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Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS

Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_20800422

Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS

About this item

Full title

Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2009-05, Vol.106 (19), p.7774-7779

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Transgenic mice that model familial (f)ALS, caused by mutations in superoxide dismutase (SOD)1, develop paralysis with pathology that includes the accumulation of aggregated forms of the mutant protein. Using a highly sensitive detergent extraction assay, we traced the appearance and abundance of detergent-insoluble and disulfide cross-linked aggre...

Alternative Titles

Full title

Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_miscellaneous_20800422

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_20800422

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.0902505106

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