Mechanisms and catalysts of disulfide bond formation in proteins (Q40535852)

21 September 2017

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title

Mechanisms and catalysts of disulfide bond formation in proteins (English)

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21 September 2017

Creighton TE

1

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21 September 2017

Zapun A

series ordinal

2

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21 September 2017

Darby NJ

series ordinal

3

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21 September 2017

publication date

1 January 1995

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21 September 2017

published in

Trends in Biotechnology

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21 September 2017

volume

13

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21 September 2017

issue

1

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21 September 2017

page(s)

18-23

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The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo.

21 September 2017

cites work

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https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

The redox properties of protein disulfide isomerase (DsbA) of Escherichia coli result from a tense conformation of its oxidized form.

1 reference

https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

Stability studies on derivatives of the bovine pancreatic trypsin inhibitor

1 reference

https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

Dissecting the disulphide-coupled folding pathway of bovine pancreatic trypsin inhibitor. Forming the first disulphide bonds in analogues of the reduced protein

1 reference

https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

Oxidized redox state of glutathione in the endoplasmic reticulum

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https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

Identification of a protein required for disulfide bond formation in vivo

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https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

The bonds that tie: catalyzed disulfide bond formation

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https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli

1 reference

https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

Structural characterization of the disulfide folding intermediates of bovine alpha-lactalbumin

1 reference

https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

1H NMR Analysis of the Partly-folded Non-native Two-disulphide Intermediates (30-51,5-14) and (30-51,5-38) in the Folding Pathway of Bovine Pancreatic Trypsin Inhibitor

1 reference

https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

Reexamination of the folding of BPTI: predominance of native intermediates.

1 reference

https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

On the biosynthesis of bovine pancreatic trypsin inhibitor (BPTI). Structure, processing, folding and disulphide bond formation of the precursor in vitro and in microsomes

1 reference

https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

Protein disulphide isomerase: building bridges in protein folding

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https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

Catalysis by protein-disulphide isomerase of the unfolding and refolding of proteins with disulphide bonds

1 reference

https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

Dissecting the mechanism of protein disulfide isomerase: catalysis of disulfide bond formation in a model peptide

1 reference

https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

Bacterial protein disulfide isomerase: efficient catalysis of oxidative protein folding at acidic pH

1 reference

https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

Effects of DsbA on the disulfide folding of bovine pancreatic trypsin inhibitor and alpha-lactalbumin.

1 reference

https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

Crystal structure of the DsbA protein required for disulphide bond formation in vivo

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https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

Replacement of the active-site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo.

1 reference

https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo

1 reference

https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

Structure of a thermostable disulfide-bridge mutant of phage T4 lysozyme shows that an engineered cross-link in a flexible region does not increase the rigidity of the folded protein

1 reference

https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli.

1 reference

https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

Protein folding in the periplasm of Escherichia coli

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https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

Protein disulfide isomerase overexpression increases secretion of foreign proteins in Saccharomyces cerevisiae

1 reference

https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

A protein-folding reaction under kinetic control

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https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

The pro region of BPTI facilitates folding

1 reference

https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

The endoplasmic reticulum as a protein-folding compartment

1 reference

https://api.crossref.org/works/10.1016/S0167-7799(00)88896-4

7 January 2021

10.1016/S0167-7799(00)88896-4

Identifiers

DOI

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21 September 2017

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