The structure in solution of the b domain of protein disulfide isomerase (Q27618778)

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9 December 2019

title

The structure in solution of the b domain of protein disulfide isomerase (English)

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9 December 2019

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9 December 2019

author name string

J Kemmink

1

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9 December 2019

K Dijkstra

2

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9 December 2019

M Mariani

3

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9 December 2019

R M Scheek

4

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9 December 2019

E Penka

5

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9 December 2019

N J Darby

7

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9 December 2019

publication date

1 April 1999

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Journal of Biomolecular NMR

9 December 2019

published in

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9 December 2019

volume

13

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issue

4

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9 December 2019

page(s)

357-368

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The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins

9 December 2019

cites work

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The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency

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Calculation of protein structures with ambiguous distance restraints. Automated assignment of ambiguous NOE crosspeaks and disulphide connectivities.

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The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules

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

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Ionization equilibria for side-chain carboxyl groups in oxidized and reduced human thioredoxin and in the complex with its target peptide from the transcription factor NF kappa B.

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Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy

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

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

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12 December 2020

Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin.

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12 December 2020

Protein disulphide isomerase: building bridges in protein folding

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12 December 2020

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

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Measurement of HN-H alpha J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods

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12 December 2020

Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF kappa B

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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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Identifying and characterizing a structural domain of protein disulfide isomerase

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Characterization of the active site cysteine residues of the thioredoxin-like domains of protein disulfide isomerase.

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12 December 2020