(Q38344871)

2 September 2017

title

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

1 reference

2 September 2017

main subject

endoplasmic reticulum

0 references

author

Stephen High

10

1 reference

2 September 2017

9

Johanna Myllyharju

1 reference

2 September 2017

Sarah J Russell

1

1 reference

2 September 2017

Lloyd W Ruddock

2

1 reference

2 September 2017

Kirsi E H Salo

3

1 reference

2 September 2017

Jason D Oliver

4

1 reference

2 September 2017

Quentin P Roebuck

5

1 reference

2 September 2017

David H Llewellyn

6

1 reference

2 September 2017

H Llewelyn Roderick

7

1 reference

2 September 2017

Peppi Koivunen

8

1 reference

2 September 2017

language of work or name

English

0 references

publication date

10 February 2004

1 reference

Journal of Biological Chemistry

2 September 2017

published in

1 reference

2 September 2017

volume

279

1 reference

2 September 2017

issue

18

1 reference

2 September 2017

page(s)

18861-18869

1 reference

Glycoprotein folding in the endoplasmic reticulum: a tale of three chaperones?

2 September 2017

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400575200

Intracellular functions of N-linked glycans

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400575200

The lectin chaperone calnexin utilizes polypeptide-based interactions to associate with many of its substrates in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400575200

Lectin-deficient calnexin is capable of binding class I histocompatibility molecules in vivo and preventing their degradation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400575200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400575200

NMR structure of the calreticulin P-domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400575200

NMR structures of 36 and 73-residue fragments of the calreticulin P-domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400575200

The Structure of calnexin, an ER chaperone involved in quality control of protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400575200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400575200

Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400575200

Protein disulfide isomerases exploit synergy between catalytic and specific binding domains

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400575200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400575200

Mutations that destabilize the a' domain of human protein-disulfide isomerase indirectly affect peptide binding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400575200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400575200

Domains b' and a' of protein disulfide isomerase fulfill the minimum requirement for function as a subunit of prolyl 4-hydroxylase. The N-terminal domains a and b enhances this function and can be substituted in part by those of ERp57.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400575200

Defining the domain boundaries of the human protein disulfide isomerases.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400575200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400575200

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/10.1074%2FJBC.M400575200

Ca2+ regulation of interactions between endoplasmic reticulum chaperones.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400575200

Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400575200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400575200

Lectin control of protein folding and sorting in the secretory pathway

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400575200

Nuclear localisation of calreticulin in vivo is enhanced by its interaction with glucocorticoid receptors

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400575200

Enhanced Catalysis of Ribonuclease B Folding by the Interaction of Calnexin or Calreticulin with ERp57

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400575200

Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400575200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400575200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M400575200

21 January 2018

Identifiers

DOI

10.1074/JBC.M400575200

1 reference

2 September 2017

1 reference