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Details on Person Unglycosylation at Asn-633 made extracellular domain of E-cadherin folded incorrectly and arrested in endoplasmic reticulum, then sequentially degraded by ERAD

Class:IdLiteratureReference:9816239
_displayNameUnglycosylation at Asn-633 made extracellular domain of E-cadherin folded incorrectly and arrested in endoplasmic reticulum, then sequentially degraded by ERAD
_timestamp2022-09-01 19:18:42
author[Person:5654821] Zhou, Feng
[Person:4088260] Su, Jianmin
[Person:9816228] Fu, Le
[Person:2252610] Yang, Yong
[Person:9816205] Zhang, Lineng
[Person:9816229] Wang, Liying
[Person:5660261] Zhao, Hongbo
[Person:9816207] Zhang, Diancai
[Person:9816238] Li, Zengxia
[Person:9625308] Zha, Xiliang
created[InstanceEdit:9816220] Orlic-Milacic, Marija, 2022-09-01
journalGlycoconj J
pages727-40
pubMedIdentifier18491227
titleUnglycosylation at Asn-633 made extracellular domain of E-cadherin folded incorrectly and arrested in endoplasmic reticulum, then sequentially degraded by ERAD
volume25
year2008
(literatureReference)[Summation:9932335]

CDH1 (E-cadherin) is N-glycosylated at asparagine residue...
[Summation:9932736] After MOGS (Glucosidase I) removes the first glucose residue...
[Summation:9932995] After Glucosidase II complex-mediated removal of the second ...
[Summation:9933300]

Upon processing in the endoplasmic reticulum (ER), pro-CD...
[Pathway:9768727] Regulation of CDH1 posttranslational processing and trafficking to plasma membrane [Homo sapiens]
[BlackBoxEvent:9816273] CDH1 translocates from ER to Golgi [Homo sapiens]
[BlackBoxEvent:9816276] CDH1 is N-glycosylated on asparagine residues in endoplasmic reticulum [Homo sapiens]
[BlackBoxEvent:9932988] CANX binds Glu1Man9GlcNAc2-CDH1 [Homo sapiens]

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