nitrate reductase [Escherichia coli str. K-12 substr. MG1655]

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Characterization of a periplasmic nitrate reductase in complex with its biosynthetic chaperone. [FEBS J. 2014]
Characterization of a periplasmic nitrate reductase in complex with its biosynthetic chaperone.
Dow JM, Grahl S, Ward R, Evans R, Byron O, Norman DG, Palmer T, Sargent F. FEBS J. 2014 Jan; 281(1):246-60. Epub 2013 Dec 9.
Overlapping transport and chaperone-binding functions within a bacterial twin-arginine signal peptide. [Mol Microbiol. 2012]
Overlapping transport and chaperone-binding functions within a bacterial twin-arginine signal peptide.
Grahl S, Maillard J, Spronk CA, Vuister GW, Sargent F. Mol Microbiol. 2012 Mar; 83(6):1254-67. Epub 2012 Feb 27.
Structural diversity in twin-arginine signal peptide-binding proteins. [Proc Natl Acad Sci U S A. 2007]
Structural diversity in twin-arginine signal peptide-binding proteins.
Maillard J, Spronk CA, Buchanan G, Lyall V, Richardson DJ, Palmer T, Vuister GW, Sargent F. Proc Natl Acad Sci U S A. 2007 Oct 2; 104(40):15641-6. Epub 2007 Sep 27.

RefSeq protein
See the reference protein sequence for NapA signal peptide-binding chaperone NapD (NP_416711.1).

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