ライフサイエンスコーパス: glucosidase II

1 nd the beta subunit of endoplasmic reticulum glucosidase II.

2 ts to be the functional catalytic subunit of glucosidase II.

3 by the action of endomannosidase rather than glucosidase II.

4 protein tyrosine phosphatase 1B (PTP1B), and glucosidase II.

5 ctivity, but the role of the beta subunit in glucosidase II activity has not been established.

6 s, demonstrating that it is not required for glucosidase II activity in vitro.

7 Plants with down-regulated glucosidase II activity showed a greater degree of plasm

8 Ac2 as a substrate, it was demonstrated that glucosidase II activity was markedly down-regulated in m

9 chizosaccharomices pombe drastically reduces glucosidase II activity, but the role of the beta subuni

10 letion of its homologue in yeast obliterates glucosidase II activity.

11 etail, strongly suggesting that MAL1 encodes glucosidase II activity.

12 on, levels of normal hepatocystin and of the glucosidase II alpha subunit are substantially reduced i

13 is mutant protein fails to assemble with the glucosidase II alpha subunit.

14 asmic reticulum, where it assembles with the glucosidase II alpha subunit.

15 structures of the main ERQC enzyme, ER alpha-glucosidase II (alpha-GluII; from mouse), alone and in c

16 unctions as the noncatalytic beta subunit of Glucosidase II, an endoplasmic reticulum (ER)-resident e

17 ions in PRKCSH, encoding the beta-subunit of glucosidase II, an N-linked glycan-processing enzyme in

18 nd yeast strains defective in glucosidase I, glucosidase II and BiP/Kar2p, it was demonstrated that c

19 ng and release are regulated by two enzymes, glucosidase II and UDP-Glc:glycoprotein:glycosyltransfer

20 (Ustilago maydis), glucosidase I (Gls1) and glucosidase II beta-subunit (Gas2), are essential for it

21 We have recently proposed that glucosidase II consisted of two different subunits, alph

22 ponse to the posttranslational inhibition of glucosidase II, demonstrating that the attenuated remova

23 We isolated enzymatically active glucosidase II from rat liver and found that, in contras

24 and genetic approaches, we demonstrate that glucosidase II (GII) mediates glycan trimming of TRPP2.

25 resent in a protein with enzymatic activity, glucosidase II (GII).

26 The non-catalytic beta subunit of glucosidase II (GIIbeta) is encoded by PRKCSH, one of th

27 sylation of N-glycans, and oppositely acting glucosidase II (GlucII), and that vIL-6 can promote prot

28 ycoprotein glucosyltransferase 1 (UGGT1) and glucosidase II (GlucII).

29 In S.cerevisiae, glucosidase II is encoded by the GLS2 gene, and glucosid

30 calization and sequence relatedness to alpha-glucosidase II, MYORG has never been shown to exhibit ca

31 similar to the glycoprotein-processing alpha-glucosidase II of mammalian and yeast origin than to oth

32 We conclude that the catalytic core of glucosidase II resides in a globular domain of the alpha

33 ycosidase F or removal of the glucoses by ER glucosidase II resulted in dissociation of the complexes

34 with a missense mutation in GANAB, encoding glucosidase II subunit alpha (GIIalpha).

35 , like the other mammalian GH31 enzyme alpha-glucosidase II, this enzyme is found in the lumen of the

36 rate 80K-H" or "noncatalytic beta-subunit of glucosidase II." This protein is highly conserved, is ex

37 y becomes accessible for processing by alpha-glucosidase II upon loading of optimal epitopes.