Metallochaperone Atox1 Transfers Copper to the NH2-terminal Domain of the Wilson's Disease Protein and Regulates Its Catalytic Activity
Open Access
- 1 August 2002
- journal article
- Published by Elsevier BV in Journal of Biological Chemistry
- Vol. 277 (31), 27953-27959
- https://doi.org/10.1074/jbc.m203845200
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- The metallochaperone Atox1 plays a critical role in perinatal copper homeostasisProceedings of the National Academy of Sciences of the United States of America, 2001
- Metallochaperones, an Intracellular Shuttle Service for Metal IonsPublished by Elsevier BV ,2000
- Identification of the copper chaperone SAH in Ovis aries: expression analysis and in vitro interaction of SAH with ATP7BBiochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 2000
- Intracellular copper routing: the role of copper chaperonesTrends in Biochemical Sciences, 2000
- Interaction of the copper chaperone HAH1 with the Wilson disease protein is essential for copper homeostasisProceedings of the National Academy of Sciences of the United States of America, 1999
- Characterization of the Interaction between the Wilson and Menkes Disease Proteins and the Cytoplasmic Copper Chaperone, HAH1pJournal of Biological Chemistry, 1999
- Undetectable Intracellular Free Copper: The Requirement of a Copper Chaperone for Superoxide DismutaseScience, 1999
- Intracellular Pathways of Copper Trafficking in Yeast and HumansAdvances in experimental medicine and biology, 1999
- Metal Ion Chaperone Function of the Soluble Cu(I) Receptor Atx1Science, 1997
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976