Ashima Bhattacharjee
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Previous Organizations / Institutes
The organizations / institutes from the scholar's other articles in the past ten years
Research Subjects
Ashima Bhattacharjee has a total of 5 co-authors. Here are the top co-authors by number of shared publications:
Martina Ralle
Oregon Health and Science University, Portland, USA
1 shared publication- Maya Schushan
Department of Biochemistry and Molecular Biology, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Ramat Aviv 69978, Israel
1 shared publication - Nir Ben-Tal
School of Neurobiology, Biochemistry and Biophysics, George S. Wise Faculty of Life Sciences, Tel Aviv University, Ramat Aviv, Israel
1 shared publication Svetlana Lutsenko
Johns Hopkins School of Medicine, Baltimore, Maryland, USA
1 shared publication- Svetlana Lutsenko
Department of Physiology, Pharmacology and Therapeutics The Johns Hopkins University School of Medicine Baltimore Maryland USA
1 shared publication
Latest Publications
- Open Access
- 1 January 2014
- Published by Springer Nature in Molecular Cytogenetics
- Vol. 7 (Suppl 1) , P54
Live-cell imaging of compartment-specific redox changes in menkes disease fibroblasts
- 1 January 2014
- Published by Springer Nature in Molecular Cytogenetics
- Vol. 7 (Suppl 1) , P54
Open AccessLive-cell imaging of compartment-specific redox changes in menkes disease fibroblasts
- 13 June 2012
- Published by Oxford University Press (OUP) in Metallomics
- Vol. 4 (7) , 669-678
A structural model of the copper ATPase ATP7B to facilitate analysis of Wilson disease-causing mutations and studies of the transport mechanism
The copper-transporting ATPase ATP7B has an essential role in human physiology, particularly for the liver and brain function. Inactivation of ATP7B is associated with a severe hepato-neurologic disorder, Wilson disease (WD). Hundreds of WD related mutations have been identified in ATP7B to date. The low frequency and the compound-heterozygous nature of causative mutations complicate the analysis of individual mutants and the establishment of genotype–phenotype correlations. To facilitate studies of disease-causing mutations and mechanistic understanding of WD, we have homology-modelled the ATP7B core (residues 643–1377) using the recent structure of the bacterial copper-ATPase LCopA as a template. The model, supported by evolutionary conservation and hydrophobicity analysis, as well as existing and new mutagenesis data, allows molecular interpretations of experimentally characterized clinical mutations. We also illustrate that structure and conservation can be used to grade potential deleterious effects for many WD mutations, which were clinically detected but have not yet been experimentally characterized. Finally, we compare the structural features of ATP7B and LCopA and discuss specific features of the eukaryotic copper pump.
- 13 June 2012
- Published by Oxford University Press (OUP) in Metallomics
- Vol. 4 (7) , 669-678
A structural model of the copper ATPase ATP7B to facilitate analysis of Wilson disease-causing mutations and studies of the transport mechanism
The copper-transporting ATPase ATP7B has an essential role in human physiology, particularly for the liver and brain function. Inactivation of ATP7B is associated with a severe hepato-neurologic disorder, Wilson disease (WD). Hundreds of WD related mutations have been identified in ATP7B to date. The low frequency and the compound-heterozygous nature of causative mutations complicate the analysis of individual mutants and the establishment of genotype–phenotype correlations. To facilitate studies of disease-causing mutations and mechanistic understanding of WD, we have homology-modelled the ATP7B core (residues 643–1377) using the recent structure of the bacterial copper-ATPase LCopA as a template. The model, supported by evolutionary conservation and hydrophobicity analysis, as well as existing and new mutagenesis data, allows molecular interpretations of experimentally characterized clinical mutations. We also illustrate that structure and conservation can be used to grade potential deleterious effects for many WD mutations, which were clinically detected but have not yet been experimentally characterized. Finally, we compare the structural features of ATP7B and LCopA and discuss specific features of the eukaryotic copper pump.