(Q38297618)

1 September 2017

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

1 reference

1 September 2017

1 reference

Stronge VS

1

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1 September 2017

Saito Y

series ordinal

2

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1 September 2017

Ihara Y

series ordinal

3

1 reference

1 September 2017

Williams DB

series ordinal

4

1 reference

1 September 2017

language of work or name

English

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publication date

20 August 2001

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Journal of Biological Chemistry

1 September 2017

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1 September 2017

276

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1 September 2017

43

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1 September 2017

39779-39787

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

1 September 2017

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107091200

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.M107091200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107091200

Association of folding intermediates of glycoproteins with calnexin during protein maturation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107091200

Folding of insulin receptor monomers is facilitated by the molecular chaperones calnexin and calreticulin and impaired by rapid dimerization

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107091200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107091200

Retention of unassembled components of integral membrane proteins by calnexin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107091200

Trimming and readdition of glucose to N-linked oligosaccharides determines calnexin association of a substrate glycoprotein in living cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107091200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107091200

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.M107091200

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.M107091200

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.M107091200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107091200

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.M107091200

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.M107091200

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.M107091200

BiP and PDI cooperate in the oxidative folding of antibodies in vitro

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107091200

Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107091200

The J-domain family and the recruitment of chaperone power

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107091200

The Hsp70 and Hsp60 chaperone machines

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107091200

Cooperation of the molecular chaperone Ydj1 with specific Hsp70 homologs to suppress protein aggregation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107091200

Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107091200

Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog, Hsp40.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107091200

The molecular chaperone Hsc70 assists the in vitro folding of the N-terminal nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107091200

Glycan-dependent and -independent association of vesicular stomatitis virus G protein with calnexin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107091200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107091200

Conformation-independent binding of monoglucosylated ribonuclease B to calnexin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107091200

Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107091200

Roles of molecular chaperones in cytoplasmic protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107091200

Assessment of the ATP binding properties of Hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107091200

Hsp90 & Co. - a holding for folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107091200

Chaperone selection during glycoprotein translocation into the endoplasmic reticulum.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107091200

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.M107091200

21 January 2018

Identifiers

DOI

10.1074/JBC.M107091200

1 reference

1 September 2017

1 reference