A place for thioether chemistry in cellular copper ion recognition and trafficking

Anna V. Davis*, Thomas V. O'Halloran

*Corresponding author for this work

Research output: Contribution to journalComment/debate

156 Scopus citations

Abstract

Over the last decade, cysteine thiolate ligands have been shown to be critical to the Cu(I) (cuprous) binding chemistry of many cytosolic metallochaperone and metalloregulatory proteins involved in copper physiology. More recently, the thioether group of methionine has begun to emerge as an important Cu(I) ligand for trafficking proteins in more oxidizing cellular environments.

Original languageEnglish (US)
Pages (from-to)148-151
Number of pages4
JournalNature Chemical Biology
Volume4
Issue number3
DOIs
StatePublished - Mar 2008

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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