Journal article icon

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.
Publication status:
Published

Actions


Access Document


Publisher copy:
10.1038/nchembio.1202

Authors


Barbieri, L More by this author
Bertini, I More by this author
Luchinat, E More by this author
Expand authors...
Journal:
Nature chemical biology
Volume:
9
Issue:
5
Pages:
297-299
Publication date:
2013-05-05
DOI:
EISSN:
1552-4469
ISSN:
1552-4450
URN:
uuid:2c58dd09-29bc-486d-b6b0-e32c7b41a89d
Source identifiers:
387749
Local pid:
pubs:387749

Terms of use


Metrics



If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP