Literature DB >> 7773751

The formation of protein disulphide bonds.

R B Freedman1.   

Abstract

The past year has provided more detail on the formation of native disulphide bonds during protein folding at biosynthesis and has identified important cellular factors in the oxidative folding compartments, namely the eukaryotic endoplasmic reticulum and the bacterial periplasm. This information has enabled traditional in vitro refolding studies to be re-evaluated and their relevance as models for folding in the cell to be established.

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Year:  1995        PMID： 7773751     DOI： 10.1016/0959-440x(95)80013-q

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN： 0959-440X            Impact factor:   6.809


  23 in total

1.  Enzymatic reduction of disulfide bonds in lysosomes: characterization of a gamma-interferon-inducible lysosomal thiol reductase (GILT).

Authors:  B Arunachalam; U T Phan; H J Geuze; P Cresswell
Journal:  Proc Natl Acad Sci U S A       Date:  2000-01-18       Impact factor: 11.205

2.  Promotion of transferrin folding by cyclic interactions with calnexin and calreticulin.

Authors:  I Wada; M Kai; S Imai; F Sakane; H Kanoh
Journal:  EMBO J       Date:  1997-09-01       Impact factor: 11.598

Review 3.  Chaperonins.

Authors:  N A Ranson; H E White; H R Saibil
Journal:  Biochem J       Date:  1998-07-15       Impact factor: 3.857

4.  Baculovirus expression of two protein disulphide isomerase isoforms from Caenorhabditis elegans and characterization of prolyl 4-hydroxylases containing one of these polypeptides as their beta subunit.

Authors:  J Veijola; P Annunen; P Koivunen; A P Page; T Pihlajaniemi; K I Kivirikko
Journal:  Biochem J       Date:  1996-08-01       Impact factor: 3.857

Review 5.  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

6.  pH-dependence of the dithiol-oxidizing activity of DsbA (a periplasmic protein thiol:disulphide oxidoreductase) and protein disulphide-isomerase: studies with a novel simple peptide substrate.

Authors:  L W Ruddock; T R Hirst; R B Freedman
Journal:  Biochem J       Date:  1996-05-01       Impact factor: 3.857

7.  The reduction potential of the active site disulfides of human protein disulfide isomerase limits oxidation of the enzyme by Ero1α.

Authors:  Joseph E Chambers; Timothy J Tavender; Ojore B V Oka; Stacey Warwood; David Knight; Neil J Bulleid
Journal:  J Biol Chem       Date:  2010-07-23       Impact factor: 5.157

8.  Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins.

Authors:  Catherine E Jessop; Rachel H Watkins; Jennifer J Simmons; Mohammed Tasab; Neil J Bulleid
Journal:  J Cell Sci       Date:  2009-11-03       Impact factor: 5.285

Review 9.  Protein folding in the endoplasmic reticulum: lessons from the human chorionic gonadotropin beta subunit.

Authors:  R W Ruddon; S A Sherman; E Bedows
Journal:  Protein Sci       Date:  1996-08       Impact factor: 6.725

10.  The refolding of hen egg white riboflavin-binding protein: effect of protein disulphide isomerase on the reoxidation of the reduced protein.

Authors:  D A McClelland; S H McLaughlin; R B Freedman; N C Price
Journal:  Biochem J       Date:  1995-10-01       Impact factor: 3.857
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