Calreticulin promotes folding of functional human leukocyte antigen class I molecules in vitro (Q40502090)

21 September 2017

Calreticulin promotes folding of functional human leukocyte antigen class I molecules in vitro (English)

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21 September 2017

Slobodan Culina

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21 September 2017

Grégoire Lauvau

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2

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21 September 2017

Brigitte Gubler

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3

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21 September 2017

Peter M van Endert

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4

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21 September 2017

language of work or name

English

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publication date

19 October 2004

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Journal of Biological Chemistry

21 September 2017

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21 September 2017

279

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21 September 2017

52

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21 September 2017

54210-54215

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The nature of the MHC class I peptide loading complex

21 September 2017

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https://api.crossref.org/works/10.1074%2FJBC.M410841200

Setting the standards: quality control in the secretory pathway

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M410841200

Getting newly synthesized proteins into shape.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M410841200

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

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M410841200

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

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M410841200

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

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M410841200

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

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M410841200

Role of calnexin in the glycan-independent quality control of proteolipid protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410841200

Major histocompatibility complex class I molecules expressed with monoglucosylated N-linked glycans bind calreticulin independently of their assembly status

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410841200

Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410841200

Deglucosylation of N-linked glycans is an important step in the dissociation of calreticulin-class I-TAP complexes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410841200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410841200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410841200

Molecular chaperones in antigen presentation

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M410841200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410841200

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

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M410841200

Optimization of the MHC class I peptide cargo is dependent on tapasin

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M410841200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410841200

Tapasin enhances MHC class I peptide presentation according to peptide half-life

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410841200

The N-terminal region of tapasin is required to stabilize the MHC class I loading complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410841200

Calreticulin recognizes misfolded HLA-A2 heavy chains

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M410841200

Tapasin enhances assembly of transporters associated with antigen processing-dependent and -independent peptides with HLA-A2 and HLA-B27 expressed in insect cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410841200

Peptide binding to the most frequent HLA-A class I alleles measured by quantitative molecular binding assays

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410841200

Ca2+ regulation of interactions between endoplasmic reticulum chaperones.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410841200

Human transporters associated with antigen processing (TAPs) select epitope precursor peptides for processing in the endoplasmic reticulum and presentation to T cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410841200

HLA-A- and HLA-B-specific monoclonal antibodies reactive with free heavy chains in western blots, in formalin-fixed, paraffin-embedded tissue sections and in cryo-immuno-electron microscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410841200

In vivo and in vitro formation and dissociation of HLA-DR complexes with invariant chain-derived peptides

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410841200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410841200

Expression of a single-chain HLA class I molecule in a human cell line: presentation of exogenous peptide and processed antigen to cytotoxic T lymphocytes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410841200

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.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410841200

Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410841200

21 January 2018

Identifiers

DOI

10.1074/JBC.M410841200

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21 September 2017

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