The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules (Q57077650)

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2 November 2019

title

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

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2 November 2019

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4

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2 November 2019

author name string

J Kemmink

1

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2 November 2019

N J Darby

2

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2 November 2019

K Dijkstra

3

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2 November 2019

T E Creighton

5

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2 November 2019

language of work or name

English

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publication date

1 April 1997

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2 November 2019

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2 November 2019

volume

7

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2 November 2019

issue

4

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2 November 2019

page(s)

239-245

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

2 November 2019

cites work

1 reference

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7 January 2021

Thioredoxin--a fold for all reasons

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7 January 2021

Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide

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7 January 2021

On the reactivity and ionization of the active site cysteine residues of Escherichia coli thioredoxin.

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7 January 2021

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

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7 January 2021

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

1 reference

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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

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7 January 2021

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

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7 January 2021

Identifying and characterizing a structural domain of protein disulfide isomerase

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7 January 2021

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

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7 January 2021

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

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7 January 2021

Protein fold recognition using sequence-derived predictions

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7 January 2021

The multiplicity of domains in proteins

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7 January 2021

Intron position as an evolutionary marker of thioredoxins and thioredoxin domains.

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7 January 2021

Crystal structure of thioredoxin-2 from Anabaena

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7 January 2021

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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7 January 2021

The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase

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7 January 2021

The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution

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7 January 2021

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

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7 January 2021

Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins.

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7 January 2021

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

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7 January 2021

Stereospecific assignment of beta-methylene protons in larger proteins using 3D 15N-separated Hartmann-Hahn and 13C-separated rotating frame Overhauser spectroscopy.

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7 January 2021

Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations

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7 January 2021

A simple method for delineating well-defined and variable regions in protein structures determined from interproton distance data

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7 January 2021

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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7 January 2021

Protein structure comparison by alignment of distance matrices

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7 January 2021

10.1016/S0960-9822(06)00119-9

Identifiers

DOI

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9094311%20AND%20SRC:MED&resulttype=core&format=json

2 November 2019

1 reference