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Biochemical and structural study of the homologues of the thiol-disulfide oxidoreductase DsbA in Neisseria meningitidis.
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Structural and biochemical characterization of the oxidoreductase NmDsbA3 from Neisseria meningitidis.
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Functional diversity of three different DsbA proteins from Neisseria meningitidis.
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The atypical thiol-disulfide exchange protein α-DsbA2 from Wolbachia pipientis is a homotrimeric disulfide isomerase.
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Dissecting the machinery that introduces disulfide bonds in Pseudomonas aeruginosa.
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3
Functional diversity of three different DsbA proteins from Neisseria meningitidis.
Microbiology (Reading). 2004 Sep;150(Pt 9):2993-3000. doi: 10.1099/mic.0.27216-0.
5
Integration of macromolecular diffraction data.
Acta Crystallogr D Biol Crystallogr. 1999 Oct;55(Pt 10):1696-702. doi: 10.1107/s090744499900846x.
6
Structure of TcpG, the DsbA protein folding catalyst from Vibrio cholerae.
J Mol Biol. 1997 Apr 25;268(1):137-46. doi: 10.1006/jmbi.1997.0940.
7
Crystallization of DsbA, an Escherichia coli protein required for disulphide bond formation in vivo.
J Mol Biol. 1993 Apr 5;230(3):1097-100. doi: 10.1006/jmbi.1993.1226.
8
Crystal structure of the DsbA protein required for disulphide bond formation in vivo.
Nature. 1993 Sep 30;365(6445):464-8. doi: 10.1038/365464a0.
9
Solvent content of protein crystals.
J Mol Biol. 1968 Apr 28;33(2):491-7. doi: 10.1016/0022-2836(68)90205-2.
10
Identification of a protein required for disulfide bond formation in vivo.
Cell. 1991 Nov 1;67(3):581-9. doi: 10.1016/0092-8674(91)90532-4.

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