ATX1/YNL259C Literature Guide Help

Other names published for ATX1: YNL259C

ATX1 - Protein/Nucleic Acid Structure (11)

ReferenceOther Genes Addressed
Sgrignani J and Pierattelli R  (2012) Nuclear magnetic resonance signal chemical shifts and molecular simulations: a multidisciplinary approach to modeling copper protein structures. J Biol Inorg Chem 17(1):71-9
Bertini I, et al.  (2011) 13C direct-detection biomolecular NMR spectroscopy in living cells. Angew Chem Int Ed Engl 50(10):2339-41
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
Arnesano F, et al.  (2004) A docking approach to the study of copper trafficking proteins; interaction between metallochaperones and soluble domains of copper ATPases. Structure 12(4):669-76
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
Arnesano F, et al.  (2002) Metallochaperones and metal-transporting ATPases: a comparative analysis of sequences and structures. Genome Res 12(2):255-71
Arnesano F, et al.  (2001) Solution structure of the Cu(I) and apo forms of the yeast metallochaperone, Atx1. Biochemistry 40(6):1528-39
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