P-domain and lectin site are involved in the chaperone function of Saccharomyces cerevisiae calnexin homologue (Q38338969)

2 September 2017

title

P-domain and lectin site are involved in the chaperone function of Saccharomyces cerevisiae calnexin homologue (English)

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2 September 2017

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Saccharomyces cerevisiae

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Xiaohua Xu

1

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2 September 2017

Hiroyuki Azakami

series ordinal

2

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2 September 2017

Akio Kato

series ordinal

3

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2 September 2017

language of work or name

English

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publication date

1 July 2004

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2 September 2017

number of pages

6

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based on heuristic

inferred from page(s)

published in

FEBS Letters

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2 September 2017

volume

570

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2 September 2017

issue

1-3

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2 September 2017

page(s)

155-160

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Setting the standards: quality control in the secretory pathway

2 September 2017

cites work

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.06.039

Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.06.039

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.06.039

Expression and characterization of Saccharomyces cerevisiae Cne1p, a calnexin homologue

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.06.039

Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.06.039

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.06.039

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.06.039

Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.06.039

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.06.039

The Merck Frosst Award Lecture 1994/La conference Merck Frosst 1994. Calnexin: a molecular chaperone with a taste for carbohydrate

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.06.039

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/10.1016%2FJ.FEBSLET.2004.06.039

Structural organization of procaryotic and eucaryotic Hsp90. Influence of divalent cations on structure and function.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.06.039

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.06.039

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.06.039

10.1016/J.FEBSLET.2004.06.039

21 January 2018

Identifiers

DOI

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release_qj55vny63rbcblciqerlfrihni

2 September 2017

Fatcat ID

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Fatcat

https://api.fatcat.wiki/v0/release/qj55vny63rbcblciqerlfrihni

mapped directly with Wikidata item

24 November 2022

based on heuristic

1 reference