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Details on Person After the middle glucose residue is removed by Glucosidase I...

Class:IdSummation:9976429
_displayNameAfter the middle glucose residue is removed by Glucosidase I...
_timestamp2026-01-20 15:37:42
created[InstanceEdit:9976430] Orlic-Milacic, Marija, 2025-12-11
literatureReference[LiteratureReference:9821544] Processing of the rough endoplasmic reticulum membrane glycoproteins of rotavirus SA11
[LiteratureReference:9976421] The molecular chaperone calnexin interacts with the NSP4 enterotoxin of rotavirus in vivo and in vitro
[LiteratureReference:9932574] Roles of N-linked glycans in the endoplasmic reticulum
modified[InstanceEdit:9979650] Orlic-Milacic, Marija, 2026-01-20
textAfter the middle glucose residue is removed by Glucosidase II, the monoglucosylated (Glu1Man9GlcNAc2) glycoprotein binds to chaperones calnexin (CANX) and/or calreticulin (CALR), and is released from the chaperones after the removal of the innermost glucose residue by Glucosidase II, which generates a Man9GlcNAc2 glycan (reviewed in Helenius and Aebi 2004). Both NSP4 products of rotavirus A (RV-A) expected to be generated by Glucosidase II, Glu1Man9GlcNAc2-NSP4 and Man9GlcNAc2-NSP4, are detectable by pulse-chase chromatography (Kabcenell and Atkinson 1985: simian RV-A strain SA11 was used), and the release of Man9GlcNAc2-NSP4 from CANX is prevented by castanospermin, an inhibitor of glucosidase I and glucosidase II (Mirazimi et al. 1998: SA11 was used).
(summation)[BlackBoxEvent:9976268] Glucosidase II removes glucose residue from Glu1Man9GlucNAc2-NSP4 [Homo sapiens]
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