(Q24317861)

GOA release 2020-03-11

author name string

Yongwang Zhong

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Hang Shen

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Ye Wang

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Yili Yang

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Peixin Yang

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Shengyun Fang

Biochemical and Biophysical Research Communications

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language of work or name

English

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publication date

6 March 2015

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published in

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volume

458

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issue

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page(s)

424-8

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cites work

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Key steps in ERAD of luminal ER proteins reconstituted with purified components

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

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Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradation

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Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity of polyglutamine-expanded huntingtin

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OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD

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Defining human ERAD networks through an integrative mapping strategy

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A high-coverage shRNA screen identifies TMEM129 as an E3 ligase involved in ER-associated protein degradation

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One step at a time: endoplasmic reticulum-associated degradation

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The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site

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Previously unknown role for the ubiquitin ligase Ubr1 in endoplasmic reticulum-associated protein degradation

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TMEM129 is a Derlin-1 associated ERAD E3 ligase essential for virus-induced degradation of MHC-I.

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