ATX1/YNL259C Literature Guide Help

Other names published for ATX1: YNL259C

ATX1 - Primary Literature (32)

ReferenceOther Genes Addressed
Allen S, et al.  (2013) The influence of protein folding on the copper affinities of trafficking and target sites. Dalton Trans 42(9):3233-9
Sukhai MA, et al.  (2013) Lysosomal disruption preferentially targets acute myeloid leukemia cells and progenitors. J Clin Invest 123(1):315-28
Heo DH, et al.  (2012) Cd2+ binds to Atx1 and affects the physical interaction between Atx1 and Ccc2 in Saccharomyces cerevisiae. Biotechnol Lett 34(2):303-7
Bertini I, et al.  (2011) 13C direct-detection biomolecular NMR spectroscopy in living cells. Angew Chem Int Ed Engl 50(10):2339-41
Minear S, et al.  (2011) Curcumin inhibits growth of Saccharomyces cerevisiae through iron chelation. Eukaryot Cell 10(11):1574-81
Morin I, et al.  (2009) Dissecting the role of the N-terminal metal-binding domains in activating the yeast copper ATPase in vivo. FEBS J 276(16):4483-95
Miras R, et al.  (2008) Interplay between glutathione, Atx1 and copper. 1. Copper(I) glutathionate induced dimerization of Atx1. J Biol Inorg Chem 13(2):195-205
Xiao Z, et al.  (2008) Transfer of copper between bis(thiosemicarbazone) ligands and intracellular copper-binding proteins. insights into mechanisms of copper uptake and hypoxia selectivity. Inorg Chem 47(10):4338-47
Banci L, et al.  (2007) Interaction of the two soluble metal-binding domains of yeast Ccc2 with copper(I)-Atx1. Biochem Biophys Res Commun 364(3):645-9
Dalosto SD  (2007) Computer simulation of the interaction of Cu(I) with cys residues at the binding site of the yeast metallochaperone Cu(I)-Atx1. J Phys Chem B 111(11):2932-40
Bertini I, et al.  (2006) Mapping protein-protein interaction by (13)C'-detected heteronuclear NMR spectroscopy. J Biomol NMR 36(2):111-22
Rousselot-Pailley P, et al.  (2006) Model peptides based on the binding loop of the copper metallochaperone Atx1: selectivity of the consensus sequence MxCxxC for metal ions Hg(II), Cu(I), Cd(II), Pb(II), and Zn(II). Inorg Chem 45(14):5510-20
Anastassopoulou I, et al.  (2004) Solution structure of the apo and copper(I)-loaded human metallochaperone HAH1. Biochemistry 43(41):13046-53
Serrano R, et al.  (2004) Copper and iron are the limiting factors for growth of the yeast Saccharomyces cerevisiae in an alkaline environment. J Biol Chem 279(19):19698-704
Serre L, et al.  (2004) Crystal structure of the oxidized form of the periplasmic mercury-binding protein MerP from Ralstonia metallidurans CH34. J Mol Biol 339(1):161-71
Xiao Z, et al.  (2004) C-terminal domain of the membrane copper transporter Ctr1 from Saccharomyces cerevisiae binds four Cu(I) ions as a cuprous-thiolate polynuclear cluster: sub-femtomolar Cu(I) affinity of three proteins involved in copper trafficking. J Am Chem Soc 126(10):3081-90
van Dongen EM, et al.  (2004) Copper-dependent protein-protein interactions studied by yeast two-hybrid analysis. Biochem Biophys Res Commun 323(3):789-95
Arnesano F, et al.  (2002) Metallochaperones and metal-transporting ATPases: a comparative analysis of sequences and structures. Genome Res 12(2):255-71
Uldschmid A, et al.  (2002) Identification and functional expression of tahA, a filamentous fungal gene involved in copper trafficking to the secretory pathway in Trametes versicolor. Microbiology 148(Pt 12):4049-58
Arnesano F, et al.  (2001) Solution structure of the Cu(I) and apo forms of the yeast metallochaperone, Atx1. Biochemistry 40(6):1528-39
Huffman DL and O'Halloran TV  (2000) Energetics of copper trafficking between the Atx1 metallochaperone and the intracellular copper transporter, Ccc2. J Biol Chem 275(25):18611-4
Kelner GS, et al.  (2000) The copper transport protein Atox1 promotes neuronal survival. J Biol Chem 275(1):580-4
Culotta VC, et al.  (1999) Intracellular pathways of copper trafficking in yeast and humans. Adv Exp Med Biol 448:247-54
Portnoy ME, et al.  (1999) Structure-function analyses of the ATX1 metallochaperone. J Biol Chem 274(21):15041-5
Rosenzweig AC, et al.  (1999) Crystal structure of the Atx1 metallochaperone protein at 1.02 A resolution. Structure 7(6):605-17
Schmidt PJ, et al.  (1999) Multiple protein domains contribute to the action of the copper chaperone for superoxide dismutase. J Biol Chem 274(34):23719-25
Himelblau E, et al.  (1998) Identification of a functional homolog of the yeast copper homeostasis gene ATX1 from Arabidopsis. Plant Physiol 117(4):1227-34
Wakabayashi T, et al.  (1998) Identification of the copper chaperone, CUC-1, in Caenorhabditis elegans: tissue specific co-expression with the copper transporting ATPase, CUA-1. FEBS Lett 440(1-2):141-6
Klomp LW, et al.  (1997) Identification and functional expression of HAH1, a novel human gene involved in copper homeostasis. J Biol Chem 272(14):9221-6
Lin SJ, et al.  (1997) A role for the Saccharomyces cerevisiae ATX1 gene in copper trafficking and iron transport. J Biol Chem 272(14):9215-20