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Items: 1 to 20 of 69

1.

The oxidative protein folding machinery in plant cells.

Aller I, Meyer AJ.

Protoplasma. 2013 Aug;250(4):799-816. doi: 10.1007/s00709-012-0463-x. Epub 2012 Oct 23. Review.

PMID:
23090240
2.

Role of ascorbate in oxidative protein folding.

Bánhegyi G, Csala M, Szarka A, Varsányi M, Benedetti A, Mandl J.

Biofactors. 2003;17(1-4):37-46. Review.

PMID:
12897427
3.

Pathways of disulfide bond formation in Escherichia coli.

Messens J, Collet JF.

Int J Biochem Cell Biol. 2006;38(7):1050-62. Epub 2006 Jan 11. Review.

PMID:
16446111
4.

DsbA and DsbC-catalyzed oxidative folding of proteins with complex disulfide bridge patterns in vitro and in vivo.

Maskos K, Huber-Wunderlich M, Glockshuber R.

J Mol Biol. 2003 Jan 17;325(3):495-513.

PMID:
12498799
5.

Making and breaking disulfide bonds.

Raina S, Missiakas D.

Annu Rev Microbiol. 1997;51:179-202. Review.

PMID:
9343348
6.

The underlying mechanism for the diversity of disulfide folding pathways.

Chang JY, Li L, Bulychev A.

J Biol Chem. 2000 Mar 24;275(12):8287-9.

7.

Structural basis of protein disulfide bond generation in the cell.

Inaba K.

Genes Cells. 2010 Sep 1;15(9):935-43. doi: 10.1111/j.1365-2443.2010.01434.x. Epub 2010 Jul 27. Review.

8.

Oxidative folding of Amaranthus alpha-amylase inhibitor: disulfide bond formation and conformational folding.

Cemazar M, Zahariev S, Pongor S, Hore PJ.

J Biol Chem. 2004 Apr 16;279(16):16697-705. Epub 2004 Jan 28.

9.

A novel plant protein-disulfide isomerase involved in the oxidative folding of cystine knot defense proteins.

Gruber CW, Cemazar M, Clark RJ, Horibe T, Renda RF, Anderson MA, Craik DJ.

J Biol Chem. 2007 Jul 13;282(28):20435-46. Epub 2007 May 22.

10.

Disulfide folding pathways of cystine knot proteins. Tying the knot within the circular backbone of the cyclotides.

Daly NL, Clark RJ, Craik DJ.

J Biol Chem. 2003 Feb 21;278(8):6314-22. Epub 2002 Dec 12.

11.

Oxidative folding of the cystine knot motif in cyclotide proteins.

Craik DJ, Daly NL.

Protein Pept Lett. 2005 Feb;12(2):147-52. Review.

PMID:
15723640
12.

Diverse pathways of oxidative folding of disulfide proteins: underlying causes and folding models.

Chang JY.

Biochemistry. 2011 May 3;50(17):3414-31. doi: 10.1021/bi200131j. Epub 2011 Apr 6. Review.

PMID:
21410235
13.

Enzymatic catalysis of disulfide formation.

Noiva R.

Protein Expr Purif. 1994 Feb;5(1):1-13. Review.

PMID:
7909462
14.

The disulfide bond formation (Dsb) system.

Ito K, Inaba K.

Curr Opin Struct Biol. 2008 Aug;18(4):450-8. doi: 10.1016/j.sbi.2008.02.002. Epub 2008 Apr 11. Review.

PMID:
18406599
15.

Oxidative protein folding: many different ways to introduce disulfide bonds.

Kadokura H.

Antioxid Redox Signal. 2006 May-Jun;8(5-6):731-3. No abstract available.

PMID:
16771664
16.

Reduction of the endoplasmic reticulum accompanies the oxidative damage of diabetes mellitus.

Nardai G, Korcsmáros T, Papp E, Csermely P.

Biofactors. 2003;17(1-4):259-67. Review.

PMID:
12897447
17.
18.

Characterization of two homologous disulfide bond systems involved in virulence factor biogenesis in uropathogenic Escherichia coli CFT073.

Totsika M, Heras B, Wurpel DJ, Schembri MA.

J Bacteriol. 2009 Jun;191(12):3901-8. doi: 10.1128/JB.00143-09. Epub 2009 Apr 17.

19.

Disulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals.

Sato Y, Inaba K.

FEBS J. 2012 Jul;279(13):2262-71. doi: 10.1111/j.1742-4658.2012.08593.x. Epub 2012 Jun 8. Review.

20.

Oxidative protein folding in eukaryotes: mechanisms and consequences.

Tu BP, Weissman JS.

J Cell Biol. 2004 Feb 2;164(3):341-6. Review.

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