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Structure of the BTB domain of Keap1 and its interaction with the triterpenoid antagonist CDDO

Structure of the BTB domain of Keap1 and its interaction with the triterpenoid antagonist CDDO

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1532653323

Structure of the BTB domain of Keap1 and its interaction with the triterpenoid antagonist CDDO

About this item

Full title

Structure of the BTB domain of Keap1 and its interaction with the triterpenoid antagonist CDDO

Publisher

United States: Public Library of Science

Journal title

PloS one, 2014-06, Vol.9 (6), p.e98896-e98896

Language

English

Formats

Publication information

Publisher

United States: Public Library of Science

More information

Scope and Contents

Contents

The protein Keap1 is central to the regulation of the Nrf2-mediated cytoprotective response, and is increasingly recognized as an important target for therapeutic intervention in a range of diseases involving excessive oxidative stress and inflammation. The BTB domain of Keap1 plays key roles in sensing environmental electrophiles and in mediating...

Alternative Titles

Full title

Structure of the BTB domain of Keap1 and its interaction with the triterpenoid antagonist CDDO

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_plos_journals_1532653323

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1532653323

Other Identifiers

ISSN

1932-6203

E-ISSN

1932-6203

DOI

10.1371/journal.pone.0098896

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