ライフサイエンスコーパス: N-acetyl-D-glucosamine

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 ucuronic acid, N-acetyl-d-galactosamine, and N-acetyl-d-glucosamine, and all except mannose were redu

21 hibitors such as alloxan, D-glucosamine, and N-acetyl-D-glucosamine, and mimicked by the non-metaboli

22 inase inhibitors alloxan, d-glucosamine, and N-acetyl-d-glucosamine; and 4) orexin glucosensors detec

23 med at improving the oral bioavailability of N-acetyl-(d)-glucosamine as its putative bioactive phosp

24 nt failed to develop biofilms when utilizing N-acetyl-D-glucosamine as a carbon source.

25 ses on the O-3 and O-4 phosphate prodrugs of N-acetyl-(d)-glucosamine bearing a 4-methoxy phenyl grou

26 The linear homopolymer poly-beta-1,6-N-acetyl-D-glucosamine (beta-1,6-GlcNAc; PGA) serves as

27 proteins known to synthesize a poly-beta-1,6-N-acetyl-D-glucosamine biofilm matrix.

28 luding L-fucose, D-gluconate, D-glucuronate, N-acetyl-D-glucosamine, D-mannose, and D-ribose.

29 lacking the polysaccharide adhesin beta-1,6-N-acetyl-d-glucosamine (DeltapgaC) also exhibited aperio

30 N-acetyl-d-glucosamine did not inhibit sCR1-MBL binding,

31 N-acetyl-D-glucosamine disrupted CR3 clusters and sinuso

32 The remaining four bands were present in N-acetyl-D-glucosamine eluates, although their % distrib

33 ssii involves chemotaxis to and transport of N-acetyl-D-glucosamine (GlcNAc) and D-glucose.

34 The monosaccharide N-acetyl-d-glucosamine (GlcNAc) is an abundant building

35 odifications of serine and threonine by beta-N-acetyl-D-glucosamine (GlcNAc) may regulate muscle cont

36 es encoding cytoplasmic proteins involved in N-acetyl-D-glucosamine (GlcNAc) metabolism.

37 HGAC 39.G3 binding to an antigen displaying N-acetyl-d-glucosamine (GlcNAc) residues on a polyrhamno

38 HEMA modified with N-acetyl-D-glucosamine (GlcNAc) was also polymerized to

39 Another major finding was that N-acetyl-D-glucosamine (GlcNAc) which does not inhibit a

40 has been identified as a molecular mimic of N-acetyl-D-glucosamine (GlcNAc), a known ligand of MBL.

41 ating disaccharides of D-glucuronic acid and N-acetyl-D-glucosamine (GlcNAc).

42 p adhesin from the F17 pilus that recognizes n-acetyl-d-glucosamine (GlcNAc).

43 rolyze chitin, a polymer of beta-1, 4-linked N-acetyl-D-glucosamine (GlcNAc).

44 -60%, heparan sulfate by approximately 35%), N-acetyl-d-glucosamine (GlcNAc)/GalNAc containing glycan

45 Chitin, a polymer of N-acetyl-d-glucosamine, is found in fungal cell walls bu

46 etion of these cells was studied using a [3H]N-acetyl-D-glucosamine labeling assay, and the stimulati

47 Because growth on N-acetyl-D-glucosamine likely reflects the ability of a

48 d of alternating residues of d-galactose and N-acetyl-d-glucosamine linked beta-(1-4) and beta-(1-3),

49 Fucoidin, heparin/heparin sulfate, N-acetyl-D-glucosamine, mannose-6-phosphate, and laminar

50 with modifications consisting of an N-linked N-acetyl-D-glucosamine monosaccharide (N-GlcNAc).

51 activity was observed with other sugars like N-acetyl-D-glucosamine, N-acetyl-D-galactosamine, D-gluc

52 t, mushroom, seaweed, or barley, but also by N-acetyl-D-glucosamine (NADG), alpha- or beta-methylmann

53 -3) beta-N-acetyl-D-glucosamine (1-] with an N-acetyl-D-glucosamine nonreducing terminus.

54 and mitochondrial proteins by O-linked beta-N-acetyl-D-glucosamine (O-GlcNAc) has been shown to regu

55 on and increased deposition of O-linked beta-N-acetyl-d-glucosamine (O-GlcNAc) in cardiac proteins ar

56 beta-O-N-acetyl-D-glucosamine (O-GlcNAc) is a post-translationa

57 infection, NleB functions as a translocated N-acetyl-D-glucosamine (O-GlcNAc) transferase that modif

58 he polysaccharide adhesin PGA (poly-beta-1,6-N-acetyl-d-glucosamine) of Escherichia coli, is the key

59 eta3 integrins were effectively inhibited by N-acetyl-D-glucosamine on extracellular matrix-coated su

60 Incubating human serum (HS) with N-acetyl-D-glucosamine or anti-human MBL monoclonal anti

61 )) human endothelial cells was attenuated by N-acetyl-D-glucosamine or D-mannose, but not L-mannose,

62 of the polysaccharide adhesin poly-beta-1,6-N-acetyl-D-glucosamine (PGA) by binding to the pgaABCD m

63 duction of the biofilm adhesin poly-beta-1,6-N-acetyl-d-glucosamine (PGA).

64 ation of the exopolysaccharide poly-beta-1,6-N-acetyl-d-glucosamine (PNAG) by the extracellular prote

65 ation of the exopolysaccharide poly-beta-1,6-N-acetyl-D-glucosamine (PNAG) by the periplasmic protein

66 Poly-beta-1,6-N-acetyl-D-glucosamine (PNAG) is an exopolysaccharide pr

67 gth-dependent deacetylation on poly-beta-1,6-N-acetyl-d-glucosamine (PNAG) oligomers, supporting prev

68 A beta-(1-->6)-linked poly-N-acetyl-d-glucosamine (PNAG) surface capsule is synthes

69 a second antigen, a beta-(1-->6)-polymer of N-acetyl-D-glucosamine (PNAG).

70 Polymeric beta-1,6-N-acetyl-D-glucosamine (poly-beta-1,6-GlcNAc) has been i

71 lly cleaves the polysaccharide poly-beta-1,6-N-acetyl-D-glucosamine (poly-beta-1,6-GlcNAc), we provid

72 to 10-microm chitin particles (nonantigenic N-acetyl-D-glucosamine polymers) is known to induce inna

73 d with phagocytosable-size chitin particles (N-acetyl-D-glucosamine polymers).

74 odulated by two enzymes: uridine diphosphate-N-acetyl-D-glucosamine:polypeptidyltransferase (OGT) and

75 eding paper, a series of novel O-6 phosphate N-acetyl (d)-glucosamine prodrugs aimed at improving the

76 overted to the UDP derivative with yeast UDP-N-acetyl-D-glucosamine pyrophosphorylase.

77 i biofilm matrix is PGA, a linear polymer of N-acetyl-D-glucosamine residues in beta(1,6) linkage.

78 catalyzes the deacetylation and sulfation of N-acetyl-D-glucosamine residues of heparan sulfate, a ke

79 e, TarS, that attaches beta-O-GlcNAc (beta-O-N-acetyl-D-glucosamine) residues to S. aureus WTAs.

80 lidene)amino N-phenyl carbamate (GalPUGNAc), N-acetyl-D-glucosamine-thiazoline (NGT), and N-acetyl-D-

81 transferase that modifies host proteins with N-acetyl-d-glucosamine to inhibit antibacterial and infl

82 be formed from core-1 by the core-2 beta1,6 N-acetyl-d-glucosamine transferase (beta1,6 GlcNAc T) th

83 hibited 58% amino acid identity with the UDP-N-acetyl-D-glucosamine (UDP-GlcNAc) 2-epimerase of Esche

84 proposed to occur by 4,6-dehydration of UDP-N-acetyl-d-glucosamine (UDP-GlcNAc) to UDP-2-acetamido-2

85 n of the 3'' position of uridine diphosphate N-acetyl-D-glucosamine (UDP-GlcNAc), forming a 3-hexulos

86 lidinone-protected derivative of 1-tolylthio-N-acetyl-D-glucosamine undergoes high-yield glycosidatio

87 cheri directly regulates several chitin- and N-acetyl-D-glucosamine-utilization genes that are co-reg

88 ugars in length engaged the lectin site, and N-acetyl D-glucosamine was not a required component mono

89 Because N-acetyl-D-glucosamine was found previously to inhibit b

90 he biofilm seems to contain a homopolymer of N-acetyl-d-glucosamine, which is a constituent of many b