(Q34199026)

31 July 2017

title

Functional characterization of ERp18, a new endoplasmic reticulum-located thioredoxin superfamily member (English)

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31 July 2017

main subject

endoplasmic reticulum

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author name string

Heli I Alanen

1

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31 July 2017

Richard A Williamson

2

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31 July 2017

Mark J Howard

3

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31 July 2017

Anna-Kaisa Lappi

4

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31 July 2017

Heli P Jäntti

5

1 reference

31 July 2017

Sini M Rautio

6

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31 July 2017

Sakari Kellokumpu

7

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31 July 2017

Lloyd W Ruddock

8

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31 July 2017

language of work or name

English

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publication date

21 May 2003

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Journal of Biological Chemistry

31 July 2017

published in

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31 July 2017

volume

278

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31 July 2017

issue

31

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31 July 2017

page(s)

28912-28920

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The formation of protein disulphide bonds

31 July 2017

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The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum

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Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum

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Yeast flavin-containing monooxygenase generates oxidizing equivalents that control protein folding in the endoplasmic reticulum

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A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation

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Eps1, a novel PDI-related protein involved in ER quality control in yeast

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The protein disulphide-isomerase family: unravelling a string of folds

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Protein disulfide isomerases exploit synergy between catalytic and specific binding domains

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ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family

21 January 2018

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ERp28, a human endoplasmic-reticulum-lumenal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin-box motif

21 January 2018

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Identification of ERp29, an endoplasmic reticulum lumenal protein, as a new member of the thyroglobulin folding complex

21 January 2018

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pH-dependence of the dithiol-oxidizing activity of DsbA (a periplasmic protein thiol:disulphide oxidoreductase) and protein disulphide-isomerase: studies with a novel simple peptide substrate

21 January 2018

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21 January 2018

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21 January 2018

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Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria

21 January 2018

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

21 January 2018

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Structure of TcpG, the DsbA protein folding catalyst from Vibrio cholerae

21 January 2018

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High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin

21 January 2018

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21 January 2018

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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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Proton-transfer effects in the active-site region of Escherichia coli thioredoxin using two-dimensional 1H NMR.

21 January 2018

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Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability.

21 January 2018

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Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M304598200

1 reference

31 July 2017

1 reference