Book Chapter10.1016/B978-0-12-385095-9.00236-0
Disulfide Bond Formation
Gautam Rajpal,Peter Arvan +1 more
- 29 Aug 2013
- pp 1721-1729
33
About: The article was published on 29 Aug 2013.
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Citations
Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system
TL;DR: An overview of current strategies to improve recombinant protein production in E. coli is provided, including the key factors for successful protein production, highlighting solubleprotein production, and a comprehensive summary of the latest available and traditionally used gene fusion technologies.
Misfolded proinsulin in the endoplasmic reticulum during development of beta cell failure in diabetes
Anoop Arunagiri,Leena Haataja,Corey N. Cunningham,Neha Shrestha,Billy Tsai,Ling Qi,Ming Liu,Ming Liu,Peter Arvan +8 more
TL;DR: The steady‐state level of misfolded proinsulin—a potential ER stressor—is linked to production rate, ER environment, presence or absence of naturally occurring (mutational) defects in proins insulin, and (4) clearance of mis Folded Proinsulin molecules.
Liquid–liquid phase separation as an organizing principle of intracellular space: overview of the evolution of the cell compartmentalization concept
Iuliia A. Antifeeva,Alexander V. Fonin,Anna S. Fefilova,Olesya V. Stepanenko,Olga I. Povarova,Sergey A. Silonov,Irina M. Kuznetsova,Vladimir N. Uversky,Konstantin K. Turoverov +8 more
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72
Advances in hydrogels based on dynamic covalent bonding and prospects for its biomedical application
TL;DR: In this paper, a review of dynamic covalent bonding (DCB) hydrogels is presented, which mainly highlights the developing techniques of preparing DCB hydrogel, the materials of DCB hygrogels preparation, the special properties of DCBs, and the biomedical application prospects for DCBs.
67
Disulfide Mispairing During Proinsulin Folding in the Endoplasmic Reticulum.
TL;DR: A molecular dissection of proinsulin disulfide bond formation is undertaken, using bioengineered proinsulins that can form only two (or even only one) of the native proins insulin disulfides, to suggest possible therapeutic avenues to ameliorate ER stress and diabetes.
55
References
Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation.
Feras Hatahet,Lloyd W. Ruddock +1 more
TL;DR: This review aims to provide background on the chemistry of disulfide bond formation and rearrangement, including the concept of reduction potential, before examining the structure of PDI and discuss other human and yeast PDI-family members.
677
The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
Alison R. Frand,Chris A. Kaiser +1 more
TL;DR: It is concluded that Ero1p functions in a novel mechanism that sustains the ER oxidizing potential, supporting net formation of protein disulfide bonds in a temperature-sensitive ero1-1 mutant.
520
ERdj5 Is Required as a Disulfide Reductase for Degradation of Misfolded Proteins in the ER
TL;DR: This work has found that an ER-resident protein ERdj5 had a reductase activity, cleaved the disulfide bonds of misfolded proteins, and accelerated ERAD through its physical and functional associations with EDEM (ER degradation–enhancing α-mannosidase–like protein) and anER-resident chaperone BiP.
408
Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum.
Alison R. Frand,Chris A. Kaiser +1 more
TL;DR: Results show that oxidizing equivalents flow from Ero1p to substrate proteins via PDI, indicating that PDI functions as an oxidase in vivo, and define a pathway for protein disulfide bond formation in the ER.
403
Oxidative protein folding by an endoplasmic reticulum localized peroxiredoxin
Ester Zito,Eduardo P. Melo,Eduardo P. Melo,Yun Yang,Asa Wahlander,Thomas A. Neubert,David Ron +6 more
TL;DR: Observations implicate ER-localized PRDX4 in a previously unanticipated, parallel, ERO1-independent pathway that couples hydroperoxide production to oxidative protein folding in mammalian cells.
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