Literature DB >> 7765801

Mechanisms and catalysts of disulfide bond formation in proteins.

T E Creighton1, A Zapun, N J Darby.   

Abstract

The formation of disulphide bonds is an important co- and post-translational event in the biosynthesis of many extracellular proteins that is often coupled to protein folding. Progress in understanding how disulphide bonds form in model proteins provides insight into how the process can be manipulated to optimize the production of engineered proteins.

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Year:  1995        PMID: 7765801     DOI: 10.1016/s0167-7799(00)88896-4

Source DB:  PubMed          Journal:  Trends Biotechnol        ISSN: 0167-7799            Impact factor:   19.536


  13 in total

Review 1.  Protein disulfide isomerases exploit synergy between catalytic and specific binding domains.

Authors:  Robert B Freedman; Peter Klappa; Lloyd W Ruddock
Journal:  EMBO Rep       Date:  2002-02       Impact factor: 8.807

2.  Oxidative refolding of recombinant prochymosin.

Authors:  C Wei; B Tang; Y Zhang; K Yang
Journal:  Biochem J       Date:  1999-05-15       Impact factor: 3.857

3.  A novel system for continuous protein refolding and on-line capture by expanded bed adsorption.

Authors:  Henrik Ferré; Emmanuel Ruffet; Lise-Lotte B Nielsen; Mogens Holst Nissen; Timothy J Hobley; Owen R T Thomas; Søren Buus
Journal:  Protein Sci       Date:  2005-08       Impact factor: 6.725

4.  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

5.  Probing protein folding and stability using disulfide bonds.

Authors:  N Darby; T E Creighton
Journal:  Mol Biotechnol       Date:  1997-02       Impact factor: 2.695

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.  Roles of protein-disulfide isomerase-mediated disulfide bond formation of yeast Mnl1p in endoplasmic reticulum-associated degradation.

Authors:  Machiko Sakoh-Nakatogawa; Shuh-Ichi Nishikawa; Toshiya Endo
Journal:  J Biol Chem       Date:  2009-03-11       Impact factor: 5.157

Review 8.  Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria.

Authors:  Melissa E Reardon-Robinson; Hung Ton-That
Journal:  J Bacteriol       Date:  2015-12-07       Impact factor: 3.490

9.  Induced ER chaperones regulate a receptor-like kinase to mediate antiviral innate immune response in plants.

Authors:  Jeffrey L Caplan; Xiaohong Zhu; Padmavathi Mamillapalli; Rajendra Marathe; Radhamani Anandalakshmi; S P Dinesh-Kumar
Journal:  Cell Host Microbe       Date:  2009-11-19       Impact factor: 21.023

10.  The C-terminal cysteine annulus participates in auto-chaperone function for Salmonella phage P22 tailspike folding and assembly.

Authors:  Takumi Takata; Cameron Haase-Pettingell; Jonathan King
Journal:  Bacteriophage       Date:  2012-01-01
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