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1 s amino acid by the cytosolic enzyme peptide N-glycanase.
2 ained following incubation of factor Va with N-glycanase.
3 edia, were converted to the 29.3 kDa band by N-glycanase.
4 ed and partially deglycosylated by cytosolic N-glycanase.
5 monosaccharides, or pretreatment of MSG with N-glycanase.
6 CD tissues with either chondroitinase ABC or N-glycanase.
7 ed in the cytosol by the PNG-1/NGLY1 peptide:N-glycanase.
8                                              N-glycanase 1 (NGLY1) deficiency is a debilitating, ultr
9                                              N-Glycanase 1 (NGLY1) is a cytoplasmic deglycosylating e
10   Here, we establish that loss of Drosophila N-glycanase 1 (Pngl) in a specific intestinal cell type
11                                              N-glycanase activity is therefore not required for dislo
12 NG1 enzyme and its mammalian homolog display N-glycanase activity towards intact glycoproteins.
13 smic intermediates that are the result of an N-glycanase activity, believed to act prior to destructi
14          The deglycosylating enzyme, peptide:N-glycanase, acts on misfolded N-linked glycoproteins di
15 ules that had been deglycosylated by peptide N-glycanase and a large number of molecules that had not
16 N-glycanase, PNG1, has been cloned, but this N-glycanase and its mammalian homolog were reported to b
17                Treatment of purified FV with N-glycanase and neuraminidase under nonprotein-denaturin
18 the cytosol, where they are acted upon by an N-glycanase and the proteasome.
19 n encode regulators of ER traffic, a peptide N-glycanase, and DDI-1, a conserved aspartic protease.
20 cell extract with the enzymes neuraminidase, N-glycanase, and O-glycanase resulted in the stepwise lo
21 the cytosolic deglycosylating enzyme peptide:N'glycanase are both required for fluorescence.
22            Rhesus erythrocytes, treated with N-glycanase, bound specifically to P. vivax region II.
23 ution crystal structure of the mouse peptide N-glycanase catalytic core in complex with the xeroderma
24 at has lost the single N-linked glycan in an N-glycanase-catalyzed reaction transiently accumulates i
25                               Treatment with N-glycanase caused a reduction in mass of 3571 +/- 219 D
26 , removal of whole oligosaccharide chains by N-glycanase caused an almost total loss of the ability o
27                                 Furthermore, N-glycanase cleavage of asparagine-linked sites in nativ
28                                              N-Glycanase cleaves the new oligosaccharide from Q333N f
29 D5, since treatment of CD5Rg with PNGaseF on N-glycanase completely abrogates its ability to bind act
30 tudy showed that cleavage of the glycan with N-glycanase decreased the attachment and infectivity of
31 nstrates that treatment of the organism with N-glycanase decreases or ablates infectivity in vivo.
32 membrane associated FR from either cell with N-glycanase did not influence its ligand binding charact
33 lphaAsn(56) was removed by selective peptide-N-glycanase digestion (N(56)dg-alpha).
34                                              N-glycanase digestion increased I566T mutant FVIII activ
35                                              N-Glycanase digestion showed that RhBG/Rhbg has a carboh
36 rides were released from the glycoprotein by N-glycanase digestion, coupled to a 2-aminopyridyl resid
37 glycosidase-H and is reduced to 37-kDa after N-glycanase digestion.
38 ked glycosylation site that was confirmed by N-glycanase digestion.
39   Here, we show that the PNG-1/NGLY1 peptide:N-glycanase edits the sequence of SKN-1A protein by conv
40 ylation because deglycosylation with peptide:N-glycanase eliminated blocking.
41 ensitivity of the mutant receptor to peptide-N-glycanase F and endoglycosidase H, and insensitivity t
42 , and COS cells expressing NIS with peptidyl N-glycanase F converted the approximately 87 kDa-polypep
43      Indeed, sensitivity of native proPC2 to N-glycanase F digestion and inhibition of proPC2 folding
44 d it shifts from 220 to 200 kDa upon protein:N-glycanase F digestion.
45 sed from Lec19 cell glycoproteins by peptide N-glycanase F revealed species with the predicted masses
46 osaccharides were released by treatment with N-glycanase F, reductively aminated with anthranilic aci
47                                      Peptide N-glycanase features a large cleft between its catalytic
48                        A cytoplasmic peptide:N-glycanase has been implicated in the proteasomal degra
49               Furthermore, the mouse peptide N-glycanase-HR23B complex mimics the interaction between
50 ed glycoproteins, consistent with a role for N-glycanase in cytoplasmic turnover of glycoproteins.
51 ), and subsequent deglycosylation by peptide-N-glycanase in the cytosol.
52 Treatment of factor V with neuraminidase and N-glycanase mainly altered the electrophoretic mobility
53                               Treatment with N-glycanase markedly reduced functionally glycosylated a
54                                Mouse peptide N-glycanase (mPNGase) cleaves the N-glycan chain from mi
55 us loss-of-function mutations in the peptide:N-glycanase (NGLY1) gene cause NGLY1 deficiency, a conge
56 gocytosis in a manner that was attenuated by N-glycanase or collagenase treatment of SP-A, implicatin
57              A gene encoding a yeast peptide:N-glycanase, PNG1, has been cloned, but this N-glycanase
58                                Yeast peptide:N-glycanase (Png1p; PNGase), a deglycosylation enzyme in
59           Here we demonstrate it is peptide: N-glycanase (PNGase or PNG1) that deglycosylates disloca
60                                      Peptide:N-glycanase (PNGase) cleaves oligosaccharide chains from
61        In this pathway the cytosolic peptide-N-glycanase (PNGase) cleaves the N-linked glycan chains
62                                      Peptide:N-glycanase (PNGase) has been proposed to participate in
63 g cofactors, such as Ufd2, Ufd3, and peptide:N-glycanase (PNGase) in higher eukaryotes.
64                                      Peptide N-glycanase (PNGase) is involved in the cleavage of olig
65 nes of evidence suggest that soluble peptide:N-glycanase (PNGase) is involved in the quality control
66 t has been proposed that cytoplasmic peptide:N-glycanase (PNGase) may be involved in the proteasome-d
67 amidase, EC 3.5.1.52; also known as peptide: N-glycanases (PNGases) release N-linked oligosaccharides
68 elated to the recently characterized peptide-N-glycanases (PNGases) which remove glycans from glycopr
69 linked carbohydrate from Asn(371) by peptide N-glycanase, proteolysis by the proteasome and other pro
70 different from the orthologous yeast peptide N-glycanase-Rad23 complex.
71 rides from gp55, by extensive digestion with N-glycanase, reduces its Mr to approximately 21 000 and
72                  The on-plate digestion with N-glycanase released effectively the corresponding oligo
73                                      Peptide N-glycanase removes N-linked oligosaccharides from misfo
74 membranes in the presence of the glycosidase N-glycanase shifted the apparent molecular weight of VMA
75 d by intact blocking IgG, but not by peptide:N-glycanase-treated blocking IgG, suggesting that blocki
76        Analysis of the masses of these after N-glycanase treatment indicated that one was substituted
77                                After peptide:N-glycanase treatment of the receptor to remove most of
78                                              N-glycanase treatment removed N-linked oligosaccharides
79    3) gp180 is heavily N-glycosylated, since N-glycanase treatment results in a >50% reduction in siz
80                                              N-Glycanase treatment to remove N-linked oligosaccharide
81  immunoprecipitated a M(r) 58,000 band after N-glycanase treatment, most likely a protein with a hete
82 the Class I MHC HCs are deglycosylated by an N-glycanase-type activity.
83  to mild deglycosylation (neuraminidase plus N-glycanase) under nondenaturing conditions.
84 e was unexpectedly resistant to digestion by N-glycanase unless first dephosphorylated, but it was se
85  the formation of a tight complex of peptide N-glycanase with Rad23 in yeast and the orthologous HR23