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1 Campylobacter jejuni expressing a GD1a-like, sialylated glycan.
2 teroids, phospholipids, phosphopeptides, and sialylated glycans.
3 the ionization responses for all neutral and sialylated glycans.
4 mproved desorption of both large and heavily sialylated glycans.
5 protein exhibiting no detectable binding to sialylated glycans.
6 generally not microbial cell surfaces, have sialylated glycans.
7 hat lack coding nucleic acids but do possess sialylated glycans.
8 he seal H3 bound preferentially to alpha-2,3 sialylated glycans.
9 MCs depends on alpha1,3-fucosylated, but not sialylated, glycans.
10 mutation on HA resulted in a mixed alpha2-3 sialylated glycan (alpha2-3)/alpha2-6 binding virus (NY1
11 lutinin (HA) to long (chain length) alpha2-6 sialylated glycan (alpha2-6) receptors on the human uppe
12 inding, with Gal-8N recognizing sulfated and sialylated glycans and Gal-8C recognizing blood group an
13 --enables specific binding of HA to alpha2-6 sialylated glycans and that recognition of this topology
14 re substituted with a variety of neutral and sialylated glycans and the spectra obtained were such th
15 ereas Gal-1 bound alpha2-3- but not alpha2-6-sialylated glycans, and Gal-3 bound to some glycans term
16 high-mannose glycans, fucolsylated glycans, sialylated glycans, and hybrid structures were studied.
17 sm for a parietal cell-deficient niche where sialylated glycans are expressed by a narrow band of pit
19 Single-cell binding studies indicate that sialylated glycans are likely not required for initial a
22 tissues and highlight a functional role for sialylated glycans as reovirus coreceptors in the CNS.
23 IL-6 secretion were enriched in ApoC-III, di-sialylated glycans at multiple A1AT glycosylation sites
26 ot only result in accurate identification of sialylated glycans but also improve the characterization
27 O) structure, we show ABH antigens stabilize sialylated glycan clusters on erythrocyte membranes uniq
28 ows for linkage specific characterization of sialylated glycans directly from the precursor mass but
32 itative binding affinity of HA to alpha2-->6 sialylated glycans (human receptors) is one of the impor
34 ring 3F-NeuAc to mice dramatically decreases sialylated glycans in cells of all tissues tested, inclu
35 NAc), were incorporated into fucosylated and sialylated glycans in several cancer cell lines, allowin
38 ies on sialic acid recognition using a novel sialylated glycan microarray containing modified sialic
39 Our results demonstrate the utility of this sialylated glycan microarray to investigate the biologic
46 ies of the first six reported siglecs, using sialylated glycans presented in multivalent form, on syn
47 s in ionization efficiency among neutral and sialylated glycans prevent direct quantitative compariso
49 in the expression of truncated core 1-based sialylated glycans rather than the core 2-based glycans
50 Crystal structures of EV-D68 in complex with sialylated glycan receptor analogues show that they bind
51 pecificity of the viral hemagglutinin to the sialylated glycan receptors (in the human host) by use o
52 on surfaces, obstructing a groove that binds sialylated glycan receptors in many other polyomaviruses
53 go-potential gastric stem cells that express sialylated glycan receptors recognized by H. pylori adhe
54 sialylated glycans) to human-like (alpha2-6 sialylated glycans) receptors is believed to be associat
55 array approach to analyze the repertoire of sialylated glycans recognized by viruses from the same c
58 2)v showed a predominant binding to alpha2-6-sialylated glycans, similar to human-adapted influenza A
61 binding to sialyl Lewis x (sLe(x)) and other sialylated glycans that decorate P selectin glycoprotein
62 which bound almost exclusively to alpha-2,6 sialylated glycans, the seal H3 bound preferentially to
64 hemagglutinin (HA) from avian-like (alpha2-3 sialylated glycans) to human-like (alpha2-6 sialylated g
66 tiates viral entry by engaging host receptor sialylated glycans via its receptor-binding site (RBS).
67 -R1 has not previously been shown to bind to sialylated glycans, we demonstrate that it preferentiall
68 and alkaline BGE systems, the mobilities of sialylated glycans were shifted relative to nonsialylate
69 hibited significantly reduced binding to all sialylated glycans, whereas Gal-1 bound alpha2-3- but no
70 ly, we used a nonmetabolic approach to label sialylated glycans with an independent chemistry, enabli
72 for simultaneous profiling both neutral and sialylated glycans without derivatization or labeling.
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