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1 hich recognizes poly-N-acetylglucosamine and poly-N-acetyllactosamine.
2 ctures with increased branching and extended poly-N-acetyllactosamine.
3 beta1-3GalNAc termini, and some increases in poly-N-acetyllactosamines.
4 in adding a galactose to linear and branched poly-N-acetyllactosamines.
5 fficiently add N-acetyllactosamine to linear poly-N-acetyllactosamines.
6 of pro-MM factor, NGFR, implicating i-linear poly-N-acetyllactosamine and Gal-8 as biomarkers and the
8 onstrated that itraconazole globally reduced poly-N-acetyllactosamine and tetra-antennary complex N-g
10 nsferases, which play important roles in how poly-N-acetyllactosamines are synthesized in different a
12 found that 4-F-GlcNAc (putative inhibitor of poly-N-acetyllactosamine biosynthesis) was more potent t
14 bodies with IGHV4-34*01 heavy chains bind to poly-N-acetyllactosamine carbohydrates (I/i antigen) on
15 mannosyl core may carry predominantly linear poly-N-acetyllactosamine chains, whereas the Manalpha1-3
19 that TbGT8 influences the processing of the poly N-acetyllactosamine-containing asparagine-linked gl
20 ifically recognize a triantennary sialylated poly-N-acetyllactosamine-containing N-glycan exposed on
22 fferent classes of complex glycans including poly-N-acetyllactosamine derivatives, human milk oligosa
23 on T cells, indicating direct inhibition on poly-N-acetyllactosamine elongation and selectin-binding
25 poly-N-acetyllactosamine synthesis, allowing poly-N-acetyllactosamine extension mostly along the line
27 the branched acceptor than the summation of poly-N-acetyllactosamines formed individually on each un
28 inyltransferase, was capable of synthesizing poly-N-acetyllactosamine in core 2 branched oligosacchar
29 irely consistent with previous findings that poly-N-acetyllactosamines in human erythrocytes, PA-1 em
31 In the present study, we first found that poly-N-acetyllactosamines in N-glycans are most efficien
32 in the presence of core 1 O-glycans, but not poly-N-acetyllactosamine, in apically targeted MUC1 and
38 lular Gal-8 bound preferentially to i-linear poly-N-acetyllactosamines on N-glycans of the TIC marker
39 ely large complex-type N-glycans with linear poly-N-acetyllactosamine (PL) [-3Galbeta1-4GlcNAcbeta1-]
40 ing, core fucosylation, and the abundance of poly-N-acetyllactosamine (PL) [-3Galbeta1-4GlcNAcbeta1-]
41 tosamine (LN; Galbeta1-4GlcNAc) sequences on poly-N-acetyllactosamine (PL; (-3Galbeta1-4GlcNAcbeta1-)
42 sed in olfactory sensory neurons (OSNs) with poly-N-acetyllactosamine (PLN) oligosaccharides determin
43 in exhibited higher binding for glycans with poly-N-acetyllactosamine (poly(LacNAc)) sequences (Galbe
49 essing moderate amounts of sialyl Lewis X in poly-N-acetyllactosamines produced large numbers of lung
50 a paucity of the Lewis(x) sequence based on poly-N-acetyllactosamine recognized by anti-SSEA-1; (ii)
51 n of N-acetylglucosamine residues within the poly(N-acetyllactosamine) repeat sequence and signals re
52 que LOS glycoforms containing di-, tri-, and poly-N-acetyllactosamine repeats added to the terminal r
53 n of branched oligosaccharides with multiple poly-N-acetyllactosamine repeats is nearly abolished by
57 ever, they produced extended GlcNAc-sulfated poly-N-acetyllactosamine structures with more than four
58 to longer carbohydrate substrates that have poly-N-acetyllactosamine structures, suggesting the invo
60 ndicate that beta4Gal-TIV is responsible for poly-N-acetyllactosamine synthesis in core 2 branched O-
61 These results, taken together, indicate that poly-N-acetyllactosamine synthesis in N-glycans and core
63 branch is a rate-limiting step in I-branched poly-N-acetyllactosamine synthesis, allowing poly-N-acet
64 B3GNT1, an enzyme proposed to be involved in poly-N-acetyllactosamine synthesis, were causal for cong
65 To determine how this increased synthesis of poly-N-acetyllactosamines takes place, the branched acce
66 on at multiple internal GlcNAc of unbranched poly-N-acetyllactosamine, termed "myeloglycan," the phys
67 branched O-glycans contain fewer and shorter poly-N-acetyllactosamines than N-glycans in many cells.
68 express a unique glycome featuring i-linear poly-N-acetyllactosamines through the loss of I-branchin
69 tylglucosaminyltransferase, the formation of poly-N-acetyllactosamine was found to be extremely ineff
72 rgeting when galectin-3, with preference for poly-N-acetyllactosamine, was depleted from polarized MD
73 cetyllactosamine branches attached to linear poly-N-acetyllactosamine, which is synthesized by I-bran
74 poorly to beta1,6-GlcNAc attached to linear poly-N-acetyllactosamines, while beta1, 3-N-acetylglucos