ライフサイエンスコーパス: GlcNAc

1 GlcNAc is a rate-limiting metabolite for N-glycan branch

2 GlcNAc, in the form of UDP-GlcNAc, and galactose, as UDP

3 GlcNAc-reactive B-1 clonotypes and serum antibodies were

4 cognition driven by interactions with the -1 GlcNAc residue in the catalytic pocket.

5 hybrid glycans with the composition Gal(0-1)GlcNAc(1)Man(3-5)GlcNAc(2)Fuc(0-1) were confirmed as the

6 Chinese hamster ovary cells with the core 2 GlcNAc transferase acting on a mucin-type O-glycoprotein

7 ctosylated structure with core fucose (Gal(2)GlcNAc(2)Man(3)GlcNAc(2)Fuc), and a group of hybrid glyc

8 Starting from a Kdo(2)GlcNAc(2) tetrasaccharide precursor, a central orthogona

9 GlcNAcMan(5)GlcNAc(2) to produce GlcNAcMan(3)GlcNAc(2), the precursor for all complex N-glycans, incl

10 The syntheses of beta-S-GlcA(1->3)GlcNAc and beta-S-Gal(1->3)GlcNAc thiodisaccharides, whi

11 beta-S-GlcA(1->3)GlcNAc and beta-S-Gal(1->3)GlcNAc thiodisaccharides, which can be considered mimeti

12 cture with core fucose (Gal(2)GlcNAc(2)Man(3)GlcNAc(2)Fuc), and a group of hybrid glycans with the co

13 ically utilizes lacto-N-biose I (Gal-beta1,3-GlcNAc) and galacto-N-biose (Gal-beta1,3-GalNAc) from hu

14 ick cells showed that paucimannose (Man(3-4) GlcNAc(2)Fuc(0-1)) and high-mannose structures with five

15 samine (LacNAc), and unnatural Galalpha(1,4)-GlcNAc and Manbeta(1,4)-GlcNAc appendages.

16 atural Galalpha(1,4)-GlcNAc and Manbeta(1,4)-GlcNAc appendages.

17 mer of App serotype 1 (App1) consists of [4)-GlcNAc-beta(1,6)-Gal-alpha-1-(PO(4)-] repeating units th

18 ith the composition Gal(0-1)GlcNAc(1)Man(3-5)GlcNAc(2)Fuc(0-1) were confirmed as the main asparagine-

19 is of two mannosyl residues from GlcNAcMan(5)GlcNAc(2) to produce GlcNAcMan(3)GlcNAc(2), the precurso

20 doBT-3987-Man(9)GlcNAc and EndoBT-3987-Man(5)GlcNAc product complexes.

21 consists of oligomannose sugars, with Man(5)GlcNAc(2) being the most abundant, and a few hybrid-type

22 ose glycan with five mannose residues (Man(5)GlcNAc(2)), a complex biantennary galactosylated structu

23 GAT4D-L causes the substrate of MGAT1 (Man(5)GlcNAc(2)Asn) to accumulate on glycoproteins, a change t

24 ructures with five and six mannoses (Man(5-6)GlcNAc(2)) were major glycans on the viral surface.

25 cogenes, we discovered novel Glc(0-2)-Man(6)-GlcNAc(2)-type N-glycans, a novel HexNAc-GalNAc-mucin-ty

26 cosylated sulfoglycans containing sulfated-6-GlcNAc and sulfated-4-GalNAc residues.

27 GalNAc-GlcNAc of sulfated-3-Gal, sulfated-6-GlcNAc, and sulfated-4-GalNAc.

28 substrate complex, and two EndoBT-3987-Man(9)GlcNAc and EndoBT-3987-Man(5)GlcNAc product complexes.

29 ked glycans are synthesized from Glc(3)Man(9)GlcNAc(2) precursors that are trimmed and modified in th

30 g the unliganded form, the EndoBT-3987-Man(9)GlcNAc(2)Asn substrate complex, and two EndoBT-3987-Man(

31 e active site that specifically accommodates GlcNAc in alpha(1,6)-linkages, suggest that enzymatic ac

32 glucosamine moieties are either acetylated (GlcNAc) or modified as a free amine (GlcNH(2) ) or Boc (

33 smic proteins with beta-N-acetylglucosamine (GlcNAc) and regulates numerous biological processes.

34 igh value nutraceutical N-acetylglucosamine (GlcNAc) could be balanced and optimized in Bacillus subt

35 t of P. aeruginosa with N-acetylglucosamine (GlcNAc), a widespread chemical present on the surface of

36 tennary glycan that has N-acetylglucosamine (GlcNAc), N-acetyllactosamine (LacNAc), and unnatural Gal

37 response to the inducer N-acetylglucosamine (GlcNAc), suggesting that a basal level of cAMP is suffic

38 ) type] terminated with N-acetylglucosamine (GlcNAc), which is generated by N-acetylglucosaminyltrans

39 monstrated that certain N-acetylglucosamine (GlcNAc)-containing polysaccharides can stabilize poliovi

40 d by the monosaccharide N-acetylglucosamine (GlcNAc).

41 at the 6-O-sulfation of N-acetylglucosamine (GlcNAc-6-O-sulfation) is highly conserved in PNS myelin

42 +128.1 Da), and loss of N-acetylglucosamine (GlcNAc; -203.1 Da).

43 acetylmannosamine-bound and substrate analog GlcNAc-bound crystal structures (2.33, 2.20, and 2.20 an

44 omeric oligomer groups, GlcNAc(1)GlcN(3) and GlcNAc(2)GlcN(2), sufficed to identify, in a directed ev

45 Our data identify N-glycan branching and GlcNAc as critical regulators of primary myelination and

46 by the GlcNAc-phosphate transferase GacO and GlcNAc-phosphate-undecaprenol (GlcNAc-P-Und) produced by

47 rms UDP-GlcNAc, the moiety for O-linked beta-GlcNAc (O-GlcNAc) post-translational modifications.

48 reonine protein glycosylation (O-linked beta-GlcNAc; O-GlcNAc) that occurs on thousands of proteins w

49 ld be obtained by removal of a terminal beta-GlcNAc moiety by treatment with beta-N-acetylglucosamini

50 Fifteen N-glycan compositions with bisecting GlcNAc, sialic acid, and core fucosylation showed signif

51 ystal structures of salmon calcitonin-bound, GlcNAc-bearing CTR ECD at 1.78 and 2.85 angstrom resolut

52 in SLC35A3-knockout HEK293T and HepG2 cells, GlcNAc was still incorporated into O-glycans.

53 that GacB is the first characterized alpha-d-GlcNAc-beta-1,4-l-rhamnosyltransferase that synthesizes

54 The addition of a single beta-d-GlcNAc sugar (O-GlcNAc) by O-GlcNAc-transferase (OGT) an

55 gand-docking simulations to analyze the dual GlcNAc- and MurNAc-binding specificities of BsPdaC and c

56 to deacetylation of all but the reducing-end GlcNAc residues.

57 henotypes that could be rescued by exogenous GlcNAc, the product of the Gna1 enzyme.

58 esult in specific, high-affinity binding for GlcNAc.

59 ptidoglycan deacetylases highly specific for GlcNAc or MurNAc residues, respectively.

60 sialylatable lacto-N-neotetraose (LNnT; Gal-GlcNAc-Gal-Glc) moiety from heptose I (HepI) of the lipo

61 lanked by a terminal sulfation sequon on Gal-GlcNAc and GalNAc-GlcNAc of sulfated-3-Gal, sulfated-6-G

62 al sulfation sequon on Gal-GlcNAc and GalNAc-GlcNAc of sulfated-3-Gal, sulfated-6-GlcNAc, and sulfate

63 rotein substrates with N-acetyl glucosamine (GlcNAc) on arginine residues.

64 high-affinity ligand N-acetyl-d-glucosamine (GlcNAc) binds in the collectin CRD calcium site by inter

65 n of isopropyl N-acetyl-alpha-d-glucosamine (GlcNAc) is used to prepare the rare sugars allosamine, l

66 ls reactive with the N-acetyl-D-glucosamine (GlcNAc)-containing Lancefield group A carbohydrate of St

67 ell-binding partner, N-acetyl-D-glucosamine (GlcNAc).

68 sities of just two isomeric oligomer groups, GlcNAc(1)GlcN(3) and GlcNAc(2)GlcN(2), sufficed to ident

69 e other MurNAc deacetylases, BsPdaC also has GlcNAc deacetylase activity on chitooligosaccharides (CO

70 Fucosylation of the innermost GlcNAc of N-glycans by fucosyltransferase 8 (FUT8) is an

71 y alpha-1,6-fucose addition to the innermost GlcNAc residue (core fucosylation) is catalyzed by an al

72 ecaprenol-linked GlcNAc-lipid intermediates: GlcNAc-pyrophosphoryl-undecaprenol (GlcNAc-P-P-Und) prod

73 ple-chain mechanism starting at the internal GlcNAc units and leading to deacetylation of all but the

74 We found that the minimal substrate is GlcNAc(3) and that activity increases with the degree of

75 The Passerini reaction applied on 3-keto-GlcNAc provides an entry into branching of the carbon sk

76 fucose moiety specifically at the Asn-linked GlcNAc moiety not only to GlcNAc-peptide but also to hig

77 is requires two distinct undecaprenol-linked GlcNAc-lipid intermediates: GlcNAc-pyrophosphoryl-undeca

78 irion stabilization required binding of long GlcNAc polymers of greater than 20 units.

79 CD23 demonstrate that they bind to mannose, GlcNAc, glucose, and fucose and to glycoproteins that be

80 FQ sequence also occurs in MGAT4A and MGAT4B GlcNAc-transferases.

81 stabilized a beta-sheet adjacent to the N130 GlcNAc and the N-terminal alpha-helix near the peptide-b

82 The N130 GlcNAc does not contact the hormone.

83 UDP-4-N3-GlcNAc served as a chain termination substrate for hyalu

84 n or heparosan synthases; the resulting 4-N3-GlcNAc-terminated hyaluronan and heparosan were then suc

85 resulted in only modification of the natural GlcNAc moieties, providing access to 6 selectively mono-

86 cNH(2) or GlcNHBoc moieties into the natural GlcNAc, followed by sialylation by sialyl transferases g

87 O-GlcNAc also has extensive cross-talk with phosphorylatio

88 O-GlcNAc is an abundant post-translational modification fo

89 O-GlcNAc is generally not elongated or modified.

90 O-GlcNAc signaling is down-regulated during macrophage pro

91 O-GlcNAc transferase (OGT) is an X-linked gene product tha

92 O-GlcNAc transferase (OGT) is responsible for the addition

93 O-GlcNAc transferase (OGT) regulates a wide range of cellu

94 O-GlcNAc-deficient Treg cells develop normally but display

95 his approach, we target an elusive Ser 405 O-GlcNAc site on OGA, showing that this site-specific modi

96 tion of O-linked beta-N-acetylglucosamine (O-GlcNAc) groups to proteins important for axonal and syna

97 modification O-linked N-Acetylglucosamine (O-GlcNAc) has emerged as an attractive target for regulati

98 rboring O-linked beta-N-acetylglucosamine (O-GlcNAc) hydrolase and cryptic lysine acetyltransferase a

99 tion by O-linked beta-N-acetylglucosamine (O-GlcNAc) moieties.

100 cation by beta-linked N-acetylglucosamine (O-GlcNAc) on HDAC4 were investigated in vivo and in vitro

101 e mapping of O-linked N-acetylglucosamine (O-GlcNAc) post-translational modification (PTM) sites in p

102 of the O-linked beta-N-acetylglucosamine (O-GlcNAc) signaling associated with the hexosamine biosynt

103 sensing O-linked beta-N-acetylglucosamine (O-GlcNAc) signaling in suppressing macrophage proinflammat

104 ification by O-linked N-Acetylglucosamine (O-GlcNAc) stabilizes FOXP3 and activates STAT5, thus integ

105 rotein by transfer of N-acetylglucosamine (O-GlcNAc) to serine and threonine hydroxyls.

106 cation, O-linked beta-N-acetylglucosamine (O-GlcNAc), in NSCs promotes a glial fate switch.

107 phorylation, and both the enzyme that adds O-GlcNAc, the O-GlcNAc transferase (OGT), and the enzyme t

108 cNAc transferase (Ogt), which catalyzes an O-GlcNAc-modification onto key target proteins, integrates

109 -GlcNAc) by O-GlcNAc-transferase (OGT) and O-GlcNAc removal by O-GlcNAcase (OGA) maintain homeostatic

110 hexosamine biosynthetic pathway (HBP) and O-GlcNAc transferase (OGT) for Drosophila homeodomain-inte

111 While in animals, O-GlcNAc transferase (OGT) modifies thousands of intracell

112 ChIP-sequencing experiments using an anti-O-GlcNAc antibody revealed significant chromatin enrichmen

113 This modification, known as O-GlcNAc, has emerged as a central regulator of both cell

114 e genes encode enzymes for its attachment (O-GlcNAc transferase (OGT)) and removal (O-GlcNAcase (OGA)

115 , to determine the consequences of blocked O-GlcNAc cycling on HSCs.

116 ubstrate for glycosylation, increased both O-GlcNAc and leptin, whereas inhibition of O-glycosyltrans

117 Both O-GlcNAc cycling enzymes are essential in mammals and plan

118 control mRNA abundance in order to buffer O-GlcNAc changes.

119 f Hippo pathway (YAP) is O-GlcNAcylated by O-GlcNAc transferase (OGT) at serine 109.

120 Suppressing O-GlcNAc signaling by O-GlcNAc transferase (OGT) knockout enhances macrophage pr

121 asmic proteins with O-GlcNAc, catalyzed by O-GlcNAc transferase (OGT), is an abundant posttranslation

122 ich facilitates O-GlcNAcylation of PKM2 by O-GlcNAc transferase (OGT).

123 igenetic regulation of MYBL1 expression by O-GlcNAc, thereby significantly affecting tumor progressio

124 f colorectal adenocarcinoma progression by O-GlcNAc, we have focused on the O-GlcNAc-mediated epigene

125 a single beta-d-GlcNAc sugar (O-GlcNAc) by O-GlcNAc-transferase (OGT) and O-GlcNAc removal by O-GlcNA

126 ous post-translational modification called O-GlcNAc, which is thought to integrate signaling pathways

127 including site-directed mutagenesis, Click O-GlcNAc labeling, immunoblotting, and immunofluorescence

128 tify a set of endogenous cotranslationally O-GlcNAc modified proteins.

129 n of O-glycosyltransferase (OGT) decreased O-GlcNAc and leptin.

130 port that countering age-related decreased O-GlcNAc transferase (OGT) expression and O-GlcNAcylation

131 ariety of cellular processes, and elevated O-GlcNAc levels have been implicated in cancer progression

132 ced obesity murine model and that elevated O-GlcNAc levels increase IL-17A production.

133 not possible without affecting the entire O-GlcNAc proteome.

134 othesized that the nutrient-sensing enzyme O-GlcNAc transferase (Ogt), which catalyzes an O-GlcNAc-mo

135 A single essential enzyme, O-GlcNAc transferase (OGT), is responsible for all nucleoc

136 on is established by two opposing enzymes: O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).

137 o show that the pan-selective antibody for O-GlcNAc does not generally recognize this modification on

138 in cancer and suggests a crucial role for O-GlcNAc signaling in transducing nutritional state to reg

139 tors of the enzyme that installs O-GlcNAc (O-GlcNAc transferase, or OGT) and the enzyme that removes

140 cNAc, the moiety for O-linked beta-GlcNAc (O-GlcNAc) post-translational modifications.

141 otein glycosylation (O-linked beta-GlcNAc; O-GlcNAc) that occurs on thousands of proteins within the

142 he enzyme that catalyzes O-GlcNAcylation - O-GlcNAc-transferase (OGT), and the extent of protein O-Gl

143 GlcNAc residue) from tau, increases global O-GlcNAc levels within the brain and reduces tau phosphory

144 t removes O-linked N-acetyl-d-glucosamine (O-GlcNAc) from target proteins.

145 lation.O-linked beta-N-acetyl glucosamine (O-GlcNAc) is an important protein modification that is hyd

146 ll as in vitro under high-glucose and high-O-GlcNAc conditions.

147 by O-GlcNAcase (OGA) maintain homeostatic O-GlcNAc levels on cellular proteins.

148 searchers seeking to better understand how O-GlcNAc influences stemness and may catalyze the discover

149 Here we show an acute increase in O-GlcNAc dampens GABAergic currents onto principal cells i

150 l dysfunction and systemic inflammation in O-GlcNAc deficient mice.

151 ing adaptability and specificity to OGA in O-GlcNAc regulation.O-linked beta-N-acetyl glucosamine (O-

152 Overnutrition stimulates an increase in O-GlcNAc signaling in macrophages.

153 The overall effect of increased O-GlcNAc is reduced synaptically-driven spike probability

154 d homozygous deletion, exhibited increased O-GlcNAc levels in adipose tissue and increased leptin lev

155 fic inhibitors of the enzyme that installs O-GlcNAc (O-GlcNAc transferase, or OGT) and the enzyme tha

156 try analyses reveal that HIPK2 is at least O-GlcNAc modified at S852, T1009, and S1147 residues.

157 These findings thus identify macrophage O-GlcNAc signaling as a homeostatic mechanism maintaining

158 between the posttranslational modification O-GlcNAc and protein aggregation.

159 le for the post-translational modification O-GlcNAc as a critical nutrient signal in these cells.

160 , post-translational protein modification, O-GlcNAc, are present in naive CD4(+) T cells from a diet-

161 entify the posttranslational modification, O-GlcNAc, as a key molecular regulator of regenerative dec

162 CCSC compartment observed after modulating O-GlcNAc levels is therefore likely to result, at least in

163 yme involved in removal of a sugar moiety (O-GlcNAc residue) from tau, increases global O-GlcNAc leve

164 We detect an age-dependent decrease in NSC O-GlcNAc levels coincident with decreased neurogenesis and

165 ies directed at understanding the roles of O-GlcNAc and other cotranslational protein modifications a

166 A key emerging function of O-GlcNAc appears to be to regulate cellular protein homeos

167 e loss of DNA methylation caused a loss of O-GlcNAc from multiple transcriptional repressor proteins

168 e an improved understanding of the role of O-GlcNAc in cytoplasmic protein quality control and proteo

169 While speculation exists about the role of O-GlcNAc in neurodegenerative conditions, such as Alzheime

170 Unlike the critical role of O-GlcNAc in regulating the animal circadian clock, here we

171 enable robust and precise localization of O-GlcNAc sites.

172 dels to evaluate the beneficial effects of O-GlcNAc stimulation at the early phase of septic shock.

173 ly stable and accurate structural mimic of O-GlcNAc that can be encoded in mammalian systems with CRI

174 In this study, we probed the importance of O-GlcNAc transferase (OGT) activity for the survival of ta

175 xpectedly, many transcriptional effects of O-GlcNAc transferase (OGT) inhibition were due to the acti

176 Deletion of O-GlcNAc transferase (OGT), a key enzyme for protein O-Glc

177 sed editing method for targeted removal of O-GlcNAc was directed against retrotransposon promoters.

178 n overview of our current understanding of O-GlcNAc's regulation, functions, and roles in chronic dis

179 vealed significant chromatin enrichment of O-GlcNAc-modified proteins at the promoter of the transcri

180 Furthermore, our results reveal that OGT O-GlcNAc-modifies eIF4G1 at Ser-61 and that this modificat

181 at during G1E-ER4 differentiation, overall O-GlcNAc levels decrease, and physical interactions of GAT

182 erase, or OGT) and the enzyme that removes O-GlcNAc (O-GlcNAcase, or OGA), we first show that O-GlcNA

183 sferase (OGT), and the enzyme that removes O-GlcNAc, O-GlcNAcase (OGA), are highly conserved from C.

184 enetic deletion of the enzyme that removes O-GlcNAc, O-GlcNAcase (OGA), to determine the consequences

185 Polyhomeotic confirmed previously reported O-GlcNAc sites in TAB1 (S395 and S396) and uncovered new s

186 he O-GlcNAc-cycling genes fails to restore O-GlcNAc homeostasis, there is a global change in detained

187 study, we demonstrate that in septic shock O-GlcNAc stimulation improves global animal and cardiovasc

188 ise functional dissection of site-specific O-GlcNAc modification in vivo is currently not possible wi

189 enesis approach, we identify loss of STAT3 O-GlcNAc at Threonine 717 as a driver of astrocyte differe

190 addition of a single beta-d-GlcNAc sugar (O-GlcNAc) by O-GlcNAc-transferase (OGT) and O-GlcNAc remov

191 Suppressing O-GlcNAc signaling by O-GlcNAc transferase (OGT) knockout

192 indicate a unique potential for targeting O-GlcNAc signaling in the treatment of obesity.

193 o a simple version of glycosylation termed O-GlcNAc modification.

194 Our results demonstrate that O-GlcNAc controls detained intron splicing to tune system-

195 These findings suggest that O-GlcNAc cycling plays a critical role in supporting HSC h

196 s from several laboratories has shown that O-GlcNAc cycling serves as a nutrient sensor to regulate s

197 ty of biochemical experiments to show that O-GlcNAc in general inhibits the aggregation of alpha-synu

198 This raises the possibility that O-GlcNAc may alter the aggregation of this protein and cou

199 , using overexpressed model proteins, that O-GlcNAc modification can occur cotranslationally and that

200 (O-GlcNAcase, or OGA), we first show that O-GlcNAc regulates splicing of the highly conserved detain

201 y sequence (10-15 amino acids) between the O-GlcNAc and the site of cleavage.

202 and PTH in serum despite the fact that the O-GlcNAc can be quite remote from characterized sites of p

203 iving thiamet G (TMG), an inhibitor of the O-GlcNAc hydrolase O-GlcNAcase, exhibited enhanced retinal

204 iving thiamet G (TMG), an inhibitor of the O-GlcNAc hydrolase O-GlcNAcase, exhibited enhanced retinal

205 ic pathway (HBP) ultimately leading to the O-GlcNAc modification of critical intracellular targets.

206 These findings link the O-GlcNAc modification to mammalian neurogenesis and highli

207 It catalyses the O-GlcNAc posttranslational modification of nucleocytoplasm

208 ot clear if this is through changes in the O-GlcNAc proteome, loss of protein-protein interactions, o

209 la genome results in global changes in the O-GlcNAc proteome, while in mouse embryonic stem cells it

210 experiments also show that several of the O-GlcNAc sites inhibit the toxicity of extracellular alpha

211 ular processes through the addition of the O-GlcNAc sugar moiety to thousands of protein substrates.

212 nd both the enzyme that adds O-GlcNAc, the O-GlcNAc transferase (OGT), and the enzyme that removes O-

213 Caenorhabditis elegans and identified the O-GlcNAc transferase OGT-1 as an EEL-1 binding protein.

214 O-fucosyltransferase SPINDLY (SPY) and the O-GlcNAc transferase SECRET AGENT (SEC) are two prominent

215 We also show that when DI splicing of the O-GlcNAc-cycling genes fails to restore O-GlcNAc homeostas

216 ession by O-GlcNAc, we have focused on the O-GlcNAc-mediated epigenetic regulation of human colon can

217 , an alpha-synuclein protein bearing three O-GlcNAc modifications can inhibit the aggregation of unmo

218 sor could modulate gene expression through O-GlcNAc modification of histones or other proteins in res

219 inputs to gene regulatory pathways through O-GlcNAc-mediated epigenetic/transcriptional regulatory me

220 Due to O-GlcNAc's fundamental roles as a nutrient and stress sens

221 utGT treatment efficiently increased total O-GlcNAc without modification of HBP enzyme expression.Tre

222 oring the importance of post-translational O-GlcNAc modification in general cell physiology.

223 erformance and accuracy of the assay using O-GlcNAc transferase (OGT) as a model system through detai

224 Moreover, using O-GlcNAc-specific mass spectrometry analysis of the aging

225 introns are spliced more efficiently when O-GlcNAc levels are low, yet other alternative splicing pa

226 at are cotranslationally glycosylated with O-GlcNAc by metabolic saccharide engineering using tetra-O

227 esidues of nucleocytoplasmic proteins with O-GlcNAc, catalyzed by O-GlcNAc transferase (OGT), is an a

228 nd fluid resuscitation (R) with or without O-GlcNAc stimulation (NButGT-10 mg/kg) 1 hour after shock

229 O cells, only limited changes were observed; GlcNAc was still incorporated into N-glycans, but comple

230 fication of proteins by O-linked addition of GlcNAc (O-GlcNAcylation) to Ser/Thr residues of proteins

231 ase (OGT) is responsible for the addition of GlcNAc moieties to target proteins.

232 sity revealed both alpha and beta anomers of GlcNAc, consistent with the added alpha/betaGlcNAc mixtu

233 The number, phenotype, and BCR clonotypes of GlcNAc-reactive B-1 B cells were modulated by neonatal e

234 ulfed cells, and, remarkably, enhancement of GlcNAc exposure on T cells in the CNS ameliorated clinic

235 2 -> partially O-acetylated at 3-hydroxyl of GlcNAc.

236 The levels of GlcNAc inside the cells depend on the nutrient availabil

237 r K50C mSlc35a3 variants had lower levels of GlcNAc-containing glycoconjugates than WT cells, indicat

238 minoglycan composed of disaccharide units of GlcNAc and d-glucuronic acid with alternating beta-1,4 a

239 riad characteristic of CE4 enzymes acting on GlcNAc residues, differing from MurNAc deacetylases that

240 he GAC polyrhamnose backbone is assembled on GlcNAc-P-P-Und.

241 oxin (cuprizone)-induced demyelination, oral GlcNAc prevents neuro-axonal damage by driving myelin re

242 Supplying oral GlcNAc to lactating mice drives primary myelination in n

243 tion and myelin repair and suggest that oral GlcNAc may be neuroprotective in demyelinating diseases

244 nt structures of MraY and its human paralog, GlcNAc-1-P-transferase, have provided insights into MraY

245 r sequence similarity with the peptidoglycan GlcNAc deacetylase SpPgdaA than with other MurNAc deacet

246 mice with a conventional microbiota promoted GlcNAc-reactive B-1 B cell development and concomitantly

247 alcitonin hormone affinity with the proximal GlcNAc residue mediating this effect through an unknown

248 ociated with mutations of the Golgi-resident GlcNAc-1-phosphotransferase, which generates mannose 6-p

249 itutions of Glu-47 and Lys-50 do not restore GlcNAc glycoconjugates.

250 ortuitous promiscuity of OGT, we show that S-GlcNAc is a hydrolytically stable and accurate structura

251 In MS patients, endogenous serum GlcNAc levels inversely correlated with imaging measures

252 We found that relatively short GlcNAc oligosaccharides, such as a six-unit GlcNAc oligo

253 These results reveal a highly specific GlcNAc-binding pocket in conglutinin and a novel collect

254 Here we report that GlcNAc and N-glycan branching trigger oligodendrogenesis

255 ndecaprenol (GlcNAc-P-P-Und) produced by the GlcNAc-phosphate transferase GacO and GlcNAc-phosphate-u

256 MGAT1 is the GlcNAc-transferase that initiates complex and hybrid N-g

257 mannose 6-phosphate tag by the action of the GlcNAc-1-phosphotransferase enzyme, allowing them to bin

258 ng units that are O-acetylated at O-6 of the GlcNAc.

259 As a result, the GlcNAc titer in a 15-l fed-batch bioreactor increased fr

260 N-glycan-free ECD, which suggested that the GlcNAc might affect CTR dynamics not observed in the sta

261 at the Asn-linked GlcNAc moiety not only to GlcNAc-peptide but also to high-mannose and complex-type

262 UDP-GlcNAc is one such metabolite that acts as a substrate f

263 l-dependent biofilm formation requires a UDP-GlcNAc C4-epimerase that generates the UDP-GalNAc precur

264 UDP-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (LpxA) catalyzes the first step

265 uridine diphosphate N-acetylglucosamine (UDP-GlcNAc).

266 -glycan branching was impaired, although UDP-GlcNAc transport into Golgi vesicles was not decreased.

267 d uses cytosolic UDP-glucuronic acid and UDP-GlcNAc as substrates.

268 the complex structures with UDP-Glc and UDP-GlcNAc.

269 a LC-MS method that assesses HBP flux as UDP-GlcNAc ((13)C)-molar percent enrichment (MPE) and concen

270 d the following: (i) all variants act as UDP-GlcNAc/UMP antiporters; (ii) conservative substitutions

271 PelX catalyzes the epimerization between UDP-GlcNAc and UDP-GalNAc.

272 In SLC35A3-knockout HEK293T cells, UDP-GlcNAc transport was significantly decreased but not com

273 f SLC35A2 has been clearly demonstrated, UDP-GlcNAc delivery by SLC35A3 is not fully understood.

274 (HBP) branches from glycolysis and forms UDP-GlcNAc, the moiety for O-linked beta-GlcNAc (O-GlcNAc) p

275 he fungal cell wall, is synthesized from UDP-GlcNAc produced in the hexosamine biosynthetic pathway.

276 d 5 'metabolite' caps-NAD, FAD, UDP-Glc, UDP-GlcNAc, and dpCoA.

277 ctures in humans and mice (FAD, UDP-Glc, UDP-GlcNAc, and m7Gpppm6A), cell- and tissue-specific variat

278 dine diphosphate N-acetyl-D-glucosamine (UDP-GlcNAc) in human prostate cancer LnCaP-LN3 cells, we wer

279 tions (E47D, E47Q, K50R, or K50H) impair UDP-GlcNAc uptake; and (iii) substitutions of Glu-47 and Lys

280 gates than WT cells, indicating impaired UDP-GlcNAc transport activity of these two variants.

281 ed a concentration-dependent increase in UDP-GlcNAc levels and MPE, with the latter reaching a platea

282 UDP-Gal into UDP-Glc and UDP-GalNAc into UDP-GlcNAc with the same level of activity that is required

283 dues involved in the activity of a mouse UDP-GlcNAc transporter, murine solute carrier family 35 memb

284 ernary complex forms: NAD(+)/UDP, NAD(+)/UDP-GlcNAc, and NAD(+)/UDP-Glc.

285 ansporter and/or different mechanisms of UDP-GlcNAc transport into the Golgi apparatus may exist.

286 GlcNAc, in the form of UDP-GlcNAc, and galactose, as UDP-Gal, are delivered into th

287 rrier protein (ACP) to the 3-OH group of UDP-GlcNAc.

288 gest that SLC35A3 may not be the primary UDP-GlcNAc transporter and/or different mechanisms of UDP-Gl

289 e structure revealed that PelX resembles UDP-GlcNAc C4-epimerases.

290 Modeling of the UDP-GlcNAc donor supports a direct displacement inverting ca

291 coordinates a Mg(2+) ion for binding the UDP-GlcNAc sugar donor.

292 ar approaches, we identified WbmV as the UDP-GlcNAc transferase and noted that WbmW represents a UDP-

293 rase GacO and GlcNAc-phosphate-undecaprenol (GlcNAc-P-Und) produced by the glycosyltransferase GacI.

294 ediates: GlcNAc-pyrophosphoryl-undecaprenol (GlcNAc-P-P-Und) produced by the GlcNAc-phosphate transfe

295 GlcNAc oligosaccharides, such as a six-unit GlcNAc oligomer, can bind poliovirus but fail to enhance

296 lysozyme, DslA, which acts, unusually, upon (GlcNAc-) deacetylated peptidoglycan.

297 ust, easily-prepared, engineered enzyme uses GlcNAc and GalNAc donors and couples them to a remarkabl

298 Amelioration of EAE via GlcNAc treatment suggests a novel first-defense pathway

299 Our data suggest a model where GlcNAc polymers of greater than 20 units bind and bridge

300 monoglycosylated cHA (cHA(mg)) vaccine with GlcNAc on each glycosite induced more stem-specific anti