Associated Papers
Co-evolution of alpha-helical transmembrane protein residues: large-scale variant profiling and complete mutational landscape of 2277 known PDB entries representing 504 unique human protein sequences.
Karagöl T et al.
Journal of Molecular Evolution, 2025
Functional Screen of Wilson Disease ATP7B Variants Reveals Residual Transport Activities.
Calvo JS et al.
Human Mutation, 2025
Analysis of Wilson disease mutations revealed that interactions between different ATP7B mutants modify their properties.
Roy S et al.
Scientific Reports, 2020
ATP7A and ATP7B copper transporters have distinct functions in the regulation of neuronal dopamine-β-hydroxylase.
Schmidt K et al.
The Journal of Biological Chemistry, 2018
Human copper transporter ATP7B (Wilson disease protein) forms stable dimers in vitro and in cells.
Jayakanthan S et al.
The Journal of Biological Chemistry, 2017
The metal chaperone Atox1 regulates the activity of the human copper transporter ATP7B by modulating domain dynamics.
Yu CH et al.
The Journal of Biological Chemistry, 2017
Probing functional roles of Wilson disease protein (ATP7B) copper-binding domains in yeast.
Ponnandai Shanmugavel K et al.
Metallomics : Integrated Biometal Science, 2017
In silico investigation of the ATP7B gene: insights from functional prediction of non-synonymous substitution to protein structure.
Squitti R et al.
Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine, 2014
Golgi in copper homeostasis: a view from the membrane trafficking field.
Polishchuk R et al.
Histochemistry and Cell Biology, 2013
Molecular events initiating exit of a copper-transporting ATPase ATP7B from the trans-Golgi network.
Hasan NM et al.
The Journal of Biological Chemistry, 2012
Diverse functional properties of Wilson disease ATP7B variants.
Huster D et al.
Gastroenterology, 2012
Reduced expression of ATP7B affected by Wilson disease-causing mutations is rescued by pharmacological folding chaperones 4-phenylbutyrate and curcumin.
van den Berghe PV et al.
Hepatology (baltimore, Md.), 2009
The distinct roles of the N-terminal copper-binding sites in regulation of catalytic activity of the Wilson's disease protein.
Huster D et al.
The Journal of Biological Chemistry, 2003
The role of the invariant His-1069 in folding and function of the Wilson's disease protein, the human copper-transporting ATPase ATP7B.
Tsivkovskii R et al.
The Journal of Biological Chemistry, 2003
Human copper-transporting ATPase ATP7B (the Wilson's disease protein): biochemical properties and regulation.
Lutsenko S et al.
Journal of Bioenergetics and Biomembranes, 2002
Metallochaperone Atox1 transfers copper to the NH2-terminal domain of the Wilson's disease protein and regulates its catalytic activity.
Walker JM et al.
The Journal of Biological Chemistry, 2002
Functional properties of the copper-transporting ATPase ATP7B (the Wilson's disease protein) expressed in insect cells.
Tsivkovskii R et al.
The Journal of Biological Chemistry, 2002
Functional characterization of missense mutations in ATP7B: Wilson disease mutation or normal variant?
Forbes JR et al.
American Journal of Human Genetics, 1998
Analysis of functional domains of Wilson disease protein (ATP7B) in Saccharomyces cerevisiae.
Iida M et al.
Febs Letters, 1998