(Q40350567)

19 September 2017

title

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

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19 September 2017

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7

Werner Müller-Esterl

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19 September 2017

Virginie Martin

1

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19 September 2017

Jody Groenendyk

2

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19 September 2017

Simone S Steiner

3

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19 September 2017

Lei Guo

4

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19 September 2017

Monika Dabrowska

5

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19 September 2017

J M Robert Parker

6

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19 September 2017

Michal Opas

8

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19 September 2017

Marek Michalak

9

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19 September 2017

language of work or name

English

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publication date

16 November 2005

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Journal of Biological Chemistry

19 September 2017

published in

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19 September 2017

volume

281

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19 September 2017

issue

4

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19 September 2017

page(s)

2338-2346

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Quality control in the endoplasmic reticulum

19 September 2017

cites work

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https://api.crossref.org/works/10.1074%2FJBC.M508302200

Lectin control of protein folding and sorting in the secretory pathway

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M508302200

Association of folding intermediates of glycoproteins with calnexin during protein maturation

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M508302200

Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M508302200

The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M508302200

Calreticulin: one protein, one gene, many functions.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M508302200

NMR structure of the calreticulin P-domain

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M508302200

Ca2+ signaling and calcium binding chaperones of the endoplasmic reticulum

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M508302200

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

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M508302200

Functional specialization of calreticulin domains

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M508302200

Identification of an N-domain Histidine Essential for Chaperone Function in Calreticulin

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M508302200

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

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M508302200

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.M508302200

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.M508302200

Site-directed mutagenesis by overlap extension using the polymerase chain reaction

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508302200

Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M508302200

The conformation of calreticulin is influenced by the endoplasmic reticulum luminal environment.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M508302200

Ca2+ regulation of interactions between endoplasmic reticulum chaperones.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M508302200

Calreticulin differentially modulates calcium uptake and release in the endoplasmic reticulum and mitochondria.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M508302200

A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M508302200

Chaperone-like activity of tubulin. binding and reactivation of unfolded substrate enzymes.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M508302200

Specific interaction of ERp57 and calnexin determined by NMR spectroscopy and an ER two-hybrid system

21 January 2018

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Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M508302200

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.M508302200

Mutational analysis provides molecular insight into the carbohydrate-binding region of calreticulin: pivotal roles of tyrosine-109 and aspartate-135 in carbohydrate recognition.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508302200

Expression and Purification of Mammalian Calreticulin in Pichia pastoris

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508302200

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.M508302200

Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M508302200

21 January 2018

Identifiers

DOI

10.1074/JBC.M508302200

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19 September 2017

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