Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomerase (Q24675311)

1

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N J Darby

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K Dijkstra

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R M Scheek

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T E Creighton

Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene

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language of work or name

English

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publication date

December 1995

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published in

Protein Science

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volume

4

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issue

12

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page(s)

2587-93

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cites work

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

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Heteronuclear three-dimensional NMR spectroscopy of the inflammatory protein C5a

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Crystal structure of thioredoxin from Escherichia coli at 1.68 A resolution

7 April 2017

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Relationship between nuclear magnetic resonance chemical shift and protein secondary structure

7 April 2017

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Sequence-specific 1H n.m.r. assignments and determination of the three-dimensional structure of reduced Escherichia coli glutaredoxin

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Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coli. This multifunctional polypeptide has two independently acting catalytic sites for the isomerase activity

7 April 2017

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Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions

7 April 2017

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NMR structure of oxidized Escherichia coli glutaredoxin: Comparison with reduced E. coli glutaredoxin and functionally related proteins

7 April 2017

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Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins

7 April 2017

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

7 April 2017

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Mutations in the thioredoxin sites of protein disulfide isomerase reveal functional nonequivalence of the N- and C-terminal domains.

28 September 2017

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Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: pre-steady-state kinetics and the utilization of the oxidizing equivalents of the isomerase

28 September 2017

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Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer

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Protein disulfide isomerase. A multifunctional protein resident in the lumen of the endoplasmic reticulum

28 September 2017

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Selective inhibition of protein disulfide isomerase by estrogens.

28 September 2017

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Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex.

28 September 2017

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Determination of the sequence of the yeast YCL313 gene localized on chromosome III. Homology with the protein disulfide isomerase (PDI gene product) of other organisms

30 May 2018

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Structural properties of the microsomal triglyceride-transfer protein complex.

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A Pro to His mutation in active site of thioredoxin increases its disulfide-isomerase activity 10-fold. New refolding systems for reduced or randomly oxidized ribonuclease

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Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H-15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: applicati

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

19 June 2018

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

28 November 2018

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12 December 2020

Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase

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12 December 2020

The interaction of human estrogen receptor with DNA is modulated by receptor-associated proteins

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12 December 2020

Improved high-level expression system for eukaryotic genes in Escherichia coli using T7 RNA polymerase and rare ArgtRNAs

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12 December 2020

Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli thioredoxin

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12 December 2020

Protein disulphide isomerase: building bridges in protein folding

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12 December 2020

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

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7 January 2021

Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy

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7 January 2021

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

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7 January 2021

Protein disulfide isomerase is essential for viability in Saccharomyces cerevisiae.

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7 January 2021

Heteronuclear three-dimensional NMR spectroscopy of isotopically labelled biological macromolecules

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7 January 2021

Assignment of the proton NMR spectrum of reduced and oxidized thioredoxin: sequence-specific assignments, secondary structure, and global fold

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7 January 2021

Empirical correlation between protein backbone conformation and C.alpha. and C.beta. 13C nuclear magnetic resonance chemical shifts

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7 January 2021

Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin.

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7 January 2021

Protein disulphide-isomerase: a homologue of thioredoxin implicated in the biosynthesis of secretory proteins

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7 January 2021