Identification of structural elements in Nox1 and Nox4 controlling localization and activity
Identification of structural elements in Nox1 and Nox4 controlling localization and activity
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Author / Creator
Publisher
United States: Mary Ann Liebert, Inc
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Language
English
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Publisher
United States: Mary Ann Liebert, Inc
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Contents
Nox NADPH oxidases differ in their mode of activation, subcellular localization, and physiological function. Nox1 releases superoxide anions (O(2)(-)) and depends on cytosolic activator proteins, whereas Nox4 extracellularly releases hydrogen peroxide (H(2)O(2)), and its activity does not require cotransfection of additional proteins. We constructe...
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Full title
Identification of structural elements in Nox1 and Nox4 controlling localization and activity
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Record Identifier
TN_cdi_proquest_miscellaneous_734035770
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_734035770
Other Identifiers
ISSN
1523-0864
E-ISSN
1557-7716
DOI
10.1089/ARS.2008.2383
