Mutational analysis of the oxidoreductase ERp57 reveals the importance of the two central residues in the redox motif (Q46974692)

27 December 2017

title

Mutational analysis of the oxidoreductase ERp57 reveals the importance of the two central residues in the redox motif (English)

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27 December 2017

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2

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27 December 2017

Simon J Powis

series ordinal

3

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27 December 2017

Siân Beynon-Jones

series ordinal

1

object named as

Siân M Beynon-Jones

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27 December 2017

language of work or name

English

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publication date

28 February 2006

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27 December 2017

published in

FEBS Letters

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27 December 2017

volume

580

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27 December 2017

page(s)

1897-1902

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27 December 2017

issue

7

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27 December 2017

Identification and characterization of structural domains of human ERp57: association with calreticulin requires several domains

cites work

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.02.055

Molecular cloning of the human glucose-regulated protein ERp57/GRP58, a thiol-dependent reductase. Identification of its secretory form and inducible expression by the oncogenic transformation

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.02.055

The oxidoreductase ERp57 efficiently reduces partially folded in preference to fully folded MHC class I molecules

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.02.055

Functional differences in yeast protein disulfide isomerases

21 January 2018

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.02.055

A conserved arginine plays a role in the catalytic cycle of the protein disulphide isomerases.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.02.055

A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.02.055

ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.02.055

The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.02.055

Impaired assembly of the major histocompatibility complex class I peptide-loading complex in mice deficient in the oxidoreductase ERp57

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.02.055

Formation of HLA-B27 homodimers and their relationship to assembly kinetics

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.02.055

Characterization of the ERp57-Tapasin complex by rapid cellular acidification and thiol modification

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.02.055

Disulfide bond isomerization and the assembly of MHC class I-peptide complexes

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.02.055

Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.02.055

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.02.055

Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active-site cysteine

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.02.055

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

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.02.055

ERp57 is a multifunctional thiol-disulfide oxidoreductase

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.02.055

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.02.055

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

21 January 2018

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Why is DsbA such an oxidizing disulfide catalyst?

21 January 2018

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.02.055

Glutathione directly reduces an oxidoreductase in the endoplasmic reticulum of mammalian cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.02.055

10.1016/J.FEBSLET.2006.02.055

21 January 2018

Identifiers

DOI

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27 December 2017

PubMed ID

16516209

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27 December 2017