Journal article

Atomic-resolution monitoring of protein maturation in live human cells by NMR

Abstract:: We use NMR directly in live human cells to describe the complete post-translational maturation process of human superoxide dismutase 1 (SOD1). We follow, at atomic resolution, zinc binding, homodimer formation and copper uptake, and discover that copper chaperone for SOD1 oxidizes the SOD1 intrasubunit disulfide bond through both copper-dependent and copper-independent mechanisms. Our approach represents a new strategy for structural investigation of endogenously expressed proteins in a physiological (cellular) environment. © 2013 Nature America, Inc.

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APA Style

Banci, L., Barbieri, L., Bertini, I., Luchinat, E., Secci, E., Zhao, Y., & Aricescu, A. (2013). Atomic-resolution monitoring of protein maturation in live human cells by NMR. Nature Chemical Biology, 9(5), 297–299.

MLA Style

Banci, L., et al. “Atomic-Resolution Monitoring of Protein Maturation in Live Human Cells by NMR.” Nature Chemical Biology, vol. 9, no. 5, 2013, pp. 297–99.

Chicago Style

Banci, L, L Barbieri, I Bertini, E Luchinat, E Secci, Y Zhao, and A Aricescu. 2013. “Atomic-Resolution Monitoring of Protein Maturation in Live Human Cells by NMR.” Nature Chemical Biology 9 (5): 297–99.
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Publisher copy:: 10.1038/nchembio.1202

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+ Banci, L More by this author

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+ Barbieri, L More by this author

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+ Bertini, I More by this author

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+ Luchinat, E More by this author

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+ Secci, E More by this author

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Journal:: Nature Chemical Biology More from this journal
Volume:: 9
Issue:: 5
Pages:: 297-299
Publication date:: 2013-05-01
DOI:: 10.1038/nchembio.1202
EISSN:: 1552-4469
ISSN:: 1552-4450

Language:: English
Pubs id:: pubs:409943
UUID:: uuid:b310a41a-fed6-41e5-85b1-4b7fee36ff66
Local pid:: pubs:409943
Source identifiers:: 409943
Deposit date:: 2013-11-17

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Copyright date:: 2013

Licence:: Terms and Conditions of Use for Oxford University Research Archive

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