Calnexin, calreticulin, and ERp57 cooperate in disulfide bond formation in human CD1d heavy chain (Q40703013)

22 September 2017

title

Calnexin, calreticulin, and ERp57 cooperate in disulfide bond formation in human CD1d heavy chain (English)

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22 September 2017

Suk-Jo Kang

1

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22 September 2017

Peter Cresswell

series ordinal

2

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22 September 2017

language of work or name

English

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publication date

17 September 2002

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Journal of Biological Chemistry

22 September 2017

published in

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22 September 2017

volume

277

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22 September 2017

issue

47

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22 September 2017

page(s)

44838-44844

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The CD1 system: antigen-presenting molecules for T cell recognition of lipids and glycolipids

22 September 2017

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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An unstable beta 2-microglobulin: major histocompatibility complex class I heavy chain intermediate dissociates from calnexin and then is stabilized by binding peptide

21 January 2018

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21 January 2018

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The majority of H2-M3 is retained intracellularly in a peptide-receptive state and traffics to the cell surface in the presence of N-formylated peptides

21 January 2018

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21 January 2018

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Tapasin enhances peptide-induced expression of H2-M3 molecules, but is not required for the retention of open conformers

21 January 2018

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

21 January 2018

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Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M207831200

1 reference

22 September 2017

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