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ATX1 antioxidant protein 1 homolog

Atx1, Atox1, HAH1
This gene encodes a copper chaperone that plays a role in copper homeostasis by binding and transporting cytosolic copper to ATPase proteins in the trans-Golgi network for later incorporation to the ceruloplasmin. This protein also functions as an antioxidant against superoxide and hydrogen peroxide, and therefore, may play a significant role in cancer carcinogenesis. Because of its cytogenetic location, this gene represents a candidate gene for 5q-syndrome. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ATP7B, CAN, ATPase, V1a, Histone
Papers on Atx1
Sequential protein expression and selective labeling for in-cell NMR in human cells.
Bruni et al., Sesto Fiorentino, Italy. In Biochim Biophys Acta, Mar 2016
METHODS: We established a human cell line stably overexpressing the copper binding protein HAH1.
ATOX1 gene silencing increases susceptibility to anticancer therapy based on copper ionophores or chelating drugs.
Condorelli et al., Catania, Italy. In J Inorg Biochem, Feb 2016
ATOX1 (antioxidant protein 1) is a copper chaperone that plays a role in copper homeostasis by binding and transporting cytosolic copper to ATPase proteins in the trans-Golgi network.
Extended functional repertoire for human copper chaperones.
Wittung-Stafshede et al., In Biomol Concepts, Feb 2016
The human cytoplasmic Cu chaperone Atox1 delivers Cu to P1B-type ATPases in the Golgi network, for incorporation into Cu-dependent enzymes following the secretory path.
The C-Terminus of Human Copper Importer Ctr1 Acts as a Binding Site and Transfers Copper to Atox1.
Wittung-Stafshede et al., Umeå, Sweden. In Biophys J, Feb 2016
We here employ biophysical experiments under anaerobic conditions in peptide models of the Ctr1 C-terminus to deduce Cu-binding residues, Cu affinity, and the ability to release Cu to the cytoplasmic Cu chaperone Atox1.
XAS Investigation of Silver(I) Coordination in Copper(I) Biological Binding Sites.
Michaud-Soret et al., Grenoble, France. In Inorg Chem, Jan 2016
By making use of X-ray absorption spectroscopy (XAS), we characterized the Ag(I) binding sites in proteins related to copper homeostasis, such as the chaperone Atox1 and metallothioneins (MTs), as well as in bioinspired thiolate Cu(I) chelators mimicking these proteins, in solution and at physiological pH.
Inhibition of human copper trafficking by a small molecule significantly attenuates cancer cell proliferation.
He et al., Chicago, United States. In Nat Chem, Dec 2015
Here we report small molecules that inhibit the human copper-trafficking proteins Atox1 and CCS, and so provide a selective approach to disrupt cellular copper transport.
Computational metallomics of the anticancer drug cisplatin.
Carloni et al., Jülich, Germany. In J Inorg Biochem, Dec 2015
These include the copper homeostasis proteins Ctr1, Atox1, and ATP7A.
Interactions of the organogold(III) compound Aubipyc with the copper chaperone Atox1: a joint mass spectrometry and circular dichroism investigation.
Massai et al., Sesto Fiorentino, Italy. In Biometals, Dec 2015
ESI and MALDI MS methods are exploited here to characterize the interactions occurring between the experimental anticancer organogold(III) drug, Aubipyc, and the copper chaperone Atox1, a key protein of the copper trafficking system.
Unresolved questions in human copper pump mechanisms.
Wittung-Stafshede, Umeå, Sweden. In Q Rev Biophys, Nov 2015
ATP7A/B receives Cu from the cytoplasmic Cu chaperone Atox1 that acts as the cytoplasmic shuttle between the cell membrane Cu importer, Ctr1 and ATP7A/B.
Genome-wide gene expression profiling to investigate molecular phenotypes of Arabidopsis mutants deprived in distinct histone methyltransferases and demethylases.
Shen et al., Strasbourg, France. In Genom Data, Jun 2015
Here we describe in details the contents and quality controls for the gene expression data of Arabidopsis mutants deprived in distinct histone methyltransferases (SDG26, SDG25, ATX1, CLF) and histone demethylases (LDL1, LDL2), in association with the study recently published by Berr and colleagues in The Plant Journal (Berr et al., 2015).
Copper Transport Protein Antioxidant-1 Promotes Inflammatory Neovascularization via Chaperone and Transcription Factor Function.
Fukai et al., Tokyo, Japan. In Sci Rep, 2014
Here we uncover a novel role of Cu transport protein Antioxidant-1 (Atox1), which is originally appreciated as a Cu chaperone and recently discovered as a Cu-dependent transcription factor, in inflammatory neovascularization.
Identification of New Potential Interaction Partners for Human Cytoplasmic Copper Chaperone Atox1: Roles in Gene Regulation?
Wittung-Stafshede et al., Uppsala, Sweden. In Int J Mol Sci, 2014
The human copper (Cu) chaperone Atox1 delivers Cu to P1B type ATPases in the Golgi network, for incorporation into essential Cu-dependent enzymes.
ATX1/AtCOMPASS and the H3K4me3 marks: how do they activate Arabidopsis genes?
Avramova et al., Lincoln, United States. In Curr Opin Plant Biol, 2014
We address these questions as well as the roles of the ARABIDOPSIS HOMOLOG OF TRITHORAX1 (ATX1), of the COMPASS-related (AtCOMPASS) protein complex, and of their product, H3K4me3, at ATX1-dependent genes.
Copper and copper proteins in Parkinson's disease.
Rios et al., Chiconcuac, Mexico. In Oxid Med Cell Longev, 2013
Some of the proteins involved in copper transport are the transporters CTR1, ATP7A, and ATP7B and the chaperone ATOX1.
An expanding range of functions for the copper chaperone/antioxidant protein Atox1.
Lutsenko et al., Baltimore, United States. In Antioxid Redox Signal, 2013
SIGNIFICANCE: Antioxidant protein 1 (Atox1 in human cells) is a copper chaperone for the copper export pathway with an essential role in cellular copper distribution.
Functional partnership of the copper export machinery and glutathione balance in human cells.
Lutsenko et al., Baltimore, United States. In J Biol Chem, 2012
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
Molecular analysis of Wilson patients: direct sequencing and MLPA analysis in the ATP7B gene and Atox1 and COMMD1 gene analysis.
Wilson et al., Bron, France. In J Trace Elem Med Biol, 2012
No major role can be attributed to Atox1 and COMMD in the pathophysiology or clinical variation of Wilson disease.
Mechanism of copper transport at the blood-cerebrospinal fluid barrier: influence of iron deficiency in an in vitro model.
Zheng et al., West Lafayette, United States. In Exp Biol Med (maywood), 2012
these results suggest that Ctr1, DMT1, ATOX1 and ATP7A contribute to Cu transport at the blood-CSF barrier
In vitro thermodynamic dissection of human copper transfer from chaperone to target protein.
Wittung-Stafshede et al., Umeå, Sweden. In Plos One, 2011
thermodynamic parameters of copper (Cu) transfer from the human copper chaperone Atox1 to the fourth metal-binding domain of the Wilson disease protein
Cisplatin binds human copper chaperone Atox1 and promotes unfolding in vitro.
Wittung-Stafshede et al., Umeå, Sweden. In Proc Natl Acad Sci U S A, 2011
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.
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