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Keywords: ER-associated degradation
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Journal Articles
J Cell Sci (2017) 130 (19): 3322–3335.
Published: 01 October 2017
... during the ubiquitin–proteasome-dependent process of ER-associated degradation (ERAD). Hrd1 associates with cofactors to execute ERAD, but their roles and how they assemble with Hrd1 are not well understood. Here, we identify crucial cofactor interaction domains within Hrd1 and report a previously...
Includes: Supplementary data
Journal Articles
J Cell Sci (2015) 128 (22): 4112–4125.
Published: 15 November 2015
...Kit Briant; Yee-Hui Koay; Yuka Otsuka; Eileithyia Swanton ABSTRACT Clearance of misfolded proteins from the endoplasmic reticulum (ER) is mediated by the ubiquitin-proteasome system in a process known as ER-associated degradation (ERAD). The mechanisms through which proteins containing aberrant...
Includes: Supplementary data
Journal Articles
J Cell Sci (2014) 127 (6): 1214–1228.
Published: 15 March 2014
... synthesis with LD assembly. The formation of the Fld1–Ldb16 complex involves putative transmembrane segments of both proteins, thus, directly contributing to the maintenance of LD morphology. The stability of Ldb16 requires Fld1, as Ldb16 is subjected to ER-associated degradation (ERAD) in the absence...
Includes: Supplementary data
Journal Articles
J Cell Sci (2012) 125 (12): 2930–2939.
Published: 15 June 2012
... called ER-associated degradation (ERAD) ( Römisch, 2006 ). During ERAD, Ubx2 functions to bridge the cytosolic Cdc48–Npl4–Ufd1 complex and the membrane-associated Hrd1–Hrd3 and Ssm4 ubiquitin ligase complexes using its N-terminal ubiquitin-associated (UBA) domain to recognize the ubiquitylated ERAD...
Includes: Supplementary data
Journal Articles
J Cell Sci (2009) 122 (21): 3942–3953.
Published: 01 November 2009
... ( lisa.swanton@manchester.ac.uk ) 1 9 2009 © The Company of Biologists Limited 2009 2009 ER-associated degradation ER stress Pelizaeus-Merzbacher disease Protein misfolding Unfolded protein response A number of clinically important human diseases are known to be caused by protein...
Includes: Supplementary data
Journal Articles
J Cell Sci (2009) 122 (9): 1374–1381.
Published: 01 May 2009
...Zlatka Kostova; Jennifer Mariano; Simone Scholz; Carolin Koenig; Allan M. Weissman Cue1p is an N-terminally anchored endoplasmic reticulum (ER) protein essential for the activity of the two major yeast RING finger ubiquitin ligases (E3s) implicated in ER-associated degradation (ERAD). Cue1p...
Includes: Supplementary data
Journal Articles
J Cell Sci (2006) 119 (21): 4373–4380.
Published: 01 November 2006
... chaperone system is regulated by de-/re-glucosylation cycles catalyzed by GII and UGT1; and how acceleration of N -glycan dismantling upon induction of EDEM variants promotes ER-associated degradation (ERAD) under conditions of ER stress. In particular, characterization of cells lacking certain ER...
Journal Articles
J Cell Sci (2006) 119 (2): 303–313.
Published: 15 January 2006
... ER-associated degradation substrate with 12 transmembrane segments. In the presence of ATP, cytosol and fully active proteasomes, CFTR was rapidly degraded and released into the cytosol solely in the form of trichloroacetic acid (TCA)-soluble peptide fragments. Inhibition of proteasome β subunits...
Journal Articles
J Cell Sci (2005) 118 (7): 1485–1492.
Published: 01 April 2005
...Zlatka Kostova; Dieter H. Wolf In the endoplasmic reticulum (ER), N -linked glycans (N-glycans) function as signals to recruit the lectin chaperones involved in protein folding, quality control and ER-associated degradation. We undertook a systematic study of the four N-glycans of mutated...