(Q38328572)

2 September 2017

title

In vitro and in vivo assays to assess the functions of calnexin and calreticulin in ER protein folding and quality control (English)

1 reference

2 September 2017

0 references

0 references

Marie-Eve Paquet

1

1 reference

2 September 2017

Michael R Leach

series ordinal

2

1 reference

2 September 2017

David B Williams

series ordinal

3

1 reference

2 September 2017

publication date

1 April 2005

1 reference

2 September 2017

1 reference

2 September 2017

volume

35

1 reference

2 September 2017

issue

4

1 reference

2 September 2017

page(s)

338-347

1 reference

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

2 September 2017

cites work

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

Efficient dissociation of the p88 chaperone from major histocompatibility complex class I molecules requires both beta 2-microglobulin and peptide

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

Association of folding intermediates of glycoproteins with calnexin during protein maturation

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

Folding and oligomerization of influenza hemagglutinin in the ER and the intermediate compartment.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

Functional relationship between calreticulin, calnexin, and the endoplasmic reticulum luminal domain of calnexin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

Role of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradation

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, IP90).

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

Calnexin Fails to Associate with Substrate Proteins in Glucosidase-deficient Cell Lines

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

NMR structure of the calreticulin P-domain

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

Ca2+ regulation of interactions between endoplasmic reticulum chaperones.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

Conformational changes induced in the endoplasmic reticulum luminal domain of calnexin by Mg-ATP and Ca2+.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

Identification and crystallization of a protease-resistant core of calnexin that retains biological activity.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

Histone accessibility determined by lysine-specific acetylation in chicken erythrocyte nuclei

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

Calreticulin recognizes misfolded HLA-A2 heavy chains

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

Relationship between calnexin and BiP in suppressing aggregation and promoting refolding of protein and glycoprotein substrates

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

The N-glycans of jack bean alpha-mannosidase. Structure, topology and function

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

GroE facilitates refolding of citrate synthase by suppressing aggregation

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

Folding of VSV G protein: sequential interaction with BiP and calnexin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

Chaperones and folding of MHC class I molecules in the endoplasmic reticulum

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

Calnexin recognizes carbohydrate and protein determinants of class I major histocompatibility complex molecules

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

Calnexin expression does not enhance the generation of MHC class I-peptide complexes

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

Calnexin Influences Folding of Human Class I Histocompatibility Proteins but Not Their Assembly with β2-Microglobulin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2004.10.005

10.1016/J.YMETH.2004.10.005

7 January 2021

Identifiers

DOI

1 reference

2 September 2017

1 reference