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Issue 37, 2010
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A numerical investigation into possible mechanisms by that the A629P mutant of ATP7A causes Menkes Disease

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Abstract

We study in silico possible mechanisms by that the A629P mutant of ATP7A causes Menkes Disease. Our results indicate that the mutation does not have appreciable affects on the stability of copper-bound states but rather destabilizes the characteristic end-to-end β-sheet. In this way, the mutation presumably increases the probability for aggregation and/or degradation leading to decreased concentration of the monomer.

Graphical abstract: A numerical investigation into possible mechanisms by that the A629P mutant of ATP7A causes Menkes Disease

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Publication details

The article was received on 23 Feb 2010, accepted on 14 Jun 2010 and first published on 16 Aug 2010


Article type: Paper
DOI: 10.1039/C003568H
Citation: Phys. Chem. Chem. Phys., 2010,12, 11390-11397
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    A numerical investigation into possible mechanisms by that the A629P mutant of ATP7A causes Menkes Disease

    M. Kouza, S. Gowtham, M. Seel and U. H. E. Hansmann, Phys. Chem. Chem. Phys., 2010, 12, 11390
    DOI: 10.1039/C003568H

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