(Q28203094)

1

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Myrna F Cohen-Doyle

2

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David Y Thomas

3

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David B Williams

Journal of Biological Chemistry

4

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language of work or name

English

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publication date

16 August 2002

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published in

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volume

277

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issue

33

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page(s)

29686-97

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cites work

Calnexin: a membrane-bound chaperone of the endoplasmic reticulum

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202405200

Protein glucosylation and its role in protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202405200

Lectins as chaperones in glycoprotein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202405200

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/10.1074%2FJBC.M202405200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202405200

Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202405200

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/10.1074%2FJBC.M202405200

Calreticulin, a peptide-binding chaperone of the endoplasmic reticulum, elicits tumor- and peptide-specific immunity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202405200

Polypeptide binding properties of the chaperone calreticulin.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202405200

Inhibition of glucose trimming with castanospermine reduces calnexin association and promotes proteasome degradation of the alpha-subunit of the nicotinic acetylcholine receptor

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202405200

Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202405200

P-glycoprotein. Associations between domains and between domains and molecular chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202405200

Differential interaction of coagulation factor VIII and factor V with protein chaperones calnexin and calreticulin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202405200

Retention of unassembled components of integral membrane proteins by calnexin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202405200

Calnexin associates exclusively with individual CD3 delta and T cell antigen receptor (TCR) alpha proteins containing incompletely trimmed glycans that are not assembled into multisubunit TCR complexes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202405200

Identification of novel peptide binding proteins in the endoplasmic reticulum: ERp72, calnexin, and grp170.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202405200

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.M202405200

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

21 January 2018

1 reference

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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.M202405200

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.M202405200

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/10.1074%2FJBC.M202405200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202405200

Ca2+ regulation of interactions between endoplasmic reticulum chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202405200

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.M202405200

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.M202405200

NMR structure of the calreticulin P-domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202405200

Human, mouse, and rat calnexin cDNA cloning: identification of potential calcium binding motifs and gene localization to human chromosome 5

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202405200

The Hsp70 and Hsp60 chaperone machines

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202405200

Structural analysis of substrate binding by the molecular chaperone DnaK

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202405200

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.M202405200

21 January 2018

Identifiers

DOI

10.1074/JBC.M202405200

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

12052826

1 reference

Consolidated OpenCitations Corpus – April 2017