(Q28260805)

1

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Richard A Williamson

2

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Mark J Howard

3

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Feras S Hatahet

4

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Kirsi E H Salo

5

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Annika Kauppila

6

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Sakari Kellokumpu

7

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Lloyd W Ruddock

Journal of Biological Chemistry

8

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language of work or name

English

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publication date

3 November 2006

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published in

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volume

281

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issue

44

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page(s)

33727-38

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cites work

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Biochemical basis of oxidative 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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Inter-Domain Redox Communication in Flavoenzymes of the Quiescin/Sulfhydryl Oxidase Family: Role of a Thioredoxin Domain in Disulfide Bond Formation,

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Protein disulfide isomerase

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The human protein disulphide isomerase family: substrate interactions and functional properties

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A major fraction of endoplasmic reticulum-located glutathione is present as mixed disulfides with protein

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Functional differences in yeast protein disulfide isomerases

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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

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Crystal structure and functional analysis of Drosophila Wind, a protein-disulfide isomerase-related protein

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Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase

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The primary substrate binding site in the b' domain of ERp57 is adapted for endoplasmic reticulum lectin association

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TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain

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Identification by mutational analysis of amino acid residues essential in the chaperone function of calreticulin

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Defining the domain boundaries of the human protein disulfide isomerases.

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

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Capturing protein interactions in the secretory pathway of living cells

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Reducing the environmental sensitivity of yellow fluorescent protein. Mechanism and applications

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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

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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

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Predicting subcellular localization of proteins based on their N-terminal amino acid sequence

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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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Thioredoxin--a fold for all reasons

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

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Molecular characterization of a pancreas-specific protein disulfide isomerase, PDIp

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ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin

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Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins

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ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress

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EndoPDI, a novel protein-disulfide isomerase-like protein that is preferentially expressed in endothelial cells acts as a stress survival factor

21 January 2018

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

21 January 2018

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Tapasin and other chaperones: models of the MHC class I loading complex.

21 January 2018

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The optimization of peptide cargo bound to MHC class I molecules by the peptide-loading complex

21 January 2018

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Cellular functions of endoplasmic reticulum chaperones calreticulin, calnexin, and ERp57.

21 January 2018

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Quality control in the endoplasmic reticulum

21 January 2018

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Three binding sites in protein-disulfide isomerase cooperate in collagen prolyl 4-hydroxylase tetramer assembly.

21 January 2018

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

21 January 2018

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