(Q40703743)

English

Identification of specific glycoforms of major histocompatibility complex class I heavy chains suggests that class I peptide loading is an adaptation of the quality control pathway involving calreticulin and ERp57.

scientific article published on 15 September 2002

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scholarly article

1 reference

Europe PubMed Central

22 September 2017

Identification of specific glycoforms of major histocompatibility complex class I heavy chains suggests that class I peptide loading is an adaptation of the quality control pathway involving calreticulin and ERp57. (English)

1 reference

Europe PubMed Central

22 September 2017

quality control

0 references

author name string

Catherine M Radcliffe

1

1 reference

Europe PubMed Central

22 September 2017

Gundo Diedrich

2

1 reference

Europe PubMed Central

22 September 2017

David J Harvey

3

1 reference

Europe PubMed Central

22 September 2017

Raymond A Dwek

4

1 reference

Europe PubMed Central

22 September 2017

Peter Cresswell

5

1 reference

Europe PubMed Central

22 September 2017

Pauline M Rudd

6

1 reference

Europe PubMed Central

22 September 2017

language of work or name

0 references

publication date

15 September 2002

1 reference

Europe PubMed Central

22 September 2017

number of pages

9

1 reference

based on heuristic

inferred from page(s)

Journal of Biological Chemistry

1 reference

Europe PubMed Central

22 September 2017

277

1 reference

Europe PubMed Central

22 September 2017

48

1 reference

Europe PubMed Central

22 September 2017

46415-46423

1 reference

Europe PubMed Central

22 September 2017

Mechanisms of MHC class I--restricted antigen processing

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

The role of ERp57 in disulfide bond formation during the assembly of major histocompatibility complex class I in a synchronized semipermeabilized cell translation system

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

Species-specific differences in chaperone interaction of human and mouse major histocompatibility complex class I molecules

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

Disulfide bond isomerization and the assembly of MHC class I-peptide complexes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

Discrete proteolytic intermediates in the MHC class I antigen processing pathway and MHC I-dependent peptide trimming in the ER.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

Intracellular functions of N-linked glycans

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

MHC class I molecules form ternary complexes with calnexin and TAP and undergo peptide-regulated interaction with TAP via their extracellular domains

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

A role for calnexin in the assembly of the MHC class I loading complex in the endoplasmic reticulum

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

Functional expression and purification of the ABC transporter complex associated with antigen processing (TAP) in insect cells

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

Sequencing of N-linked oligosaccharides directly from protein gels: in-gel deglycosylation followed by matrix-assisted laser desorption/ionization mass spectrometry and normal-phase high-performance liquid chromatography

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

Kinetics and the mechanism of interaction of the endoplasmic reticulum chaperone, calreticulin, with monoglucosylated (Glc1Man9GlcNAc2) substrate

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

Soluble tapasin restores MHC class I expression and function in the tapasin-negative cell line .220.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

Assembly of asparagine-linked oligosaccharides

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

Setting the standards: quality control in the secretory pathway

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

Direct binding of peptide to empty MHC class I molecules on intact cells and in vitro.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

Peptide-induced stabilization and intracellular localization of empty HLA class I complexes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

The role of the lectin calnexin in conformation independent binding to N-linked glycoproteins and quality control.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

A rapid high-resolution high-performance liquid chromatographic method for separating glycan mixtures and analyzing oligosaccharide profiles

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M202466200

21 January 2018

Identifiers

10.1074/JBC.M202466200

1 reference

Europe PubMed Central

22 September 2017

1 reference

Europe PubMed Central

22 September 2017

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