ATOX1 Antibody

1. Copper chaperone Atox-1 is involved in the induction of SOD3 in a monocyte cell line. PMID: 29168020
2. Since full occupancy of the tetrahedral cavity is a common feature of all Atox1 dimeric structures obtained with other metal ions (Cu(+), Cd(2+), and Hg(2+)), we propose that in the case of platinum, where the occupancy is only 0.4, the remaining cavities are occupied by Cu(+) ions PMID: 27305454
3. Data suggest that N-terminal segment of metal-binding domains (MBDs) 1-3 of ATOX1 interact with nucleotide-binding domain of ATP7B, thus physically coupling the domains involved in copper binding and those involved in ATP hydrolysis; interactions with MBDs 1-3 of ATOX1 activate ATP7B ATP hydrolysis. (ATOX1 = copper transport protein ATOX1; ATP7B = Cu-binding P type ATPase ATP7B) PMID: 28900031
4. It show that copper(I) and glutathione form large polymers with a molecular mass of approximately 8 kDa, which can transfer copper to Atox1. PMID: 28549213
5. Highlighted in this review are unique redox properties of Atox1 and other copper chaperones. Also, summarized are the redox nodes in the cytosol which potentially play dominant roles in the redox regulation of copper chaperones PMID: 28294521
6. The structural flexibility of the human copper chaperone Atox1 has been reported based on insights from combined pulsed EPR studies and computations. PMID: 28543811
7. Cu chaperone Atox1 has a role in breast cancer cell migration PMID: 28027931
8. Multiple genetic models identified genetic associations with systolic blood pressure and ATOX1. PMID: 26866891
9. In addition to Atox1, the human cytoplasm also contains Cu chaperones for loading of superoxide dismutase 1 (i.e. CCS) and cytochrome c oxidase in mitochondria (i.e. Cox17). [review] PMID: 26745464
10. results suggest the possibility of a therapy with copper-chelating or ionophore drugs in subtypes of tumors showing specific alterations in ATOX1 expression PMID: 26784148
11. C-Terminus of Human Copper Importer Ctr1 Acts as a Binding Site and Transfers Copper to Atox1 PMID: 26745413
12. Cu chaperone function of Atox1 mediated through Cu transporter ATP7A is required for VEGF-induced angiogenesis via activation of Cu enzyme lysyl oxidase. PMID: 26437801
13. Upon neuronal differentiation, transitions in redox states upregulates expression of ATOX1 and its partner ATP7A, producing higher flux of copper through the secretory pathway. PMID: 26879543
14. To identify new interactions partners of Atox1, a yeast two-hybrid screen with a large human placenta library of cDNA fragments using Atox1 as bait, was performed. PMID: 26213915
15. Studied the localization of Atox1 in HeLa cells using fluorescence imaging in combination with in vitro binding experiments to fluorescently labeled DNA duplexes harboring the proposed promotor sequence. PMID: 25962064
16. Human cytoplasmic copper chaperones Atox1 and CCS exchange copper ions in vitro PMID: 25673218
17. Cisplatin is one of the most used anticancer drugs. Its cellular influx and delivery to target DNA may involve the copper chaperone Atox1 protein. PMID: 25111319
18. The data collected here shows that the Atox1 keeps its dimer nature also in the presence of the CTR1 c-terminal domain; however, two geometrical states are assumed by the Atox1. PMID: 24837030
19. The Cu-binding motif in Atox1, as well as in target Cu-binding domains of ATP7A/B, consists of a MX1CXXC motif where X1 = T. PMID: 24824562
20. Human Grx1 can catalyse reduction of Atox1 by glutathione but only in the presence of Cu(I). PMID: 24522867
21. These results indicate that the roles of Atox1 in the regulation of cellular trafficking of platinum drugs are dependent on the coordination configurations. PMID: 24469739
22. Atox1 has a role in copper transport to tumor cell nuclei. PMID: 24445997
23. CTR1 silencing increased the protein levels of copper chaperone ATOX1 and copper chaperone for superoxide dismutase 1 (CCS-1), but decreased copper chaperone for cytochrome c oxidase (COX17). PMID: 24343031
24. Atox1 contains positive residues that mediate membrane association and aid subsequent copper loading. PMID: 24036897
25. the primary coordination site of Atox1 for interaction wtih cisplatin is at the cysteine residues in the Cu(I)-binding sequence Cys(12)GlyGlyCys(15) PMID: 23778981
26. Based on structural analysis, this work determines that the protein possesses two distinct conformations referred to as "in" and "out" due to the relative positioning of Cys12 (one of Cu(I) binding residues). PMID: 23553875
27. Knockdown of ATOX1 in non-small cell lung cancer cells was associated with reduction in copper-stimulated cell proliferation. These findings suggest that ATOX1 plays an important role in copper-stimulated proliferation of non-small cell lung cancer cells. PMID: 23624903
28. Binding of free cisplatin and reaction with the cisplatin-loaded Atox1 produce the same protein-bound platinum intermediate in the transfer of metal-binding domain (repeat) (MBD)2 from Atox1. PMID: 23751120
29. different effects of ATX1 unfolding on Cu(I) affinity PMID: 23169585
30. GSSG oxidizes copper-coordinating cysteines of Atox1 with formation of an intramolecular disulfide. GSH alone is sufficient to reduce the disulfide, restoring the ability of Atox1 to bind copper; glutaredoxin 1 facilitates this reaction when GSH is low PMID: 22648419
31. No major role can be attributed to Atox1 and COMMD in the pathophysiology or clinical variation of Wilson disease. PMID: 22677543
32. thermodynamic parameters of copper (Cu) transfer from the human copper chaperone Atox1 to the fourth metal-binding domain of the Wilson disease protein PMID: 22574136
33. By binding to Atox1 in the cytoplasm, cisPt transport to DNA may be blocked. In agreement with this model, cell line studies demonstrate a correlation between Atox1 expression levels, and cisplatin resistance. PMID: 21482801
34. Unification of the copper(I) binding affinities of the metallo-chaperones Atx1, Atox1, and related proteins: detection probes and affinity standards. PMID: 21258123
35. transfers copper to the NH2-terminal domain of the Wilson's disease protein and regulates its catalytic activity PMID: 12029094
36. Gene structure of ATOX1. PMID: 12594858
37. A copper-dependent interaction of Atox1 with the metal binding sites of menkes protein was observed PMID: 12679332
38. X-ray absorption spectroscopy of this copper chaperone reveals a copper center capable of formation with exogenous thiols and phosphines PMID: 12686548
39. Regulates the function of ATP7B in Wilson's disease PMID: 12763797
40. handling of copper by Atox1 and copper transfer between Atox1 and WND are under kinetic rather than thermodynamic control PMID: 14709553
41. Detailed structural and dynamic characterization of the behavior of human HAH1 in solution, in the physiologically relevant reduced apo and copper(I)-bound forms PMID: 15476398
42. interaction between the human copper(I) chaperone, HAH1, and one of its two physiological partners, the Menkes disease protein (ATP7A), was investigated in solution using heteronuclear NMR PMID: 15670166
43. Atox1 functions not only as a copper chaperone for SOD3 but also as a positive regulator for SOD3 transcription and may have an important role in modulating oxidative stress in the cardiovascular system. PMID: 15761197
44. a three-domain construct of ATP7A interacts with copper(I) and copper(I)-HAH1 PMID: 16172131
45. Wilson disease protein is an acceptor of oopper from HAH1 protein. PMID: 16571664
46. localization of ATP7A between the trans-Golgi network and the plasma membrane may be regulated by the accumulation of the adducts with HAH1, whereas the main role of domains 5 and 6 is to assist copper(I) translocation PMID: 17545667
47. The results from the quantum mechanical (QM) and MD simulations suggest that either a two- or three-coordinate exchange reaction is preferred and that it is unlikely that a four-coordinate Cu(I) species plays a role in copper exchange. PMID: 17616150
48. Divergent energetic properties of Atox1 apo- and holo-forms may be linked to conformational changes that facilitate copper transfer to the target. PMID: 17881304
49. Atox1 functions as a novel transcription factor that, when activated by copper, undergoes nuclear translocation, DNA binding, and transactivation, thereby contributing to cell proliferation. PMID: 18245776
50. No major role can be attributed to Atox1 in the pathophysiology or clinical variation of Wilson disease. PMID: 18416466

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HGNC: 798

OMIM: 602270

KEGG: hsa:475

STRING: 9606.ENSP00000316854

UniGene: Hs.125213