(Q38363552)

2 September 2017

title

Randomization of the entire active-site helix alpha 1 of the thiol-disulfide oxidoreductase DsbA from Escherichia coli (English)

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2 September 2017

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Bjorn Philipps

1

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2 September 2017

Rudi Glockshuber

series ordinal

2

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2 September 2017

language of work or name

English

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publication date

21 August 2002

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Journal of Biological Chemistry

2 September 2017

published in

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2 September 2017

volume

277

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2 September 2017

issue

45

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2 September 2017

page(s)

43050-43057

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Identification of a protein required for disulfide bond formation in vivo.

2 September 2017

cites work

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https://api.crossref.org/works/10.1074%2FJBC.M207638200

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

21 January 2018

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Structure of reduced DsbA from Escherichia coli in solution

21 January 2018

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Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization

21 January 2018

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Thioredoxin--a fold for all reasons

21 January 2018

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

21 January 2018

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

21 January 2018

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

21 January 2018

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

21 January 2018

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The role of the alpha-helix dipole in protein function and structure

21 January 2018

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Ionisation of cysteine residues at the termini of model alpha-helical peptides. Relevance to unusual thiol pKa values in proteins of the thioredoxin family.

21 January 2018

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Electrostatic interactions in the active site of the N-terminal thioredoxin-like domain of protein disulfide isomerase

21 January 2018

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Urea dependence of thiol-disulfide equilibria in thioredoxin: confirmation of the linkage relationship and a sensitive assay for structure

21 January 2018

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Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases

21 January 2018

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Why is DsbA such an oxidizing disulfide catalyst?

21 January 2018

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Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum

21 January 2018

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Efficient catalysis of disulfide formation during protein folding with a single active-site cysteine

21 January 2018

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Random circular permutation of DsbA reveals segments that are essential for protein folding and stability

21 January 2018

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Rapid and efficient site-specific mutagenesis without phenotypic selection

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M207638200

Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli

21 January 2018

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Calculation of protein extinction coefficients from amino acid sequence data

21 January 2018

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21 January 2018

Tissue sulfhydryl groups

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Quenching of tryptophan fluorescence by the active-site disulfide bridge in the DsbA protein from Escherichia coli.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M207638200

Elimination of all charged residues in the vicinity of the active-site helix of the disulfide oxidoreductase DsbA. Influence of electrostatic interactions on stability and redox properties.

21 January 2018

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Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasm

21 January 2018

1 reference

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Influence of acidic residues and the kink in the active-site helix on the properties of the disulfide oxidoreductase DsbA.

21 January 2018

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De novo design and structural characterization of proteins and metalloproteins

21 January 2018

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Exploration of sequence space for protein engineering.

21 January 2018

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Active barnase variants with completely random hydrophobic cores

21 January 2018

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Functional rapidly folding proteins from simplified amino acid sequences.

21 January 2018

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The complete genome sequence of Escherichia coli K-12

21 January 2018

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MOLMOL: a program for display and analysis of macromolecular structures

21 January 2018

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Context-dependent secondary structure formation of a designed protein sequence

21 January 2018

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Reconstitution of a protein disulfide catalytic system

21 January 2018

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Oxidative protein folding is driven by the electron transport system

21 January 2018

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

21 January 2018

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Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomerase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M207638200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M207638200

A single dipeptide sequence modulates the redox properties of a whole enzyme family

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M207638200

REDUCTION-POTENTIAL OF GLUTATHIONE

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M207638200

Fluorescence quenching in the DsbA protein from Escherichia coli: complete picture of the excited-state energy pathway and evidence for the reshuffling dynamics of the microstates of tryptophan

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M207638200

Influence of the pK(a) value of the buried, active-site cysteine on the redox properties of thioredoxin-like oxidoreductases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M207638200

21 January 2018

Identifiers

DOI

10.1074/JBC.M207638200

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2 September 2017

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