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1 e export of the polysaccharide poly beta-1,6-N-acetyl-d-glucosamine.
2 amine-6-phosphate, the intracellular form of N-acetyl-D-glucosamine.
3 nthesis of UDP-ManNAc3NAcA starting from UDP-N-acetyl-d-glucosamine.
4 he sugars composing the unit as rhamnose and N-acetyl-D-glucosamine.
5 cetyl-D-mannosaminuronic acid, and GlcNAc is N-acetyl-D-glucosamine.
6 cetyl-D-mannosaminuronic acid, and GlcNAc is N-acetyl-D-glucosamine.
7 lucose), alpha- or beta-methylmannoside, and N-acetyl-D-glucosamine.
8  for biosynthesis of the (alpha1-->4)-linked N-acetyl-D-glucosamine 1-phosphate capsule of Neisseria
9 de repeat is [-4) beta-L-rhamnose (1-3) beta-N-acetyl-D-glucosamine (1-] with an N-acetyl-D-glucosami
10 , confirming that CsaA is the functional UDP-N-acetyl-D-glucosamine-2-epimerase and CsaB the function
11 aA, -B, and -C are thought to encode the UDP-N-acetyl-D-glucosamine-2-epimerase, poly-ManNAc-1-phosph
12             NagA catalyzes the hydrolysis of N-acetyl-d-glucosamine-6-phosphate to d-glucosamine-6-ph
13 ssion by NagC is relieved in the presence of N-acetyl-D-glucosamine-6-phosphate, the intracellular fo
14 perfamily and catalyzes the deacetylation of N-acetyl-d-glucosamine-6-phosphate.
15 e analyses to consist of unbranched beta-1,6-N-acetyl-D-glucosamine, a polymer previously unknown fro
16 yme activity and reduced uridine diphosphate-N-acetyl-D-glucosamine, along with decreased O- and N-li
17                                              N-acetyl-D-glucosamine-alpha-1-phosphate is then deacety
18                                          The N-acetyl-D-glucosamine-alpha-1-phosphate used in this sy
19                                              N-Acetyl-D-glucosamine and beta-glucan, which inhibit Ma
20 rides (paCOS), consisting of beta-1,4-linked N-acetyl-d-glucosamine and d-glucosamine units, possess
21 ucuronic acid, N-acetyl-d-galactosamine, and N-acetyl-d-glucosamine, and all except mannose were redu
22 hibitors such as alloxan, D-glucosamine, and N-acetyl-D-glucosamine, and mimicked by the non-metaboli
23 inase inhibitors alloxan, d-glucosamine, and N-acetyl-d-glucosamine; and 4) orexin glucosensors detec
24 med at improving the oral bioavailability of N-acetyl-(d)-glucosamine as its putative bioactive phosp
25 nt failed to develop biofilms when utilizing N-acetyl-D-glucosamine as a carbon source.
26 ses on the O-3 and O-4 phosphate prodrugs of N-acetyl-(d)-glucosamine bearing a 4-methoxy phenyl grou
27         The linear homopolymer poly-beta-1,6-N-acetyl-D-glucosamine (beta-1,6-GlcNAc; PGA) serves as
28 proteins known to synthesize a poly-beta-1,6-N-acetyl-D-glucosamine biofilm matrix.
29 ose, d-xylose, d-mannoheptaose) and charged (N-acetyl d-glucosamine, d-glucosamine, d-glucuronic acid
30 luding L-fucose, D-gluconate, D-glucuronate, N-acetyl-D-glucosamine, D-mannose, and D-ribose.
31  lacking the polysaccharide adhesin beta-1,6-N-acetyl-d-glucosamine (DeltapgaC) also exhibited aperio
32                                              N-acetyl-d-glucosamine did not inhibit sCR1-MBL binding,
33                                              N-acetyl-D-glucosamine disrupted CR3 clusters and sinuso
34     The remaining four bands were present in N-acetyl-D-glucosamine eluates, although their % distrib
35 ssii involves chemotaxis to and transport of N-acetyl-D-glucosamine (GlcNAc) and D-glucose.
36                                We identified N-acetyl-d-glucosamine (GlcNAc) as the most predictive m
37 ures disclosed that the high-affinity ligand N-acetyl-d-glucosamine (GlcNAc) binds in the collectin C
38                                              N-acetyl-d-glucosamine (GlcNAc) is a major component of
39                           The monosaccharide N-acetyl-d-glucosamine (GlcNAc) is an abundant building
40 odifications of serine and threonine by beta-N-acetyl-D-glucosamine (GlcNAc) may regulate muscle cont
41 es encoding cytoplasmic proteins involved in N-acetyl-D-glucosamine (GlcNAc) metabolism.
42  HGAC 39.G3 binding to an antigen displaying N-acetyl-d-glucosamine (GlcNAc) residues on a polyrhamno
43                           HEMA modified with N-acetyl-D-glucosamine (GlcNAc) was also polymerized to
44               Another major finding was that N-acetyl-D-glucosamine (GlcNAc) which does not inhibit a
45  has been identified as a molecular mimic of N-acetyl-D-glucosamine (GlcNAc), a known ligand of MBL.
46 ing an Ig H chain conferring specificity for N-acetyl-d-glucosamine (GlcNAc), we developed transgenic
47 direct labeling of B cells reactive with the N-acetyl-D-glucosamine (GlcNAc)-containing Lancefield gr
48 in NOD mice by promoting clonal expansion of N-acetyl-d-glucosamine (GlcNAc)-specific B-1 B cells tha
49 rolyze chitin, a polymer of beta-1, 4-linked N-acetyl-D-glucosamine (GlcNAc).
50 ating disaccharides of D-glucuronic acid and N-acetyl-D-glucosamine (GlcNAc).
51 ndent lectin and its T cell-binding partner, N-acetyl-D-glucosamine (GlcNAc).
52 p adhesin from the F17 pilus that recognizes n-acetyl-d-glucosamine (GlcNAc).
53 -60%, heparan sulfate by approximately 35%), N-acetyl-d-glucosamine (GlcNAc)/GalNAc containing glycan
54 patterns of appropriate carbohydrates (e.g., N-acetyl-d-glucosamine, GlcNAc) enable selective, multiv
55     Biologically-relevant mannose- (Man) and N-acetyl-D-glucosamine- (GlcNAc) containing di-, tri-, t
56                         Chitin, a polymer of N-acetyl-d-glucosamine, is found in fungal cell walls bu
57 F6 using a panel of Le(x) analogues in which N-acetyl-d-glucosamine, l-fucose, or d-galactose (D-Gal)
58 etion of these cells was studied using a [3H]N-acetyl-D-glucosamine labeling assay, and the stimulati
59                            Because growth on N-acetyl-D-glucosamine likely reflects the ability of a
60 d of alternating residues of d-galactose and N-acetyl-d-glucosamine linked beta-(1-4) and beta-(1-3),
61           Fucoidin, heparin/heparin sulfate, N-acetyl-D-glucosamine, mannose-6-phosphate, and laminar
62 with modifications consisting of an N-linked N-acetyl-D-glucosamine monosaccharide (N-GlcNAc).
63 activity was observed with other sugars like N-acetyl-D-glucosamine, N-acetyl-D-galactosamine, D-gluc
64 t, mushroom, seaweed, or barley, but also by N-acetyl-D-glucosamine (NADG), alpha- or beta-methylmann
65  analogues N-acetyl-D-mannosamine (NADM) and N-acetyl-D-glucosamine (NADG).
66 -3) beta-N-acetyl-D-glucosamine (1-] with an N-acetyl-D-glucosamine nonreducing terminus.
67 GA) is the only enzyme that removes O-linked N-acetyl-d-glucosamine (O-GlcNAc) from target proteins.
68  and mitochondrial proteins by O-linked beta-N-acetyl-D-glucosamine (O-GlcNAc) has been shown to regu
69 on and increased deposition of O-linked beta-N-acetyl-d-glucosamine (O-GlcNAc) in cardiac proteins ar
70                                       beta-O-N-acetyl-D-glucosamine (O-GlcNAc) is a post-translationa
71  infection, NleB functions as a translocated N-acetyl-D-glucosamine (O-GlcNAc) transferase that modif
72 he polysaccharide adhesin PGA (poly-beta-1,6-N-acetyl-d-glucosamine) of Escherichia coli, is the key
73 eta3 integrins were effectively inhibited by N-acetyl-D-glucosamine on extracellular matrix-coated su
74             Incubating human serum (HS) with N-acetyl-D-glucosamine or anti-human MBL monoclonal anti
75 )) human endothelial cells was attenuated by N-acetyl-D-glucosamine or D-mannose, but not L-mannose,
76  of the polysaccharide adhesin poly-beta-1,6-N-acetyl-D-glucosamine (PGA) by binding to the pgaABCD m
77 duction of the biofilm adhesin poly-beta-1,6-N-acetyl-d-glucosamine (PGA).
78 ation of the exopolysaccharide poly-beta-1,6-N-acetyl-d-glucosamine (PNAG) by the extracellular prote
79 ation of the exopolysaccharide poly-beta-1,6-N-acetyl-D-glucosamine (PNAG) by the periplasmic protein
80                                Poly-beta-1,6-N-acetyl-D-glucosamine (PNAG) is an exopolysaccharide pr
81 gth-dependent deacetylation on poly-beta-1,6-N-acetyl-d-glucosamine (PNAG) oligomers, supporting prev
82                   A beta-(1-->6)-linked poly-N-acetyl-d-glucosamine (PNAG) surface capsule is synthes
83  a second antigen, a beta-(1-->6)-polymer of N-acetyl-D-glucosamine (PNAG).
84                           Polymeric beta-1,6-N-acetyl-D-glucosamine (poly-beta-1,6-GlcNAc) has been i
85 lly cleaves the polysaccharide poly-beta-1,6-N-acetyl-D-glucosamine (poly-beta-1,6-GlcNAc), we provid
86  to 10-microm chitin particles (nonantigenic N-acetyl-D-glucosamine polymers) is known to induce inna
87 d with phagocytosable-size chitin particles (N-acetyl-D-glucosamine polymers).
88 odulated by two enzymes: uridine diphosphate-N-acetyl-D-glucosamine:polypeptidyltransferase (OGT) and
89 eding paper, a series of novel O-6 phosphate N-acetyl (d)-glucosamine prodrugs aimed at improving the
90 overted to the UDP derivative with yeast UDP-N-acetyl-D-glucosamine pyrophosphorylase.
91 i biofilm matrix is PGA, a linear polymer of N-acetyl-D-glucosamine residues in beta(1,6) linkage.
92 catalyzes the deacetylation and sulfation of N-acetyl-D-glucosamine residues of heparan sulfate, a ke
93 e, TarS, that attaches beta-O-GlcNAc (beta-O-N-acetyl-D-glucosamine) residues to S. aureus WTAs.
94 lidene)amino N-phenyl carbamate (GalPUGNAc), N-acetyl-D-glucosamine-thiazoline (NGT), and N-acetyl-D-
95 exploited the ADAMTS-5 binding capacity of B-N-acetyl-D-glucosamine to design a new class of sugar-ba
96 transferase that modifies host proteins with N-acetyl-d-glucosamine to inhibit antibacterial and infl
97  be formed from core-1 by the core-2 beta1,6 N-acetyl-d-glucosamine transferase (beta1,6 GlcNAc T) th
98 hibited 58% amino acid identity with the UDP-N-acetyl-D-glucosamine (UDP-GlcNAc) 2-epimerase of Esche
99 )C isotopologue data for uridine diphosphate N-acetyl-D-glucosamine (UDP-GlcNAc) in human prostate ca
100  proposed to occur by 4,6-dehydration of UDP-N-acetyl-d-glucosamine (UDP-GlcNAc) to UDP-2-acetamido-2
101 n of the 3'' position of uridine diphosphate N-acetyl-D-glucosamine (UDP-GlcNAc), forming a 3-hexulos
102 is beginning with uridine dinucleotide (UDP)-N-acetyl-d-glucosamine (UDP-GlcNAc).
103 lidinone-protected derivative of 1-tolylthio-N-acetyl-D-glucosamine undergoes high-yield glycosidatio
104 cheri directly regulates several chitin- and N-acetyl-D-glucosamine-utilization genes that are co-reg
105 ugars in length engaged the lectin site, and N-acetyl D-glucosamine was not a required component mono
106                                      Because N-acetyl-D-glucosamine was found previously to inhibit b
107 he biofilm seems to contain a homopolymer of N-acetyl-d-glucosamine, which is a constituent of many b

 
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