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Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli.
Zapun A, Missiakas D, Raina S, Creighton TE. Zapun A, et al. Among authors: missiakas d. Biochemistry. 1995 Apr 18;34(15):5075-89. doi: 10.1021/bi00015a019. Biochemistry. 1995. PMID: 7536035
The membrane-associated lipoprotein-9 GmpC from Staphylococcus aureus binds the dipeptide GlyMet via side chain interactions.
Williams WA, Zhang RG, Zhou M, Joachimiak G, Gornicki P, Missiakas D, Joachimiak A. Williams WA, et al. Among authors: missiakas d. Biochemistry. 2004 Dec 28;43(51):16193-202. doi: 10.1021/bi048877o. Biochemistry. 2004. PMID: 15610013 Free PMC article.
Thiol-disulfide exchange in an immunoglobulin-like fold: structure of the N-terminal domain of DsbD.
Goulding CW, Sawaya MR, Parseghian A, Lim V, Eisenberg D, Missiakas D. Goulding CW, et al. Among authors: missiakas d. Biochemistry. 2002 Jun 4;41(22):6920-7. doi: 10.1021/bi016038l. Biochemistry. 2002. PMID: 12033924
Making and breaking disulfide bonds.
Raina S, Missiakas D. Raina S, et al. Among authors: missiakas d. Annu Rev Microbiol. 1997;51:179-202. doi: 10.1146/annurev.micro.51.1.179. Annu Rev Microbiol. 1997. PMID: 9343348 Review.
DsbD-catalyzed transport of electrons across the membrane of Escherichia coli.
Krupp R, Chan C, Missiakas D. Krupp R, et al. Among authors: missiakas d. J Biol Chem. 2001 Feb 2;276(5):3696-701. doi: 10.1074/jbc.M009500200. Epub 2000 Nov 20. J Biol Chem. 2001. PMID: 11085993
Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasm.
Chung J, Chen T, Missiakas D. Chung J, et al. Among authors: missiakas d. Mol Microbiol. 2000 Mar;35(5):1099-109. doi: 10.1046/j.1365-2958.2000.01778.x. Mol Microbiol. 2000. PMID: 10712691
The functional properties of DsbG, a thiol-disulfide oxidoreductase from the periplasm of Escherichia coli.
van Straaten M, Missiakas D, Raina S, Darby NJ. van Straaten M, et al. Among authors: missiakas d. FEBS Lett. 1998 May 29;428(3):255-8. doi: 10.1016/s0014-5793(98)00539-0. FEBS Lett. 1998. PMID: 9654144
A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins.
Andersen CL, Matthey-Dupraz A, Missiakas D, Raina S. Andersen CL, et al. Among authors: missiakas d. Mol Microbiol. 1997 Oct;26(1):121-32. doi: 10.1046/j.1365-2958.1997.5581925.x. Mol Microbiol. 1997. PMID: 9383195
Effects of mutations in genes for proteins involved in disulphide bond formation in the periplasm on the activities of anaerobically induced electron transfer chains in Escherichia coli K12.
Metheringham R, Tyson KL, Crooke H, Missiakas D, Raina S, Cole JA. Metheringham R, et al. Among authors: missiakas d. Mol Gen Genet. 1996 Nov 27;253(1-2):95-102. doi: 10.1007/pl00013815. Mol Gen Genet. 1996. PMID: 9003292
The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation.
Missiakas D, Georgopoulos C, Raina S. Missiakas D, et al. EMBO J. 1994 Apr 15;13(8):2013-20. EMBO J. 1994. PMID: 8168498 Free PMC article.
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