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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.
9 smic intermediates that are the result of an N-glycanase activity, believed to act prior to destructi
11 ules that had been deglycosylated by peptide N-glycanase and a large number of molecules that had not
12 N-glycanase, PNG1, has been cloned, but this N-glycanase and its mammalian homolog were reported to b
15 n encode regulators of ER traffic, a peptide N-glycanase, and DDI-1, a conserved aspartic protease.
16 cell extract with the enzymes neuraminidase, N-glycanase, and O-glycanase resulted in the stepwise lo
19 ution crystal structure of the mouse peptide N-glycanase catalytic core in complex with the xeroderma
20 at has lost the single N-linked glycan in an N-glycanase-catalyzed reaction transiently accumulates i
22 , removal of whole oligosaccharide chains by N-glycanase caused an almost total loss of the ability o
25 D5, since treatment of CD5Rg with PNGaseF on N-glycanase completely abrogates its ability to bind act
26 tudy showed that cleavage of the glycan with N-glycanase decreased the attachment and infectivity of
27 nstrates that treatment of the organism with N-glycanase decreases or ablates infectivity in vivo.
28 membrane associated FR from either cell with N-glycanase did not influence its ligand binding charact
32 rides were released from the glycoprotein by N-glycanase digestion, coupled to a 2-aminopyridyl resid
36 ensitivity of the mutant receptor to peptide-N-glycanase F and endoglycosidase H, and insensitivity t
37 , and COS cells expressing NIS with peptidyl N-glycanase F converted the approximately 87 kDa-polypep
40 sed from Lec19 cell glycoproteins by peptide N-glycanase F revealed species with the predicted masses
41 osaccharides were released by treatment with N-glycanase F, reductively aminated with anthranilic aci
45 ed glycoproteins, consistent with a role for N-glycanase in cytoplasmic turnover of glycoproteins.
47 Treatment of factor V with neuraminidase and N-glycanase mainly altered the electrophoretic mobility
50 gocytosis in a manner that was attenuated by N-glycanase or collagenase treatment of SP-A, implicatin
59 nes of evidence suggest that soluble peptide:N-glycanase (PNGase) is involved in the quality control
60 t has been proposed that cytoplasmic peptide:N-glycanase (PNGase) may be involved in the proteasome-d
61 amidase, EC 3.5.1.52; also known as peptide: N-glycanases (PNGases) release N-linked oligosaccharides
62 elated to the recently characterized peptide-N-glycanases (PNGases) which remove glycans from glycopr
63 linked carbohydrate from Asn(371) by peptide N-glycanase, proteolysis by the proteasome and other pro
65 rides from gp55, by extensive digestion with N-glycanase, reduces its Mr to approximately 21 000 and
68 membranes in the presence of the glycosidase N-glycanase shifted the apparent molecular weight of VMA
69 d by intact blocking IgG, but not by peptide:N-glycanase-treated blocking IgG, suggesting that blocki
73 3) gp180 is heavily N-glycosylated, since N-glycanase treatment results in a >50% reduction in siz
75 immunoprecipitated a M(r) 58,000 band after N-glycanase treatment, most likely a protein with a hete
78 e was unexpectedly resistant to digestion by N-glycanase unless first dephosphorylated, but it was se
79 the formation of a tight complex of peptide N-glycanase with Rad23 in yeast and the orthologous HR23
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