Dislocation of an endoplasmic reticulum membrane glycoprotein involves the formation of partially dislocated ubiquitinated polypeptides. (Q53790105)

19 May 2018

title

Dislocation of an endoplasmic reticulum membrane glycoprotein involves the formation of partially dislocated ubiquitinated polypeptides. (English)

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19 May 2018

main subject

endoplasmic reticulum

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protein ubiquitination

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19 May 2018

author name string

Brooke M Baker

series ordinal

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19 May 2018

language of work or name

English

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publication date

23 July 2007

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19 May 2018

Journal of Biological Chemistry

published in

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19 May 2018

volume

282

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19 May 2018

issue

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19 May 2018

page(s)

26845-26856

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19 May 2018

Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control

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21 January 2018

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21 January 2018

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Proteasome subunit Rpn1 binds ubiquitin-like protein domains

21 January 2018

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Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis.

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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Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome

21 January 2018

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21 January 2018

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Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress

21 January 2018

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The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway

21 January 2018

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21 January 2018

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21 January 2018

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Novel aspects of degradation of T cell receptor subunits from the endoplasmic reticulum (ER) in T cells: importance of oligosaccharide processing, ubiquitination, and proteasome-dependent removal from ER membranes

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M704315200

1 reference

19 May 2018

1 reference

19 May 2018