A Novel SOD1 Intermediate Oligomer, Role of Free Thiols and Disulfide Exchange
A Novel SOD1 Intermediate Oligomer, Role of Free Thiols and Disulfide Exchange
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Switzerland: Frontiers Research Foundation
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Language
English
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Publisher
Switzerland: Frontiers Research Foundation
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Contents
Wild-type human SOD1 forms a highly conserved intra-molecular disulfide bond between C57-C146, and in its native state is greatly stabilized by binding one copper and one zinc atom per monomer rendering the protein dimeric. Loss of copper extinguishes dismutase activity and destabilizes the protein, increasing accessibility of the disulfide with mo...
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Full title
A Novel SOD1 Intermediate Oligomer, Role of Free Thiols and Disulfide Exchange
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TN_cdi_doaj_primary_oai_doaj_org_article_82d89eaebea5447ea481d71a42a980f0
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_82d89eaebea5447ea481d71a42a980f0
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ISSN
1662-4548,1662-453X
E-ISSN
1662-453X
DOI
10.3389/fnins.2020.619279
