ATX1/YNL259C Literature Guide Help

Other names published for ATX1: YNL259C

ATX1 - Substrates/Ligands/Cofactors (20)

ReferenceOther Genes Addressed
Wegner SV, et al.  (2011) The tightly regulated copper window in yeast. Chem Commun (Camb) 47(9):2571-3
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
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
Banci L, et al.  (2006) The Atx1-Ccc2 complex is a metal-mediated protein-protein interaction. Nat Chem Biol 2(7):367-8
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
Narindrasorasak S, et al.  (2004) Comparative Analysis of Metal Binding Characteristics of Copper Chaperone Proteins, Atx1 and ATOX1. Bioinorg Chem Appl :105-23
Seneque O, et al.  (2004) Novel model peptide for Atx1-like metallochaperones. Chem Commun (Camb) (7):770-1
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
Field LS, et al.  (2002) Copper chaperones: personal escorts for metal ions. J Bioenerg Biomembr 34(5):373-9
Xiao Z and Wedd AG  (2002) A C-terminal domain of the membrane copper pump Ctr1 exchanges copper(I) with the copper chaperone Atx1. Chem Commun (Camb) (6):588-9
Arnesano F, et al.  (2001) Characterization of the binding interface between the copper chaperone Atx1 and the first cytosolic domain of Ccc2 ATPase. J Biol Chem 276(44):41365-76
Arnesano F, et al.  (2001) Solution structure of the Cu(I) and apo forms of the yeast metallochaperone, Atx1. Biochemistry 40(6):1528-39
Banci L, et al.  (2001) Solution structure of the yeast copper transporter domain Ccc2a in the apo and Cu(I)-loaded states. J Biol Chem 276(11):8415-26
Portnoy ME, et al.  (2001) Metal transporters that contribute copper to metallochaperones in Saccharomyces cerevisiae. Mol Genet Genomics 265(5):873-82
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
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