Journal
NATURE CHEMICAL BIOLOGY
Volume 4, Issue 3, Pages 148-151Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nchembio0308-148
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Funding
- NIGMS NIH HHS [GM 38784, F32 GM071129, R37 GM038784-20, R01 GM038784, R37 GM038784, GM 071129] Funding Source: Medline
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R37GM038784, R29GM038784, R01GM038784, F32GM071129] Funding Source: NIH RePORTER
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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.
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