Soluble and membrane-bound protein carrier mediate direct copper transport to the ethylene receptor family
Author:
Funder
Deutsche Forschungsgemeinschaft
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-019-47185-6.pdf
Reference35 articles.
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2. Lamb, A. L. et al. Crystal structure of the copper chaperone for superoxide dismutase. Nat Struct Biol 6, 724–729, https://doi.org/10.1038/11489 (1999).
3. Lamb, A. L., Torres, A. S., O’Halloran, T. V. & Rosenzweig, A. C. Heterodimeric structure of superoxide dismutase in complex with its metallochaperone. Nat Struct Biol 8, 751–755, https://doi.org/10.1038/nsb0901-751 (2001).
4. Portnoy, M. E. et al. Structure-function analyses of the ATX1 metallochaperone. The Journal of biological chemistry 274, 15041–15045 (1999).
5. Burg, S. P. & Burg, E. A. Molecular requirements for the biological activity of ethylene. Plant physiology 42, 144–152 (1967).
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