Format
Sort by
Items per page

Send to

Choose Destination

Links from PubMed

Items: 1 to 20 of 102

1.

Protein folding drives disulfide formation.

Kosuri P, Alegre-Cebollada J, Feng J, Kaplan A, Inglés-Prieto A, Badilla CL, Stockwell BR, Sanchez-Ruiz JM, Holmgren A, Fernández JM.

Cell. 2012 Nov 9;151(4):794-806. doi: 10.1016/j.cell.2012.09.036.

2.

Effect of glutaredoxin and protein disulfide isomerase on the glutathione-dependent folding of ribonuclease A.

Ruoppolo M, Lundström-Ljung J, Talamo F, Pucci P, Marino G.

Biochemistry. 1997 Oct 7;36(40):12259-67.

PMID:
9315864
3.

Protein disulfide-isomerase interacts with a substrate protein at all stages along its folding pathway.

Irvine AG, Wallis AK, Sanghera N, Rowe ML, Ruddock LW, Howard MJ, Williamson RA, Blindauer CA, Freedman RB.

PLoS One. 2014 Jan 20;9(1):e82511. doi: 10.1371/journal.pone.0082511. eCollection 2014.

4.

Discrimination between native and non-native disulfides by protein-disulfide isomerase.

Zheng J, Gilbert HF.

J Biol Chem. 2001 May 11;276(19):15747-52. Epub 2001 Feb 2.

5.

Protein disulfide isomerase isomerizes non-native disulfide bonds in human proinsulin independent of its peptide-binding activity.

Winter J, Gleiter S, Klappa P, Lilie H.

Protein Sci. 2011 Mar;20(3):588-96. doi: 10.1002/pro.592.

6.

Is protein disulfide isomerase a redox-dependent molecular chaperone?

Lumb RA, Bulleid NJ.

EMBO J. 2002 Dec 16;21(24):6763-70.

7.

The thioredoxin superfamily in oxidative protein folding.

Lu J, Holmgren A.

Antioxid Redox Signal. 2014 Jul 20;21(3):457-70. doi: 10.1089/ars.2014.5849. Epub 2014 Mar 6. Review.

PMID:
24483600
8.

The crystal structure of the protein-disulfide isomerase family member ERp27 provides insights into its substrate binding capabilities.

Kober FX, Koelmel W, Kuper J, Drechsler J, Mais C, Hermanns HM, Schindelin H.

J Biol Chem. 2013 Jan 18;288(3):2029-39. doi: 10.1074/jbc.M112.410522. Epub 2012 Nov 28.

9.

Catalysis of protein folding by protein disulfide isomerase and small-molecule mimics.

Kersteen EA, Raines RT.

Antioxid Redox Signal. 2003 Aug;5(4):413-24. Review.

10.

Oxidative protein folding in vitro: a study of the cooperation between quiescin-sulfhydryl oxidase and protein disulfide isomerase.

Rancy PC, Thorpe C.

Biochemistry. 2008 Nov 18;47(46):12047-56. doi: 10.1021/bi801604x. Epub 2008 Oct 21.

11.

Different interaction modes for protein-disulfide isomerase (PDI) as an efficient regulator and a specific substrate of endoplasmic reticulum oxidoreductin-1α (Ero1α).

Zhang L, Niu Y, Zhu L, Fang J, Wang X, Wang L, Wang CC.

J Biol Chem. 2014 Nov 7;289(45):31188-99. doi: 10.1074/jbc.M114.602961. Epub 2014 Sep 25.

12.
13.

Protein disulfide isomerase: the multifunctional redox chaperone of the endoplasmic reticulum.

Noiva R.

Semin Cell Dev Biol. 1999 Oct;10(5):481-93. Review.

PMID:
10597631
14.

Protein disulfide isomerase assists protein folding as both an isomerase and a chaperone.

Wang CC.

Ann N Y Acad Sci. 1998 Dec 13;864:9-13. Review.

PMID:
9928079
15.

A small-molecule catalyst of protein folding in vitro and in vivo.

Woycechowsky KJ, Wittrup KD, Raines RT.

Chem Biol. 1999 Dec;6(12):871-9.

16.

Reduction-reoxidation cycles contribute to catalysis of disulfide isomerization by protein-disulfide isomerase.

Schwaller M, Wilkinson B, Gilbert HF.

J Biol Chem. 2003 Feb 28;278(9):7154-9. Epub 2002 Dec 15.

17.

Mia40 combines thiol oxidase and disulfide isomerase activity to efficiently catalyze oxidative folding in mitochondria.

Koch JR, Schmid FX.

J Mol Biol. 2014 Dec 12;426(24):4087-98. doi: 10.1016/j.jmb.2014.10.022. Epub 2014 Nov 1.

PMID:
25451030
18.
19.

The machinery for oxidative protein folding in thermophiles.

Pedone E, Limauro D, Bartolucci S.

Antioxid Redox Signal. 2008 Jan;10(1):157-69. Review.

PMID:
17956189
20.

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

Supplemental Content

Support Center