Literature DB >> 11006541

Native disulfide bond formation in proteins.

K J Woycechowsky1, R T Raines.   

Abstract

Native disulfide bond formation is critical for the proper folding of many proteins. Recent studies using newly identified protein oxidants, folding catalysts, and mutant cells provide insight into the mechanism of oxidative protein folding in vivo. This insight promises new strategies for more efficient protein production.

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Year:  2000        PMID： 11006541      PMCID： PMC2814060          DOI： 10.1016/s1367-5931(00)00128-9

Source DB:  PubMed          Journal:  Curr Opin Chem Biol        ISSN： 1367-5931            Impact factor:   8.822


  39 in total

Review 1.  Electron avenue: pathways of disulfide bond formation and isomerization.

Authors:  L Debarbieux; J Beckwith
Journal:  Cell       Date:  1999-10-15       Impact factor: 41.582

2.  Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum.

Authors:  A R Frand; C A Kaiser
Journal:  Mol Cell       Date:  1999-10       Impact factor: 17.970

3.  Identifying and characterizing a second structural domain of protein disulfide isomerase.

Authors:  N J Darby; M van Straaten; E Penka; R Vincentelli; J Kemmink
Journal:  FEBS Lett       Date:  1999-04-01       Impact factor: 4.124

Review 4.  The protein disulphide-isomerase family: unravelling a string of folds.

Authors:  D M Ferrari; H D Söling
Journal:  Biochem J       Date:  1999-04-01       Impact factor: 3.857

5.  Yeast flavin-containing monooxygenase generates oxidizing equivalents that control protein folding in the endoplasmic reticulum.

Authors:  J K Suh; L L Poulsen; D M Ziegler; J D Robertus
Journal:  Proc Natl Acad Sci U S A       Date:  1999-03-16       Impact factor: 11.205

6.  The CXXC motif: crystal structure of an active-site variant of Escherichia coli thioredoxin.

Authors:  L W Schultz; P T Chivers; R T Raines
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  1999-09

7.  Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway.

Authors:  T Kobayashi; K Ito
Journal:  EMBO J       Date:  1999-03-01       Impact factor: 11.598

8.  Expression of active human tissue-type plasminogen activator in Escherichia coli.

Authors:  J Qiu; J R Swartz; G Georgiou
Journal:  Appl Environ Microbiol       Date:  1998-12       Impact factor: 4.792

9.  The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide.

Authors:  P Koivunen; A Pirneskoski; P Karvonen; J Ljung; T Helaakoski; H Notbohm; K I Kivirikko
Journal:  EMBO J       Date:  1999-01-04       Impact factor: 11.598

10.  An unconventional role for cytoplasmic disulfide bonds in vaccinia virus proteins.

Authors:  J K Locker; G Griffiths
Journal:  J Cell Biol       Date:  1999-01-25       Impact factor: 10.539
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  32 in total

1.  CxxS: fold-independent redox motif revealed by genome-wide searches for thiol/disulfide oxidoreductase function.

Authors:  Dmitri E Fomenko; Vadim N Gladyshev
Journal:  Protein Sci       Date:  2002-10       Impact factor: 6.725

2.  n→π* Interactions Modulate the Properties of Cysteine Residues and Disulfide Bonds in Proteins.

Authors:  Henry R Kilgore; Ronald T Raines
Journal:  J Am Chem Soc       Date:  2018-12-06       Impact factor: 15.419

3.  Organocatalysts of oxidative protein folding inspired by protein disulfide isomerase.

Authors:  John C Lukesh; Kristen A Andersen; Kelly K Wallin; Ronald T Raines
Journal:  Org Biomol Chem       Date:  2014-11-21       Impact factor: 3.876

4.  Short stature explained by dimerization of human growth hormone induced by a p.C53S point mutation.

Authors:  Max Sander; Zida Wu; Christian J Strasburger
Journal:  J Biol Chem       Date:  2020-03-04       Impact factor: 5.157

5.  The CXC motif: a functional mimic of protein disulfide isomerase.

Authors:  Kenneth J Woycechowsky; Ronald T Raines
Journal:  Biochemistry       Date:  2003-05-13       Impact factor: 3.162

6.  Both chaperone and isomerase functions of protein disulfide isomerase are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor.

Authors:  Jui Pandhare; Vasanti Deshpande
Journal:  Protein Sci       Date:  2004-08-04       Impact factor: 6.725

Review 7.  Misfolded proinsulin in the endoplasmic reticulum during development of beta cell failure in diabetes.

Authors:  Anoop Arunagiri; Leena Haataja; Corey N Cunningham; Neha Shrestha; Billy Tsai; Ling Qi; Ming Liu; Peter Arvan
Journal:  Ann N Y Acad Sci       Date:  2018-01-28       Impact factor: 5.691

8.  The boxing glove shape of subunit d of the yeast V-ATPase in solution and the importance of disulfide formation for folding of this protein.

Authors:  Youg R Thaker; Manfred Roessle; Gerhard Grüber
Journal:  J Bioenerg Biomembr       Date:  2007-09-26       Impact factor: 2.945

9.  pH dependence of the isomerase activity of protein disulfide isomerase: insights into its functional relevance.

Authors:  Yu-Hsiang Wang; Mahesh Narayan
Journal:  Protein J       Date:  2008-04       Impact factor: 2.371

10.  Structure and function of Bacillus subtilis YphP, a prokaryotic disulfide isomerase with a CXC catalytic motif .

Authors:  Urszula Derewenda; Tomasz Boczek; Kelly L Gorres; Minmin Yu; Li-wei Hung; David Cooper; Andrzej Joachimiak; Ronald T Raines; Zygmunt S Derewenda
Journal:  Biochemistry       Date:  2009-09-15       Impact factor: 3.162
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