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1 N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase).
2 , BgaA, a beta-galactosidase, and StrH, an N-acetylglucosaminidase.
3 pecificity expected of the processing beta-N-acetylglucosaminidase.
4 cture used to confirm that SleL acts as an N-acetylglucosaminidase.
5 trated that ACS activity co-localized with N-acetylglucosaminidase.
6 c hydrolases, a chitodextrinase and a beta-N-acetylglucosaminidase.
7 tic transglycosylases but rather as a beta-N-acetylglucosaminidase.
8 ve cloned the cDNA and gene encoding alpha-N-acetylglucosaminidase.
9 ases but also contains a subfamily of beta-N-acetylglucosaminidases.
11 utation in the gene (NAGLU) encoding alpha-N-acetylglucosaminidase, a lysosomal enzyme required for t
12 that the satellites are the products of an N-acetylglucosaminidase activity that differs from the atl
13 genous levels of specific, processing beta-N-acetylglucosaminidase activity were significantly reduce
14 olase family associated with peptidoglycan N-acetylglucosaminidase activity, suggesting that T6S pept
16 N-Acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase, also known as "uncovering" enzyme
17 ve developed an assay system for endo-beta-N-acetylglucosaminidase and glycoamidase (PNGase), using E
20 GLU gene, resulting in deficiency of alpha-N-acetylglucosaminidase and lysosomal accumulation of hepa
21 beta-GlcNAc moiety by treatment with beta-N-acetylglucosaminidase and selective extension of the oth
22 ne with (Man(9)GlcNAc(2))Asn for endo-beta-N-acetylglucosaminidase and the other with Ala-Ser-Phe-(Ma
23 acid sequence comparisons, the novel beta-N-acetylglucosaminidase appears to be conserved in all 12
24 ll-separating activity of BslO, a putative N-acetylglucosaminidase bearing three N-terminal S-layer h
26 lcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc
30 N-Acetylglucosamine-1-phosphodiester alpha-N-Acetylglucosaminidase (EC 3.1.4.45; phosphodiester alpha
31 us suggestion that the broad-spectrum beta-N-acetylglucosaminidase encoded by the SfGlcNAcase-3/SfHex
32 297 by the streptococcal enzyme endo-beta-N-acetylglucosaminidase (EndoS) induced a dominant suppres
33 ical synthesis was combined with endo-beta-N-acetylglucosaminidase (ENGase) catalysis to allow the co
34 modifications are generated when endo-beta-N-acetylglucosaminidase (ENGase) cleaves N-linked glycans.
36 III B) is caused by a deficiency of alpha-N-acetylglucosaminidase enzyme (Naglu), leading to accumul
37 cted protein sequence is unique among beta-N-acetylglucosaminidases excepting Cht60, recently cloned
41 ng peptide : N-glycosidase F and endo-beta-N-acetylglucosaminidase F3 resulted in the formation of cr
42 can be either trimmed by a processing beta-N-acetylglucosaminidase (FDL) to produce paucimannosidic N
44 ansglycosylation activity of the endo-beta-N-acetylglucosaminidase from Arthrobacter protophormiae (E
45 on a representative member, the Nag3 beta-N-acetylglucosaminidase from Cellulomonas fimi, we now sho
47 ansglycosylation activity of the endo-beta-N-acetylglucosaminidases from Arthrobacter protophormiae (
49 t allows sequential isolation of endo-beta-N-acetylglucosaminidase H (EC 3.2.1.96)-released high-mann
50 immunoprecipitates digested with endo-beta-N-acetylglucosaminidase H (Endo H), indicate that ZP3 is s
51 paragine amidase (PNGase F)- and endo-beta-N-acetylglucosaminidase H (Endo H)-released oligosaccharid
54 ion to functional heterogeneity, endo-beta-N-acetylglucosaminidase H digestion and glycomic profiling
55 etry, brefeldin A treatment, and endo-beta-N-acetylglucosaminidase H digestion suggested that glycosy
56 ked oligosaccharides released by endo-beta-N-acetylglucosaminidase H from Schizosaccharomyces pombe g
59 secreted enzyme were cleaved by endo-beta-N-acetylglucosaminidase H, with phosphate present on the s
63 absence of this specific, processing beta-N-acetylglucosaminidase is a key factor distinguishing the
64 age disorder caused by deficiency of alpha-N-acetylglucosaminidase; it is characterized by profound m
66 this route for prenatal delivery of alpha-N-acetylglucosaminidase (Naglu) enzyme into the enzyme-def
67 erotype 2/5 (rAAV2/5) encoding human alpha-N-acetylglucosaminidase (NAGLU) plus immunosuppressive the
68 use is mutation in the gene encoding alpha-N-acetylglucosaminidase (NAGLU), deficiency of NAGLU, and
71 ied transgenic mice that over express beta-N-acetylglucosaminidase (O-GlcNAcase), an enzyme that cata
72 rase (OGT), which adds the sugar, and beta-N-acetylglucosaminidase (O-GlcNAcase), which hydrolyzes it
73 f N-acetylglucosamine is regulated by beta-N-acetylglucosaminidase (O-GlcNAcase), which was previousl
77 -fdl encodes the specific, processing beta-N-acetylglucosaminidase of S. frugiperda and validate our
79 sive disease caused by deficiency of alpha-N-acetylglucosaminidase, one of the enzymes required for t
80 gars on these moieties with mannosidase or N-acetylglucosaminidase, or the cleavage of the protein th
82 N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase (phosphodiester alpha-GlcNAcase) w
83 as a natural substrate for beta-(1 --> 4) N-acetylglucosaminidase producing a species possessing a s
84 ct inhibition of the peptide O-GlcNAc-beta-N-acetylglucosaminidase since neither the O-GlcNAc transfe
85 ase (NanA), beta-galactosidase (BgaA), and N-acetylglucosaminidase (StrH), have been previously demon
86 ear the amino or the carboxyl end of alpha-N-acetylglucosaminidase, suggesting a role for these regio
87 concluded that dspB encodes a soluble beta-N-acetylglucosaminidase that causes detachment and dispers
88 at this gene encodes a broad-spectrum beta-N-acetylglucosaminidase that functions in glycan and chiti
90 olase family GH85 is a family of endo-beta-N-acetylglucosaminidases that is responsible for the hydro
91 stent with this observation, inhibition of N-acetylglucosaminidase, the enzyme involved in the remova
95 estion by protein phosphatase 1 and beta-d-N-acetylglucosaminidase was more pronounced in STZ-diabeti
97 eatment of the soluble complexes with beta-N-acetylglucosaminidase, which catalyzes hydrolysis of the
98 e structure is produced by an unusual beta-N-acetylglucosaminidase, which removes the terminal N-acet
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