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Details on Person After Glucosidase II complex-mediated removal of the second ...

Class:IdSummation:9976321
_displayNameAfter Glucosidase II complex-mediated removal of the second ...
_timestamp2025-12-11 12:43:19
created[InstanceEdit:9976320] Orlic-Milacic, Marija, 2025-12-10
literatureReference[LiteratureReference:9932574] Roles of N-linked glycans in the endoplasmic reticulum
[LiteratureReference:9976315] Endoplasmic reticulum chaperones are involved in the morphogenesis of rotavirus infectious particles
[LiteratureReference:9976432] Targeting of endoplasmic reticulum-associated proteins to axons and dendrites in rotavirus-infected neurons
modified[InstanceEdit:9976436] Orlic-Milacic, Marija, 2025-12-11
textAfter Glucosidase II complex-mediated removal of the second glucose residue, the Glu1Man9GlcNAc2-proteoglycans enter the so-called calnexin/calreticulin cycle, binding to chaperones CANX (calnexin) (membrane-bound glycoproteins) or CALR (calreticulin) (soluble glycoproteins), which ensure proper folding of nascent glycoproteins (reviewed in Helenius and Aebi 2004). While binding of rotavirus A (RV-A) VP7 to CANX has not been demonstrated, CANX is required for proper maturation of VP7, while CALR is not (Maruri-Avidal et al. 2008: simian RV-A strain RRV was used). In rat neurons infected with RRV, VP7 co-localizes with CANX (Weclewicz et al. 1998).
(summation)[BlackBoxEvent:9976263] CANX binds Glu1Man9GlcNAc2-VP7 [Homo sapiens]
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