Other names published for ATX1: YNL259C
ATX1 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Protein Physical Properties
- Protein Sequence Features
- Protein-protein Interactions
- Protein/Nucleic Acid Structure
- Substrates/Ligands/Cofactors
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Other Topics
- Additional Information
ATX1 - Protein Sequence Features (14)
| Reference | Other Genes Addressed |
|---|---|
| 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 | |
| Seneque O, et al. (2004) Novel model peptide for Atx1-like metallochaperones. Chem Commun (Camb) (7):770-1 | |
| 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 | |
| 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 | |
| Banci L, et al. (2002) A new zinc-protein coordination site in intracellular metal trafficking: solution structure of the Apo and Zn(II) forms of ZntA(46-118). J Mol Biol 323(5):883-97 | |
| 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 | |
| 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 | |
| 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 and Culotta VC (1995) The ATX1 gene of Saccharomyces cerevisiae encodes a small metal homeostasis factor that protects cells against reactive oxygen toxicity. Proc Natl Acad Sci U S A 92(9):3784-8 |



