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1 s with increased branching and extended poly-N-acetyllactosamine.
2 not require DD-heptose to form the terminal N-acetyllactosamine.
3 opically labeled CMP-N-acetylneuraminate and N-acetyllactosamine.
4 ic pathway leading to the addition of sialyl-N-acetyllactosamine.
5 ipooligosaccharide (LOS) which terminates in N-acetyllactosamine.
6 ently add N-acetyllactosamine to linear poly-N-acetyllactosamines.
7 -3GalNAc termini, and some increases in poly-N-acetyllactosamines.
8 ding a galactose to linear and branched poly-N-acetyllactosamines.
9 ther beta-Xyl or chains of, on average, five N-acetyllactosamine (-3Galbeta1-4GlcNAcbeta1-) (LacNAc)
11 s for lactose, lactulose, lacto-N-biose, and N-acetyllactosamine, all of which exhibit binding enthal
12 methyl beta-galactopyranoside, lactose, and N-acetyllactosamine and a greater -delta H value for the
13 three other H. ducreyi strains also contain N-acetyllactosamine and are highly sialylated (approxima
14 h sequence and linkage data are obtained for N-acetyllactosamine and sialyl-N-acetyllactosamine oligo
15 0 have been previously found to terminate in N-acetyllactosamine and sialyl-N-acetyllactosamine, Neu5
16 ated that itraconazole globally reduced poly-N-acetyllactosamine and tetra-antennary complex N-glycan
17 eyi contain terminal sialic acid attached to N-acetyllactosamine and that this modification is likely
19 cans, fetuin N-glycans, synthetic sialylated N-acetyllactosamines, and on alpha(2)-HS-glycoprotein.
20 Complex glycan structural features, such as N-acetyllactosamine antenane, neuraminic acids, and nonr
22 ases, which play important roles in how poly-N-acetyllactosamines are synthesized in different accept
26 e of galectin-3 (GaL3), a multicompartmented N-acetyllactosamine-binding chimeric lectin, on atheroge
27 that 4-F-GlcNAc (putative inhibitor of poly-N-acetyllactosamine biosynthesis) was more potent than B
28 amine (4-F-GlcNAc), a metabolic inhibitor of N-acetyllactosamine biosynthesis, and analyzed tumor gro
29 osamine is a unique carbohydrate composed of N-acetyllactosamine branches attached to linear poly-N-a
32 lts also showed that monosialyl and disialyl N-acetyllactosamines can serve equally as an acceptor, s
33 s with IGHV4-34*01 heavy chains bind to poly-N-acetyllactosamine carbohydrates (I/i antigen) on eryth
34 syl core may carry predominantly linear poly-N-acetyllactosamine chains, whereas the Manalpha1-3 arm
37 y crystallographic structure of the galectin-N-acetyllactosamine complex determined by Liao et al.
43 TbGT8 influences the processing of the poly N-acetyllactosamine-containing asparagine-linked glycans
44 cterized to demonstrate that they produced a N-acetyllactosamine-containing LOS by silver-stained sod
49 of CD45, and more specifically, an N-linked N-acetyllactosamine determinant preferentially expressed
50 ate carbohydrate chains consist of repeating N-acetyllactosamine disaccharides with sulfation on the
51 cells, indicating direct inhibition on poly-N-acetyllactosamine elongation and selectin-binding dete
52 complete loss of sialylation of the terminal N-acetyllactosamine epitope and expression of the higher
55 N-acetyllactosamine synthesis, allowing poly-N-acetyllactosamine extension mostly along the linear po
58 jor product was the oligosaccharide with one N-acetyllactosamine extension on the linear Galbeta1-->4
60 opy compensation, and, with the exception of N-acetyllactosamine, follow a van't Hoff dependence of t
61 ed by the addition of beta1,3-linked GlcA to N-acetyllactosamine followed by sulfation of the C-3 pos
62 branched acceptor than the summation of poly-N-acetyllactosamines formed individually on each unbranc
63 group consists of Neu5Acalpha2-3(lactose or N-acetyllactosamine) forms that lack the branched mannos
64 -sialyltransferases for the common substrate N-acetyllactosamine (Gal(beta)1-4GlcNAc-R) on N-linked c
65 timal configuration of sulfate esters on the N-acetyllactosamine (Galbeta1-->4GlcNAc) core of sulfosi
67 possess essentially the same affinities for N-acetyllactosamine; however, the animal lectin shows a
68 ialylated, triantennary oligosaccharide with N-acetyllactosamine (i.e. Galbeta1,4GlcNAc-) or lacto-N-
70 a for 4-6 showed that each enzyme recognizes N-acetyllactosamine in a low minimum energy conformation
72 ransferase, was capable of synthesizing poly-N-acetyllactosamine in core 2 branched oligosaccharides.
73 demonstrate the importance of Gal-1-binding N-acetyllactosamines in controlling the fate and functio
74 consistent with previous findings that poly-N-acetyllactosamines in human erythrocytes, PA-1 embryon
76 the present study, we first found that poly-N-acetyllactosamines in N-glycans are most efficiently s
77 e presence of core 1 O-glycans, but not poly-N-acetyllactosamine, in apically targeted MUC1 and chime
81 It has been shown that the amount of poly-N-acetyllactosamine is increased in N-glycans, when they
83 enous lectin that recognizes glycans bearing N-acetyllactosamine (LacNAc) epitopes, induces branching
84 ces (Galbeta1-4GlcNAc)(n) when compared with N-acetyllactosamine (LacNAc) glycans (Galbeta1-4GlcNAc).
86 lycan that has N-acetylglucosamine (GlcNAc), N-acetyllactosamine (LacNAc), and unnatural Galalpha(1,4
87 anti-skin inflammatory activity by ablating N-acetyllactosamine (LacNAc), sialyl Lewis X (sLe(X)), a
88 re that sialylated glycosphingolipids with 5 N-acetyllactosamine (LacNAc, Galbeta1-4GlcNAcbeta1-3) re
89 bilized extended glycans containing terminal N-acetyllactosamine (LN; Galbeta1-4GlcNAc) sequences on
90 est that metabolic lowering of Gal-1-binding N-acetyllactosamines may attenuate tumor growth by boost
92 h transfers a galactose molecule to terminal N-acetyllactosamine (N-lac) present on various glycoprot
93 terminate in N-acetyllactosamine and sialyl-N-acetyllactosamine, Neu5Ac alpha 2-->3Gal beta 1-->4Glc
95 Development of an effective synthesis of N-acetyllactosamine oligomers will therefore provide a n
97 obtained for N-acetyllactosamine and sialyl-N-acetyllactosamine oligosaccharide antennae from biante
99 ine (LN; Galbeta1-4GlcNAc) sequences on poly-N-acetyllactosamine (PL; (-3Galbeta1-4GlcNAcbeta1-)(n))
100 n olfactory sensory neurons (OSNs) with poly-N-acetyllactosamine (PLN) oligosaccharides determined by
101 hibited higher binding for glycans with poly-N-acetyllactosamine (poly(LacNAc)) sequences (Galbeta1-4
104 A77 lacks the galactose residue found in the N-acetyllactosamine portion of the strain 35000HP LOS as
105 ant lacks the galactose residue found in the N-acetyllactosamine portion of the strain 35000HP LOS.
106 e, termed Gal3ST-3, that acts exclusively on N-acetyllactosamine present in N-glycans and core2-branc
107 eisseria gonorrhoeae sialylates the terminal N-acetyllactosamine present on its lipooligosaccharide (
108 g moderate amounts of sialyl Lewis X in poly-N-acetyllactosamines produced large numbers of lung tumo
109 abundance of the Lewis(x) sequence based on N-acetyllactosamine recognized by anti-L5, and a paucity
110 ucity of the Lewis(x) sequence based on poly-N-acetyllactosamine recognized by anti-SSEA-1; (ii) insi
111 N-acetylglucosamine residues within the poly(N-acetyllactosamine) repeat sequence and signals represe
112 OS glycoforms containing di-, tri-, and poly-N-acetyllactosamine repeats added to the terminal region
113 osamine is a unique carbohydrate composed of N-acetyllactosamine repeats and provides the backbone st
114 branched oligosaccharides with multiple poly-N-acetyllactosamine repeats is nearly abolished by AZT c
115 -TI leads to efficient and equal addition of N-acetyllactosamine repeats on both side chains of GlcNA
118 dramatically as the acceptors contained more N-acetyllactosamine repeats, consistent with the fact th
119 n acceptors containing increasing numbers of N-acetyllactosamine repeats, in contrast to beta4Gal-TI,
120 uestion of how the gonococcus infects men if N-acetyllactosamine residues are substituted by Neu5Ac d
125 them, cores 2 and 4 are important for having N-acetyllactosamine side chains, which can be further mo
126 3Gal-3, -4, and -6, which act on the type II N-Acetyllactosamine structure (Galbeta1,4GlcNAc) to crea
129 they produced extended GlcNAc-sulfated poly-N-acetyllactosamine structures with more than four repea
130 onger carbohydrate substrates that have poly-N-acetyllactosamine structures, suggesting the involveme
131 te that beta4Gal-TIV is responsible for poly-N-acetyllactosamine synthesis in core 2 branched O-glyca
132 results, taken together, indicate that poly-N-acetyllactosamine synthesis in N-glycans and core 2- a
134 h is a rate-limiting step in I-branched poly-N-acetyllactosamine synthesis, allowing poly-N-acetyllac
135 1, an enzyme proposed to be involved in poly-N-acetyllactosamine synthesis, were causal for congenita
136 termine how this increased synthesis of poly-N-acetyllactosamines takes place, the branched acceptor
137 multiple internal GlcNAc of unbranched poly-N-acetyllactosamine, termed "myeloglycan," the physiolog
139 ing activity of the B. arenarum galectin for N-acetyllactosamine, the human blood group A tetrasaccha
140 finities and -delta H values for lactose and N-acetyllactosamine, the soybean agglutinin possesses si
141 possess essentially the same affinities for N-acetyllactosamine, the two mutants possess much lower
142 ltransferase and beta4Gal-TI efficiently add N-acetyllactosamine to linear poly-N-acetyllactosamines.
145 ore than four repeats of the GlcNAc-sulfated N-acetyllactosamine unit in the presence of corneal N-ac
146 , the Lc3 synthase could extend the terminal N-acetyllactosamine unit of nLc4 and also had a broad sp
147 core with > 10 monosaccharide units (or > 4 N-acetyllactosamine units) showed E-selectin binding und
148 e having at least 10 monosaccharide units (4 N-acetyllactosamine units) with internal multiple fucosy
150 Ic, and the large difference in the price of N-acetyllactosamine vs. lactose, it is suggested that la
151 The efficacy of the galectin-3 inhibitor N-acetyllactosamine was evaluated in TGR(mREN2)27 (REN2)
152 ucosaminyltransferase, the formation of poly-N-acetyllactosamine was found to be extremely inefficien
155 ng when galectin-3, with preference for poly-N-acetyllactosamine, was depleted from polarized MDCK ce
156 tivity and both activities were inhibited by N-acetyllactosamine, whereas a C-terminal deletion mutan
157 lactosamine branches attached to linear poly-N-acetyllactosamine, which is synthesized by I-branching
158 ly to beta1,6-GlcNAc attached to linear poly-N-acetyllactosamines, while beta1, 3-N-acetylglucosaminy
159 librium dialysis, N-Gal-1 and V5D-Gal-1 bind N-acetyllactosamine with a Kd approximately 90 microM, w
161 of the terminal alpha-Gal or whether capping N-acetyllactosamine with another oligosaccharide would a
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