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1 tissues with either chondroitinase ABC or N-glycanase.
2 amino acid by the cytosolic enzyme peptide N-glycanase.
3 ned following incubation of factor Va with N-glycanase.
4 y O-glycosylation of the type sensitive to O-glycanase.
5 ia, were converted to the 29.3 kDa band by N-glycanase.
6 and partially deglycosylated by cytosolic N-glycanase.
7 nosaccharides, or pretreatment of MSG with N-glycanase.
8 96% similarity to sequences of family F beta-glycanases.
9 bility of succinoglycan to cleavage by these glycanases.
14 ic intermediates that are the result of an N-glycanase activity, believed to act prior to destruction
17 es that had been deglycosylated by peptide N-glycanase and a large number of molecules that had not b
18 glycanase, PNG1, has been cloned, but this N-glycanase and its mammalian homolog were reported to be
20 hat is required for the secretion of NodO, a glycanase and probably a number of other proteins, at le
22 encode regulators of ER traffic, a peptide N-glycanase, and DDI-1, a conserved aspartic protease.
23 ll extract with the enzymes neuraminidase, N-glycanase, and O-glycanase resulted in the stepwise lowe
24 tinase ABC, and heparitinases, but not other glycanases, and 2) purified chondroitin sulfates, hepara
25 ant to degradation by proteases and N- and O-glycanases, and unaffected by oxidation with sodium peri
27 o yield LMW succinoglycan, but only when the glycanases are added to cultures at greater than physiol
29 idase F, sialidase alone, or sialidase and O-glycanase but not to treatment with endoglycosidase H.
30 ion crystal structure of the mouse peptide N-glycanase catalytic core in complex with the xeroderma p
31 has lost the single N-linked glycan in an N-glycanase-catalyzed reaction transiently accumulates in
33 removal of whole oligosaccharide chains by N-glycanase caused an almost total loss of the ability of
34 tor Va heavy chain, whereas treatment with O-glycanase changed the mobility of the connecting region.
36 exsH+ genes, implying that the ExoK and ExsH glycanases cleave HMW succinoglycan to yield LMW succino
38 , since treatment of CD5Rg with PNGaseF on N-glycanase completely abrogates its ability to bind activ
39 of PrsD and PrsE, and that the ExsH and ExoK glycanases contribute to production of low-molecular-wei
40 dy showed that cleavage of the glycan with N-glycanase decreased the attachment and infectivity of ch
43 ng retting using chemical analysis, specific glycanase degradation and immuno-labelling of cell wall
44 mbrane associated FR from either cell with N-glycanase did not influence its ligand binding character
50 des were released from the glycoprotein by N-glycanase digestion, coupled to a 2-aminopyridyl residue
53 of Env-SU, and this was verified by specific glycanase digestions and a detailed analysis of the mole
56 m meliloti) cultures, the endo-1, 3-1,4-beta-glycanases ExoK and ExsH depolymerize nascent high-molec
57 termined by both the levels of ExoK and ExsH glycanase expression and the susceptibility of succinogl
58 sitivity of the mutant receptor to peptide-N-glycanase F and endoglycosidase H, and insensitivity to
59 and COS cells expressing NIS with peptidyl N-glycanase F converted the approximately 87 kDa-polypepti
60 Indeed, sensitivity of native proPC2 to N-glycanase F digestion and inhibition of proPC2 folding s
62 d from Lec19 cell glycoproteins by peptide N-glycanase F revealed species with the predicted masses o
63 accharides were released by treatment with N-glycanase F, reductively aminated with anthranilic acid,
70 eatment of factor V with neuraminidase and N-glycanase mainly altered the electrophoretic mobility of
73 cytosis in a manner that was attenuated by N-glycanase or collagenase treatment of SP-A, implicating
75 RapA2, RapB and RapC, two cadherins and the glycanase PlyB), the polysaccharide regulator RosR, and
84 s of evidence suggest that soluble peptide:N-glycanase (PNGase) is involved in the quality control sy
85 has been proposed that cytoplasmic peptide:N-glycanase (PNGase) may be involved in the proteasome-dep
86 idase, EC 3.5.1.52; also known as peptide: N-glycanases (PNGases) release N-linked oligosaccharides f
87 ated to the recently characterized peptide-N-glycanases (PNGases) which remove glycans from glycoprot
89 nked carbohydrate from Asn(371) by peptide N-glycanase, proteolysis by the proteasome and other prote
91 des from gp55, by extensive digestion with N-glycanase, reduces its Mr to approximately 21 000 and in
94 he enzymes neuraminidase, N-glycanase, and O-glycanase resulted in the stepwise lowering of the appar
95 ermined by [3H]glucosamine incorporation and glycanase sensitivity of the products on SDS-polyacrylam
96 mbranes in the presence of the glycosidase N-glycanase shifted the apparent molecular weight of VMAT2
98 taining proteoglycans, we treated cells with glycanases to remove these confounding factors, which di
99 by intact blocking IgG, but not by peptide:N-glycanase-treated blocking IgG, suggesting that blocking
101 intracellular Ca(2+) mobilization on either glycanase-treated or untreated peripheral blood mononucl
102 led RANTES demonstrated saturable binding to glycanase-treated peripheral blood mononuclear cells, an
103 Analysis of the masses of these after N-glycanase treatment indicated that one was substituted a
105 , these activities are strongly inhibited by glycanase treatment of receptor-expressing cells, indica
108 3) gp180 is heavily N-glycosylated, since N-glycanase treatment results in a >50% reduction in size.
110 mmunoprecipitated a M(r) 58,000 band after N-glycanase treatment, most likely a protein with a hetero
114 was unexpectedly resistant to digestion by N-glycanase unless first dephosphorylated, but it was sens
115 he formation of a tight complex of peptide N-glycanase with Rad23 in yeast and the orthologous HR23 p
116 xsH encodes a homologue of endo-1,3-1,4-beta-glycanases with glycine-rich nonameric repeats typical o
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