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Found 9 results
Filters: keyword is Oxidation-Reduction [Clear All Filters]
2009
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2009. The zinc center influences the redox and thermodynamic properties of Escherichia coli thioredoxin 2.
386(1):60-71. Abstract
2008
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2008. The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner.
Mol. Microbiol.. 67(2):336-349. Abstract
2007
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2007. The conserved active site proline determines the reducing power of Staphylococcus aureus thioredoxin.
J. Mol. Biol.. 368(3):800-811. Abstract
2006
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2006. Arsenate reduction: thiol cascade chemistry with convergent evolution.
J. Mol. Biol.. 362(1):1-17. Abstract
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2006. Pathways of disulfide bond formation in Escherichia coli.
Int. J. Biochem. Cell Biol.. 38(7):1050-1062. Abstract
2004
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2004. How thioredoxin can reduce a buried disulphide bond.
J. Mol. Biol.. 339(3):527-537. Abstract
2003
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2003. Purification of an oxidation-sensitive enzyme, pI258 arsenate reductase from Staphylococcus aureus.
J. Chromatogr. B Analyt. Technol. Biomed. Life Sci.. 790(1-2):217-227. Abstract
2001
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2001. Arsenate reductase from S. aureus plasmid pI258 is a phosphatase drafted for redox duty.
Nat. Struct. Biol.. 8(10):843-847. Abstract
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2001. 1H, 13C and 15N backbone resonance assignment of the arsenate reductase from Staphylococcus aureus in its reduced state.
J. Biomol. NMR. 20(1):95-96.