATP7B, showing domains 4 and 2 are the direct HAH1 acceptors that relay copper to domains 5-6.

    Evidence NMR titration and relaxation with WLN4, WLN2, and WLN5-6 domain constructs

    PMID:16571664

    Open questions at the time
    • Did not establish which domain transfer is rate-limiting in vivo
  11. 2008 High

    Discovered a non-chaperone role for ATOX1 as a copper-dependent transcription factor driving cyclin D1 and cell proliferation, expanding its biology beyond metal delivery.

    Evidence EMSA, ChIP, Gal4 transactivation, nuclear translocation imaging, and Atox1−/− MEF rescue

    PMID:18245776

    Open questions at the time
    • Full repertoire of transcriptional targets unknown
    • Mechanism of promoter recognition by a small chaperone unclear
  12. 2008 High

    Defined kinetic control of copper release and confirmed ATP7B domain-4 preference, identifying residues that tune delivery rate.

    Evidence Stopped-flow Cu(I) displacement kinetics with Met10/Lys60 mutants; NMR of WLN3-4 interaction

    PMID:18558714 PMID:18685091

    Open questions at the time
    • In-cell impact of Met10/Lys60 mutations not tested
  13. 2009 High

    Established Lys60-driven electrostatics as the key energetic contributor to heterocomplex stability and reconciled ATPase-specific delivery modes.

    Evidence CD, gel filtration, and MD with Atox1 mutants for WD4; whole six-domain ATP7B NMR vs ATP7A; SXRF copper imaging of knockout cells

    PMID:19181666 PMID:19863064 PMID:19865834

    Open questions at the time
    • Why ATP7A and ATP7B use different numbers of acceptor domains is unexplained
  14. 2011 High

    Quantified ATOX1's sub-femtomolar Cu(I) affinity and uncovered cisplatin binding/destabilization, linking the protein to platinum-drug handling.

    Evidence Validated Cu(I) probe affinity measurements; solution and in-cell NMR and CD of cisplatin adducts

    PMID:21258123 PMID:21482801 PMID:21981264

    Open questions at the time
    • Physiological significance of cisplatin destabilization in tumors not established here
  15. 2013 Medium

    Showed ATOX1 can carry platinum along the copper export pathway and that copper and platinum can bind simultaneously, supporting a drug-detoxification model.

    Evidence XAS and in vitro Pt transfer to ATP7B MBD2/WD4; MS and XAS of Cu-S-Pt bridges with both cysteines

    PMID:23751120 PMID:23936210 PMID:28549213

    Open questions at the time
    • In vivo contribution to cisplatin resistance not quantified
    • Single-lab biophysical observations
  16. 2014 High

    Connected copper homeostasis to redox regulation by showing glutaredoxin 1 controls the redox state of the ATOX1 CXXC motif via the GSH/GSSG couple.

    Evidence In vitro redox catalysis, Cu(I) affinity, and reduction-potential measurements with cysteine mutants

    PMID:24522867

    Open questions at the time
    • In-cell relevance of redox switching to delivery rate not tested
  17. 2015 High

    Identified the upstream copper source by demonstrating ATOX1 acquires copper from the Cu-loaded Ctr1 C-terminal tail and from CCS, completing the import-to-chaperone handoff.

    Evidence Residue-level NMR and BCA competition with Ctr1 HCH peptide; SEC and NMR Cu exchange with CCS domain 1 and Atox1 Cys mutant

    PMID:25673218 PMID:26745413

    Open questions at the time
    • Directional preference between Ctr1, CCS, and ATPases under cellular copper levels unresolved
  18. 2016 Medium

    Linked ATOX1 to cell motility, showing it localizes to lamellipodia and is required for breast cancer cell migration.

    Evidence Immunostaining and wound-healing assay with siRNA knockdown

    PMID:28027931

    Open questions at the time
    • Molecular target at lamellipodia not identified in this study
  19. 2017 High

    Provided a structural-dynamic mechanism for ATPase activation and identified the membrane as a scaffold for copper loading.

    Evidence SAXS, NMR dynamics, and ATPase assays on ATP7B MBD1-3; lipid binding and in vivo copper-loading assays with Lys mutants; ChIP-based SOD3 transcription study

    PMID:24036897 PMID:28900031 PMID:29168020

    Open questions at the time
    • Transcriptional SOD3 role established in only one cell context
  20. 2019 High

    Revealed an anti-amyloid role by mapping a direct ATOX1-α-synuclein interaction that inhibits amyloid formation.

    Evidence Residue-level NMR, in-cell proximity ligation, and in vitro amyloid assays

    PMID:31600047

    Open questions at the time
    • In vivo neuroprotective relevance not established
  21. 2020 High

    Placed ATOX1 mechanistically in copper-driven cancer migration via the ATP7A-LOX axis and clarified its monomer/dimer transfer cycle.

    Evidence Single-cell tracking with siRNA and proximity ligation/LOX activity assays; EPR/QM-MM of Cu(I) coordination and dimerization; EPR transfer to ATP7B MBD1/MBD4

    PMID:31932435 PMID:32396355 PMID:32748830

    Open questions at the time
    • Whether migration phenotype reflects chaperone vs transcriptional function not fully dissected
  22. 2021 High

    Expanded the chaperone target network by identifying nuclear CRIP2 as a copper acceptor whose ATOX1-driven copper loading triggers its degradation and modulates ROS and autophagy.

    Evidence APEX2 proximity labeling/MS, Co-IP, in vitro copper transfer, and knockdown with ROS/autophagy assays

    PMID:34550632

    Open questions at the time
    • Generality of nuclear copper-transfer targeting beyond CRIP2 unknown
  23. 2022 Medium

    Extended ATOX1 transcriptional control to DNA damage repair via MDC1 and added Memo1 and zinc-bridged dimerization to its interaction repertoire.

    Evidence ChIP and promoter reporters with ATOX1 knockout xenografts and gemcitabine sensitivity; Memo1 Cu exchange and proximity ligation; Zn-loaded Atox1 crystal structure

    PMID:35315340 PMID:36067318 PMID:36291703

    Open questions at the time
    • Physiological role of zinc binding not established
    • Memo1-to-Atox1 shuttling not demonstrated in vivo
  24. 2024 Medium

    Defined a copper-dependent ATOX1-DJ-1 partnership as the basis of ATOX1's antioxidant protection, mechanistically separating it from the chaperone CXXC delivery role.

    Evidence Co-IP/MS, copper-binding mutants, DJ-1 knockdown/overexpression epistasis, and oxidative-stress assays in cells and a mouse TBI model

    PMID:38640584

    Open questions at the time
    • Direct biochemical mechanism of DJ-1-dependent protection unresolved
    • Single-lab finding

Open questions

Synthesis pass · forward-looking unresolved questions
  • How ATOX1 partitions between its cytosolic chaperone, nuclear transcription-factor, and antioxidant roles under physiological copper and redox states remains unresolved.
  • No integrated model coupling copper flux to nuclear translocation
  • Determinants of target-protein vs DNA selectivity unknown
  • In vivo significance of zinc, platinum, and α-synuclein interactions unestablished

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140104 molecular carrier activity 5 GO:0003677 DNA binding 3 GO:0140110 transcription regulator activity 3 GO:0016209 antioxidant activity 2 GO:0098772 molecular function regulator activity 2
Localization
GO:0005634 nucleus 3 GO:0005829 cytosol 3 GO:0005886 plasma membrane 2
Pathway
R-HSA-382551 Transport of small molecules 5 R-HSA-74160 Gene expression (Transcription) 3 R-HSA-8953897 Cellular responses to stimuli 3
Partners
ATP7AATP7BCCSCRIP2CTR1MEMO1PARK7SNCA

Evidence

Reading pass · 40 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1997 HAH1 (ATOX1) encodes a 68-amino acid copper-binding protein that functionally complements yeast ATX1 deletion: expression in atx1Δ yeast restores copper incorporation into the multicopper oxidase Fet3p and rescues high-affinity iron uptake, establishing its role as a copper chaperone for the secretory pathway. Yeast complementation assay (atx1Δ growth rescue, Fet3p copper incorporation) The Journal of biological chemistry High 9083055
1998 HAH1 binds Cu(I) via two conserved cysteine residues (Cys12, Cys15) in the MTCXGC motif; site-directed mutagenesis of these cysteines abrogates copper trafficking to the secretory compartment in vivo. In contrast, mutation of conserved C-terminal lysine residues eliminates antioxidant function but not copper trafficking, demonstrating that distinct residues mediate the two functions. In vitro Cu(I) binding assay with recombinant protein; site-directed mutagenesis; yeast complementation (Fet3p copper incorporation; sod1Δ antioxidant assay) The Journal of biological chemistry High 9430722
1999 HAH1 directly interacts with the Wilson disease protein (ATP7B) and the Menkes protein (ATP7A) in a copper-dependent manner; interaction requires the cysteine copper ligands in the HAH1 amino terminus. Disease-associated mutations in the N-terminus of ATP7B markedly diminish HAH1 interaction, suggesting impaired copper delivery underlies Wilson disease in those patients. GST pulldown with recombinant GST-HAH1 fusion; co-immunoprecipitation from human cell lysates; site-directed mutagenesis of cysteine ligands and disease-associated ATP7B mutations Proceedings of the National Academy of Sciences of the United States of America High 10557326
2001 Atox1-deficient (Atox1−/−) mouse cells accumulate high levels of intracellular copper due to impaired cellular copper efflux, directly demonstrating Atox1's role in trafficking copper to the secretory pathway for export. Genetic knockout mouse model; metabolic copper studies in Atox1−/− vs Atox1+/+ cells; measurement of intracellular copper accumulation and efflux Proceedings of the National Academy of Sciences of the United States of America High 11391006
2002 Atox1 transfers copper to the purified N-terminal domain of the Wilson disease protein (N-WNDP) in a dose-dependent and saturable manner (up to six copper atoms); incubation of copper-Atox1 with full-length WNDP stimulates its ATPase catalytic activity. Apo-Atox1 can remove copper from metalated N-WNDP, down-regulating WNDP activity, demonstrating bidirectional copper regulation. In vitro copper transfer assay with recombinant proteins; ATPase activity measurements; copper occupancy analysis The Journal of biological chemistry High 12029094
2003 Atox1 is essential for copper-mediated intracellular trafficking of the Menkes ATPase (ATP7A): in Atox1-deficient cells, copper-stimulated translocation of the Menkes ATPase from the Golgi compartment is significantly impaired compared to wild-type cells, even at equivalent intracellular copper content. Quantitative confocal immunofluorescence time-course in Atox1+/+ vs Atox1−/− immortalized fibroblasts; copper dose-response trafficking assays Proceedings of the National Academy of Sciences of the United States of America High 12538877
2003 X-ray absorption spectroscopy (XAS) of HAH1 reconstituted with Cu(I) reveals a linear bis-cysteinate coordination geometry (two Cu-S interactions at 2.16 Å); exogenous thiols (GSH, DTT) and phosphines can form three-coordinate adducts with Cu(I)-HAH1, with differing affinities. X-ray absorption spectroscopy (EXAFS/XANES); Cu(I) reconstitution; titration with exogenous ligands The Journal of biological chemistry High 12686548
2003 Atox1 interacts with all six metal-binding sites (MBS1–6) of the Menkes ATPase (MNK) in a copper-dependent manner; copper-dependent binding requires intact CXXC cysteine motifs. Binding constants for chaperone–MBS interactions are in the 10−5–10−6 M range and are non-cooperative. Yeast two-hybrid assay; surface plasmon resonance (SPR) kinetic analysis; site-directed mutagenesis of CXXC motifs The Journal of biological chemistry High 12679332
2004 The N-terminal metal-binding site 2 (MBS2) of the Wilson disease protein plays a preferential role in copper transfer from Atox1: copper transfer from Atox1 selectively protects MBS2 cysteines against labeling, site-directed mutagenesis of MBS2 eliminates ATPase stimulation by copper-Atox1 but not by free copper, and MBS2 retains copper better than Atox1 (demonstrated by chelator competition), facilitating directional transfer. Cysteine-directed probe labeling; site-directed mutagenesis; ATPase activity assay; copper chelator competition; X-ray absorption spectroscopy of isolated MBS2 The Journal of biological chemistry High 14754885
2004 NMR solution structure of apo- and Cu(I)-loaded HAH1 shows minor structural rearrangements upon copper binding; Cu(I) is confirmed to be two-coordinate in the holoprotein. The lower tendency of HAH1 versus orthologs to switch from two- to three-coordination may be mechanistically relevant for copper transfer. NMR solution structure determination; comparison of apo vs holo forms Biochemistry High 15476398
2004 HAH1 forms copper-dependent homodimers (apparent Kd ~6 µM) as measured by solid-phase assay and Biacore; copper-loaded HAH1 interacts independently with each of the six individual metal-binding domains of the Menkes ATPase; homodimerization was confirmed in living cells by FRET. Solid-phase binding assay; Biacore surface plasmon resonance; FRET in living cells Biochemical and biophysical research communications Medium 15530404
2006 NMR titration of the Wilson disease protein domains 5–6 (WLN5-6) with Cu(I)-HAH1 reveals no complex formation and no copper exchange, whereas HAH1 forms a fast-exchange adduct with domain 4 (WLN4) and domain 2 (WLN2). Cu(I) is transferred from WLN4 to WLN5-6 (first to WLN6, then to WLN5) without forming a detectable adduct, suggesting WLN4 and WLN2 are the direct acceptors from HAH1 that route copper to WLN5-6. NMR titration; 15N relaxation measurements; solution structure of apoWLN5-6 Proceedings of the National Academy of Sciences of the United States of America High 16571664
2008 Atox1 functions as a copper-dependent transcription factor: copper stimulates Atox1 nuclear translocation (via C-terminal KKTGK motif and N-terminal copper-binding sites), binding to a cis-element in the cyclin D1 (Ccnd1) promoter (shown by EMSA and ChIP), and transactivation of cyclin D1 expression, driving cell proliferation. Atox1−/− MEFs fail to proliferate in response to copper; re-expression of nuclear-targeted Atox1 rescues this defect. Promoter analysis; EMSA; ChIP assay; Gal4-fusion transactivation assay; Atox1−/− MEF rescue experiments; fluorescence microscopy for nuclear translocation; cell cycle analysis The Journal of biological chemistry High 18245776
2008 HAH1 forms a ~70% complex (fast exchange) with metal-binding domain 4 of ATP7B but not with domains 5–6; both domains 3 and 4 can be loaded with Cu(I) by HAH1, while domains 3 and 4 tend to aggregate in a concentration-dependent manner via nonspecific intermolecular interactions. NMR solution structure of WLN3-4; NMR interaction experiments with Cu(I)-HAH1; 15N relaxation data Biochemistry Medium 18558714
2008 Conserved residues Met10 and Lys60 modulate Cu(I) release from Atox1: both Met10Ala and Lys60Ala mutants lose Cu(I) more readily than wild-type due to more rapid displacement from the Atox1-Cu-BCA intermediate, suggesting these residues control the kinetics of copper delivery to target proteins. Cu(I) displacement kinetics using bicinchoninic acid (BCA) as metal acceptor; stopped-flow spectroscopy; point mutagenesis Proceedings of the National Academy of Sciences of the United States of America High 18685091
2009 Atox1 forms a stable Cu-dependent heterocomplex with the fourth metal-binding domain of Wilson disease protein (WD4); Lys60 is essential for adduct formation and copper transfer, while Met10 and Thr11 are dispensable for adduct formation. Electrostatic interaction mediated by Lys60 is the key energetic contributor to heterocomplex stability. Near-UV circular dichroism; gel filtration; molecular dynamics simulations; point-mutated Atox1 variants Journal of the American Chemical Society High 19863064
2009 NMR study of the entire six-domain N-terminal tail of ATP7B shows that all six metal-binding domains are metallated by Cu(I)-HAH1, with domains 1, 2, and 4 forming adducts with HAH1. This is distinct from ATP7A, where only two domains form such adducts, indicating different mechanisms of copper delivery between the two ATPases. NMR solution spectroscopy; interaction experiments with Cu(I)-HAH1 and the full-length N-terminal tail construct The Journal of biological chemistry Medium 19181666
2009 In Atox1-deficient fibroblasts, synchrotron X-ray fluorescence imaging reveals that the characteristic perinuclear copper distribution of wild-type cells is replaced by a diffuse, unstructured distribution throughout the cell, without changes in zinc or iron distribution, confirming Atox1 as a key organizer of subcellular copper localization. Quantitative synchrotron X-ray fluorescence (SXRF) imaging of Atox1+/+ vs Atox1−/− mouse fibroblasts Journal of biological inorganic chemistry Medium 19865834
2011 Atox1 binds cisplatin at its metal-binding site in both the apo and Cu-loaded forms; the resulting Atox1-cisplatin adduct is unstable over time and the protein unfolds and aggregates in a cisplatin-specific manner. In-cell NMR shows that a {Pt(NH3)2}-Atox1 adduct forms intracellularly, leading to protein dimerization and loss of ammine ligands over time. Overexpression of Atox1 in E. coli reduces DNA platination. Solution NMR; in-cell NMR spectroscopy; circular dichroism; cell filamentation assay Journal of the American Chemical Society High 21981264
2011 Cu(I) binding affinities of Atox1 and related metallochaperone proteins (including ATP7B domains 5 and 6) were unified using validated Cu(I) probes (bicinchoninic acid and bathocuproine disulfonate); Atox1-type proteins bind Cu(I) with sub-femtomolar affinities (KD values), consistent with tight buffering of labile Cu+ in cells. Competitive and non-competitive Cu(I) binding assays with four validated spectroscopic probes; quantitative affinity determination The Journal of biological chemistry High 21258123
2011 Cisplatin binds to the metal-binding site of Atox1 in vitro regardless of copper occupancy; the cisplatin-bound protein is destabilized and unfolds/aggregates over time. The unfolding effect is specific to Atox1 and not observed for two unrelated cisplatin-binding proteins. Near-UV and far-UV circular dichroism; NMR spectroscopy; in vitro protein stability assays Proceedings of the National Academy of Sciences of the United States of America High 21482801
2013 Atox1 transfers platinum (cisplatin) to the metal-binding domain 2 (MBD2) of ATP7B, producing the same Pt-cysteine adduct as direct cisplatin binding, suggesting that Pt can travel along the copper transport pathway as a mechanism of cisplatin detoxification/delivery. X-ray absorption spectroscopy; in vitro Pt transfer assays from Atox1 to MBD2 The Biochemical journal Medium 23751120
2013 Cu(I) and glutathione form large polymeric clusters that can transfer copper to Atox1; under physiological redox conditions, both copper and cisplatin bind simultaneously to Atox1 through copper-sulfur-platinum bridges involving both Cys12 and Cys15. Mass spectrometry; X-ray absorption spectroscopy; redox-controlled in vitro binding assays Biochemistry Medium 28549213
2013 Both Cys12 and Cys15 of Atox1 are required to form a simultaneous Cu-Pt di-metal complex with cisplatin; Cys41 is not involved. Atox1 can deliver cisplatin to ATP7B domain 4 (WD4) in vitro, providing evidence for a drug detoxification mechanism via the copper export pathway. Near-UV CD spectroscopy; gel filtration; strategic Atox1 point mutants; in vitro Pt transfer to WD4 PloS one Medium 23936210
2014 Human glutaredoxin 1 (hGrx1) catalyzes the interchange between dithiol and disulfide forms of the Cys12-Cys15 motif in Atox1; the direction of catalysis is regulated by the GSSG/2GSH ratio and availability of Cu(I). hGrx1 binds Cu(I) with femtomolar affinity, and the reduction potential of Atox1's CXXC motif (−188 mV) is more negative than that of hGrx1 (−118 mV), mechanistically linking copper homeostasis to redox regulation. In vitro redox catalysis assays; Cu(I) affinity measurements; reduction potential determination; mutagenesis of active-site cysteines Metallomics High 24522867
2015 The C-terminal cytoplasmic tail of Ctr1 (13-residue HCH-containing peptide) binds Cu(I) with KD ~10−14 M; Atox1 acquires Cu from the Cu-loaded Ctr1 C-terminal peptide as demonstrated by NMR at the residue level. The two proteins do not interact in the absence of Cu, indicating that Cu binding to the Ctr1 tail regulates release to downstream chaperones. NMR spectroscopy; bicinchoninic acid competition assays; site-directed mutation of HCH motif Biophysical journal High 26745413
2015 The cytoplasmic Cu chaperones Atox1 and CCS (domain 1) can exchange Cu ions in vitro; Cu transfer occurs in both directions, and mutation of the Cu-binding cysteine in Atox1 eliminates Cu transfer from CCS1, demonstrating that exchange involves the metal-binding sites. Size-exclusion chromatography with 254/280 nm ratio as Cu-loading indicator; NMR; full-length CCS transfer experiments; Atox1 Cys mutant Biometals Medium 25673218
2016 Atox1 accumulates at lamellipodia edges of migrating breast cancer cells; siRNA-mediated silencing of Atox1 reduces breast cancer cell migration (wound healing assay), suggesting a role in cell motility linked to copper chaperone function. Immunostaining and fluorescence microscopy; wound healing migration assay; siRNA knockdown Biochemical and biophysical research communications Medium 28027931
2017 The copper chaperone Atox1 regulates ATP7B catalytic activity by modulating domain dynamics of MBD1-3: copper transfer from Atox1 to ATP7B decreases domain interactions within MBD1-3 and increases individual domain mobility (measured by SAXS and NMR), activating ATP hydrolysis. The N-terminal segment of MBD1-3 physically interacts with the nucleotide-binding domain of ATP7B, coupling copper binding to ATP hydrolysis. Small-angle X-ray scattering (SAXS); solution NMR; ATPase activity assays; apo-Atox1 and Cu-Atox1 comparative studies The Journal of biological chemistry High 28900031
2017 Atox1 contains positively charged surface lysine residues that mediate association with negatively charged lipid membranes; loss of these residues lowers copper loading efficiency in vivo, suggesting the membrane bilayer acts as a scaffold facilitating copper loading of Atox1. Lipid binding assays; in vivo copper loading assays with Lys mutants; membrane association experiments The Journal of membrane biology Medium 24036897
2017 Atox1 can function as a transcription factor for SOD3: in TPA-differentiated THP-1 cells, Atox1 undergoes copper-dependent nuclear translocation, binds the SOD3 promoter (demonstrated by ChIP), and overexpression/knockdown of Atox1 enhances/suppresses TPA-induced SOD3 expression. Nuclear translocation assay; ChIP assay; Atox1 overexpression and knockdown; quantitative RT-PCR and Western blot for SOD3 Biometals Medium 29168020
2019 Atox1 interacts with α-synuclein in living cells (proximity ligation assay) and in vitro (NMR); the interaction interface in α-synuclein involves the N-terminal region up to Gln24, while in Atox1, residues around the copper-binding cysteines (positions 11–16) are primarily involved. Atox1 inhibits amyloid formation of both non-acetylated and N-terminally acetylated α-synuclein in vitro. Solution NMR spectroscopy with isotopically labeled proteins; in-cell proximity ligation assay; in vitro amyloid formation assays ACS chemical neuroscience High 31600047
2020 Atox1 is required for breast cancer cell migration velocity and directionality (tracked at single-cell level); silencing Atox1 also reduces copper transporter ATP7A expression effects and decreases LOX (lysyl oxidase) activity, placing Atox1 in the ATP7A–LOX axis for copper-mediated cancer cell migration. Video microscopy single-cell tracking (~hundreds of cells per condition); siRNA knockdown; in-cell proximity ligation assay for Atox1-ATP7A-LOX proximity; LOX activity assay Proceedings of the National Academy of Sciences of the United States of America High 31932435
2020 EPR and computational analysis reveals that Cu(I) binding in Atox1 involves Cys12 as the primary Cu(I)-binding residue while Cys15 is important for Atox1 dimerization; Lys60 electrostatically stabilizes the Cu(I)-Atox1 dimer. Atox1 interacts with Ctr1 as a dimer but transfers copper to ATP7A/B as a monomer. Continuous wave and pulsed EPR spectroscopy; QM/MM molecular dynamics simulations; site-directed spin labeling The journal of physical chemistry. B Medium 32396355
2020 EPR spectroscopy of Cu(I)-bound Atox1 with ATP7B metal-binding domains shows that Cu(I) is most likely transferred from Atox1 monomer to MBD1 and MBD4 of ATP7B; MBD1-3 and MBD4-6 act as two independent functional units, and other MBDs mediate intramolecular copper routing. CW and pulsed EPR spectroscopy in solution; spin-labeled protein constructs International journal of molecular sciences Medium 32748830
2021 APEX2-based proximity labeling of Atox1 identified CRIP2 as a nuclear copper-binding protein that interacts with Atox1; Atox1 transfers copper to CRIP2, inducing a conformational change that promotes CRIP2 ubiquitin-mediated proteasomal degradation. CRIP2 degradation (or depletion) elevates ROS and activates autophagy in cancer cells. APEX2 proximity labeling combined with mass spectrometry; co-immunoprecipitation; in vitro copper transfer; secondary structure analysis; siRNA knockdown; autophagy and ROS assays Angewandte Chemie High 34550632
2022 ATOX1 promotes copper-dependent transcription of MDC1 (a double-strand DNA damage repair protein): after genotoxic stress, ATOX1 translocates to the nucleus and binds the MDC1 promoter in a copper-dependent manner, enhancing DNA damage repair. Knockout or blockade of ATOX1 sensitizes tumors to gemcitabine in mouse models. ChIP assay; promoter reporter assay; ATOX1 knockout cell lines and mouse xenograft models; Western blot for MDC1; genotoxic drug sensitivity assays Cancer letters Medium 35315340
2022 Memo1 binds two Cu(I) ions per protein, shields them from ROS generation, and exchanges Cu(I) with the copper chaperone Atox1 in vitro; spatial proximity between Memo1 and Atox1 is confirmed in breast cancer cells by proximity ligation assay, suggesting Memo1 may shuttle Cu to Atox1 for delivery to the secretory pathway. Multiple biophysical methods (spectroscopy) for Cu binding; in vitro Cu exchange assay; proximity ligation assay in breast cancer cells Proceedings of the National Academy of Sciences of the United States of America Medium 36067318
2022 Crystal structure of Atox1 loaded with Zn2+ shows the Zn ion bridging the CXXC motifs of two Atox1 molecules in a homodimer with tetrahedral coordination; EDTA soaking causes only limited Zn removal, suggesting potential involvement of Atox1 in zinc metabolism in addition to copper. X-ray crystallography; anomalous diffraction near Zn K-edge for metal identity; EDTA soaking experiments Biomolecules Medium 36291703
2024 Atox1 binds DJ-1 in a copper-dependent manner (copper-binding motif mutation or free copper sequestration reduces the interaction); DJ-1 mediates Atox1's antioxidant capacity, as DJ-1 knockdown impairs Atox1-mediated protection against oxidative stress, and overexpression of DJ-1 fails to restore antioxidant function of copper-binding-deficient Atox1 mutants. Co-immunoprecipitation and mass spectrometry; site-directed Atox1 mutations; DJ-1 knockdown and overexpression; oxidative stress and mitochondrial function assays in HT-22 cells and mouse TBI model Redox biology Medium 38640584

Source papers

Stage 0 corpus · 100 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1997 Identification and functional expression of HAH1, a novel human gene involved in copper homeostasis. The Journal of biological chemistry 294 9083055
2008 Novel role of antioxidant-1 (Atox1) as a copper-dependent transcription factor involved in cell proliferation. The Journal of biological chemistry 260 18245776
1999 Interaction of the copper chaperone HAH1 with the Wilson disease protein is essential for copper homeostasis. Proceedings of the National Academy of Sciences of the United States of America 226 10557326
2011 Unification of the copper(I) binding affinities of the metallo-chaperones Atx1, Atox1, and related proteins: detection probes and affinity standards. The Journal of biological chemistry 208 21258123
2001 The metallochaperone Atox1 plays a critical role in perinatal copper homeostasis. Proceedings of the National Academy of Sciences of the United States of America 192 11391006
2003 Essential role for Atox1 in the copper-mediated intracellular trafficking of the Menkes ATPase. Proceedings of the National Academy of Sciences of the United States of America 165 12538877
2016 The Role of Copper Chaperone Atox1 in Coupling Redox Homeostasis to Intracellular Copper Distribution. Antioxidants (Basel, Switzerland) 136 27472369
1998 HAH1 is a copper-binding protein with distinct amino acid residues mediating copper homeostasis and antioxidant defense. The Journal of biological chemistry 133 9430722
2002 Metallochaperone Atox1 transfers copper to the NH2-terminal domain of the Wilson's disease protein and regulates its catalytic activity. The Journal of biological chemistry 131 12029094
2006 Structure of human Wilson protein domains 5 and 6 and their interplay with domain 4 and the copper chaperone HAH1 in copper uptake. Proceedings of the National Academy of Sciences of the United States of America 128 16571664
2020 Single-cell tracking demonstrates copper chaperone Atox1 to be required for breast cancer cell migration. Proceedings of the National Academy of Sciences of the United States of America 114 31932435
2004 Solution structure of the apo and copper(I)-loaded human metallochaperone HAH1. Biochemistry 96 15476398
2003 X-ray absorption spectroscopy of the copper chaperone HAH1 reveals a linear two-coordinate Cu(I) center capable of adduct formation with exogenous thiols and phosphines. The Journal of biological chemistry 96 12686548
2011 Probing the interaction of cisplatin with the human copper chaperone Atox1 by solution and in-cell NMR spectroscopy. Journal of the American Chemical Society 95 21981264
2004 The N-terminal metal-binding site 2 of the Wilson's Disease Protein plays a key role in the transfer of copper from Atox1. The Journal of biological chemistry 92 14754885
2011 Cisplatin binds human copper chaperone Atox1 and promotes unfolding in vitro. Proceedings of the National Academy of Sciences of the United States of America 82 21482801
2008 Metal binding domains 3 and 4 of the Wilson disease protein: solution structure and interaction with the copper(I) chaperone HAH1. Biochemistry 81 18558714
2009 An NMR study of the interaction of the N-terminal cytoplasmic tail of the Wilson disease protein with copper(I)-HAH1. The Journal of biological chemistry 80 19181666
2008 Effects of the loss of Atox1 on the cellular pharmacology of cisplatin. Journal of inorganic biochemistry 72 19124158
2013 An expanding range of functions for the copper chaperone/antioxidant protein Atox1. Antioxidants & redox signaling 71 23249252
2000 The copper transport protein Atox1 promotes neuronal survival. The Journal of biological chemistry 68 10617654
2021 APEX2-based Proximity Labeling of Atox1 Identifies CRIP2 as a Nuclear Copper-binding Protein that Regulates Autophagy Activation. Angewandte Chemie (International ed. in English) 66 34550632
2008 ATOX1: a novel copper-responsive transcription factor in mammals? The international journal of biochemistry & cell biology 64 18761103
2016 The C-Terminus of Human Copper Importer Ctr1 Acts as a Binding Site and Transfers Copper to Atox1. Biophysical journal 60 26745413
2014 Redox sulfur chemistry of the copper chaperone Atox1 is regulated by the enzyme glutaredoxin 1, the reduction potential of the glutathione couple GSSG/2GSH and the availability of Cu(I). Metallomics : integrated biometal science 59 24522867
2003 Kinetic analysis of the interaction of the copper chaperone Atox1 with the metal binding sites of the Menkes protein. The Journal of biological chemistry 57 12679332
2005 A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains. The Journal of biological chemistry 56 16172131
2022 Copper enhances genotoxic drug resistance via ATOX1 activated DNA damage repair. Cancer letters 55 35315340
2016 Copper chaperone Atox1 plays role in breast cancer cell migration. Biochemical and biophysical research communications 55 28027931
2016 Copper transporters and chaperones CTR1, CTR2, ATOX1, and CCS as determinants of cisplatin sensitivity. Metallomics : integrated biometal science 54 27157188
2019 Copper chaperone ATOX1 is required for MAPK signaling and growth in BRAF mutation-positive melanoma. Metallomics : integrated biometal science 52 31317143
2022 Memo1 binds reduced copper ions, interacts with copper chaperone Atox1, and protects against copper-mediated redox activity in vitro. Proceedings of the National Academy of Sciences of the United States of America 50 36067318
2013 Copper chaperone Atox1 interacts with the metal-binding domain of Wilson's disease protein in cisplatin detoxification. The Biochemical journal 49 23751120
2017 The metal chaperone Atox1 regulates the activity of the human copper transporter ATP7B by modulating domain dynamics. The Journal of biological chemistry 48 28900031
2014 Roles of Atox1 and p53 in the trafficking of copper-64 to tumor cell nuclei: implications for cancer therapy. Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry 45 24445997
2012 Molecular analysis of Wilson patients: direct sequencing and MLPA analysis in the ATP7B gene and Atox1 and COMMD1 gene analysis. Journal of trace elements in medicine and biology : organ of the Society for Minerals and Trace Elements (GMS) 45 22677543
2010 Copper-transfer mechanism from the human chaperone Atox1 to a metal-binding domain of Wilson disease protein. The journal of physical chemistry. B 45 20166696
2020 Nuclear translocation of Atox1 potentiates activin A-induced cell migration and colony formation in colon cancer. PloS one 44 31961892
2013 Determinants for simultaneous binding of copper and platinum to human chaperone Atox1: hitchhiking not hijacking. PloS one 42 23936210
2017 Thiol-based copper handling by the copper chaperone Atox1. IUBMB life 41 28294521
2008 Conserved residues modulate copper release in human copper chaperone Atox1. Proceedings of the National Academy of Sciences of the United States of America 41 18685091
2009 Lysine-60 in copper chaperone Atox1 plays an essential role in adduct formation with a target Wilson disease domain. Journal of the American Chemical Society 38 19863064
2015 Human cytoplasmic copper chaperones Atox1 and CCS exchange copper ions in vitro. Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine 35 25673218
2024 Atox1 protects hippocampal neurons after traumatic brain injury via DJ-1 mediated anti-oxidative stress and mitophagy. Redox biology 32 38640584
2009 Copper redistribution in Atox1-deficient mouse fibroblast cells. Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry 31 19865834
2007 Insights into Cu(I) exchange in HAH1 using quantum mechanical and molecular simulations. Biochemistry 30 17616150
2003 Functional properties of the human copper-transporting ATPase ATP7B (the Wilson's disease protein) and regulation by metallochaperone Atox1. Annals of the New York Academy of Sciences 30 12763797
2015 Identification of New Potential Interaction Partners for Human Cytoplasmic Copper Chaperone Atox1: Roles in Gene Regulation? International journal of molecular sciences 29 26213915
2015 Human Copper Chaperone Atox1 Translocates to the Nucleus but does not Bind DNA In Vitro. Protein and peptide letters 28 25962064
2012 Reaction of platinum anticancer drugs and drug derivatives with a copper transporting protein, Atox1. Biochemical pharmacology 28 22285228
2008 Structure and dynamics of Cu(I) binding in copper chaperones Atox1 and CopZ: a computer simulation study. The journal of physical chemistry. B 28 18361527
2024 Atox1 regulates macrophage polarization in intestinal inflammation via ROS-NLRP3 inflammasome pathway. Journal of translational medicine 25 38796413
2017 Copper chaperone antioxidant-1, Atox-1, is involved in the induction of SOD3 in THP-1 cells. Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine 25 29168020
2004 Copper-mediated homo-dimerisation for the HAH1 metallochaperone. Biochemical and biophysical research communications 24 15530404
2019 Interaction between Copper Chaperone Atox1 and Parkinson's Disease Protein α-Synuclein Includes Metal-Binding Sites and Occurs in Living Cells. ACS chemical neuroscience 23 31600047
2017 Binding of Copper and Cisplatin to Atox1 Is Mediated by Glutathione through the Formation of Metal-Sulfur Clusters. Biochemistry 21 28549213
2013 Atox1 contains positive residues that mediate membrane association and aid subsequent copper loading. The Journal of membrane biology 21 24036897
2003 Genomic organization of ATOX1, a human copper chaperone. BMC genetics 21 12594858
2018 Copper Chaperone Atox1 Interacts with Cell Cycle Proteins. Computational and structural biotechnology journal 20 30455854
2014 Interaction between the anticancer drug Cisplatin and the copper chaperone Atox1 in human melanoma cells. Protein and peptide letters 20 23988033
2005 Molecular dynamics study of the metallochaperone Hah1 in its apo and Cu(I)-loaded states: role of the conserved residue M10. FEBS letters 20 16194538
2020 Clioquinol inhibits dopamine-β-hydroxylase secretion and noradrenaline synthesis by affecting the redox status of ATOX1 and copper transport in human neuroblastoma SH-SY5Y cells. Archives of toxicology 19 33034664
2016 Oxaliplatin Binding to Human Copper Chaperone Atox1 and Protein Dimerization. Inorganic chemistry 19 27305454
2017 The structural flexibility of the human copper chaperone Atox1: Insights from combined pulsed EPR studies and computations. Protein science : a publication of the Protein Society 18 28543811
2013 Probing the coordination environment of the human copper chaperone HAH1: characterization of Hg(II)-bridged homodimeric species in solution. Chemistry (Weinheim an der Bergstrasse, Germany) 18 23677531
1999 The copper chaperone Atox1 in canine copper toxicosis in Bedlington terriers. Genomics 17 10585777
2025 Targeting copper homeostasis: Akkermansia-derived OMVs co-deliver Atox1 siRNA and elesclomol for cancer therapy. Acta pharmaceutica Sinica. B 16 40487636
2022 Transcriptional Responses of Copper-Transport-Related Genes ctr1, ctr2 and atox1 and Their Roles in the Regulation of Cu Homeostasis in Yellow Catfish Pelteobagrus fulvidraco. International journal of molecular sciences 16 36293101
2004 Comparative analysis of metal binding characteristics of copper chaperone proteins, Atx1 and ATOX1. Bioinorganic chemistry and applications 16 18365072
2020 Cu(I) Controls Conformational States in Human Atox1 Metallochaperone: An EPR and Multiscale Simulation Study. The journal of physical chemistry. B 15 32396355
2018 Tat-ATOX1 inhibits inflammatory responses via regulation of MAPK and NF-κB pathways. BMB reports 15 30545441
2012 Dynamics and stability of the metal binding domains of the Menkes ATPase and their interaction with metallochaperone HAH1. Biochemistry 15 23075277
2009 Differential roles of Met10, Thr11, and Lys60 in structural dynamics of human copper chaperone Atox1. Biochemistry 15 19146392
2013 Interaction of cisplatin and analogue Pt(en)Cl2 with the copper metallo-chaperone Atox1. Metallomics : integrated biometal science 14 23778981
2000 Structure, expression, and chromosomal localization of the mouse Atox1 gene. Genomics 14 10673341
2016 Tat-ATOX1 inhibits streptozotocin-induced cell death in pancreatic RINm5F cells and attenuates diabetes in a mouse model. International journal of molecular medicine 13 27222268
2000 Physical mapping of the human ATX1 homologue (HAH1) to the critical region of the 5q- syndrome within 5q32, and immediately adjacent to the SPARC gene. Human genetics 13 10982193
2016 ATOX1 gene silencing increases susceptibility to anticancer therapy based on copper ionophores or chelating drugs. Journal of inorganic biochemistry 12 26784148
2014 Copper binding modulates the platination of human copper chaperone Atox1 by antitumor trans-platinum complexes. Metallomics : integrated biometal science 12 24469739
2014 Structural biology of cisplatin complexes with cellular targets: the adduct with human copper chaperone atox1 in aqueous solution. Chemistry (Weinheim an der Bergstrasse, Germany) 12 25111319
2018 Neuroprotective effects of Tat-ATOX1 protein against MPP+-induced SH-SY5Y cell deaths and in MPTP-induced mouse model of Parkinson's disease. Biochimie 11 30352250
2002 Tissue localization of the copper chaperone ATOX1 and its potential role in disease. Mammalian genome : official journal of the International Mammalian Genome Society 11 12420134
2024 Dysfunction in atox-1 and ceruloplasmin alters labile Cu levels and consequently Cu homeostasis in C. elegans. Frontiers in molecular biosciences 10 38389896
2024 Cuproptosis-related gene ATOX1 promotes MAPK signaling and diffuse large B-cell lymphoma proliferation via modulating copper transport. Biomolecules & biomedicine 10 39036924
2022 Crystal Structure of the Human Copper Chaperone ATOX1 Bound to Zinc Ion. Biomolecules 9 36291703
2018 Tetrathiomolybdate inhibits the reaction of cisplatin with human copper chaperone Atox1. Metallomics : integrated biometal science 9 29721562
2017 Copper chaperone ATOX1 regulates pluripotency factor OCT4 in preimplantation mouse embryos. Biochemical and biophysical research communications 9 28711491
2024 Hippo-YAP signaling alleviates copper-induced mitochondrial dysfunction and oxidative damage via the ATOX1-PPA2 pathway. International journal of biological macromolecules 8 39706439
2020 An EPR Study on the Interaction between the Cu(I) Metal Binding Domains of ATP7B and the Atox1 Metallochaperone. International journal of molecular sciences 8 32748830
2019 Oxidation of Human Copper Chaperone Atox1 and Disulfide Bond Cleavage by Cisplatin and Glutathione. International journal of molecular sciences 8 31500118
2019 Generation of a genetically modified human embryonic stem cells expressing fluorescence tagged ATOX1. Stem cell research 8 31704540
2025 Complanatoside A disrupts copper homeostasis and induces cuproptosis via directly targeting ATOX1 in prostate cancer. Toxicology and applied pharmacology 7 39909165
2025 Balancing between cuproplasia and copper-dependent cell death: molecular basis and clinical implications of ATOX1 in cancer. Journal of experimental & clinical cancer research : CR 7 40721800
2024 Curcumin suppresses copper accumulation in non-small cell lung cancer by binding ATOX1. BMC pharmacology & toxicology 7 39169392
2023 The p53 protein is a suppressor of Atox1 copper chaperon in tumor cells under genotoxic effects. PloS one 7 38127999
2022 Copper coordination states affect the flexibility of copper Metallochaperone Atox1: Insights from molecular dynamics simulations. Protein science : a publication of the Protein Society 7 36208051
2021 Evaluation of ATOX1 as a Potential Predictive Biomarker for Tetrathiomolybdate Treatment of Breast Cancer Patients with High Risk of Recurrence. Biomedicines 7 34944703
2019 In-silico analysis of novel p.(Gly14Ser) variant of ATOX1 gene: plausible role in modulating ATOX1-ATP7B interaction. Molecular biology reports 7 30980273
2025 COMMD3 Regulates Copper Metabolism via the ATOX1-ATP7A-LOX Axis to Promote Multiple Myeloma Progression. Biomedicines 6 40002764
2017 Platinum transfer from hCTR1 to Atox1 is dependent on the type of platinum complex. Metallomics : integrated biometal science 5 28383086

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