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Amyotrophic lateral sclerosis-associated copper/zinc superoxide dismutase mutations preferentially reduce the repulsive charge of the proteins
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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2007 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 282, no 29, 21230-21236 p.Article in journal (Refereed) Published
Abstract [en]

We provide bioinformatical evidence that protein charge plays a key role in the disease mechanism of amyotrophic lateral sclerosis (ALS). Analysis of 100 ALS-associated mutations in copper/zinc superoxide dismutase (SOD1) shows that these are site-selective with a preference to decrease the proteins' net repulsive charge. For each SOD1 monomer this charge is normally -6. Because biomolecules as a rule maintain net negative charge to assure solubility in the cellular interior, the result lends support to the hypothesis of protein aggregation as an initiating event in the ALS pathogenesis. The strength of the preferential reduction of repulsive charge is higher in SOD1 associated ALS than in other inherited protein disorders.

Place, publisher, year, edition, pages
2007. Vol. 282, no 29, 21230-21236 p.
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Biochemistry and Molecular Biology
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URN: urn:nbn:se:su:diva-22465DOI: 10.1074/jbc.M700765200ISI: 000248047500050PubMedID: 17513298OAI: oai:DiVA.org:su-22465DiVA: diva2:188992
Available from: 2007-12-20 Created: 2007-12-20 Last updated: 2015-07-29Bibliographically approved

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Nordlund, AnnaOliveberg, Mikael
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