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1 glucosamine (neosamine) series prepared from N-acetylglucosamine.
2 as well as UDP-N-acetylgalactosamine and UDP-N-acetylglucosamine.
3 osidic linkages of N-acetylgalactosamine and N-acetylglucosamine.
4 etic reactions involving uridine diphosphate N-acetylglucosamine.
5 nnose, alpha-glucose, beta-glucose, and beta-N-acetylglucosamine.
6 -linked sialic acid, galactose, and bisected N-acetylglucosamine.
7 ersion of UDP-N-acetylgalactosamine with UDP-N-acetylglucosamine.
8 e (OGT) modifies intracellular proteins with N-acetylglucosamine.
9 , lipoprotein YceK, toxin HicA, or MurA (UDP-N-acetylglucosamine 1-carboxyvinyltransferase) suppresse
10 iotic identified two signaling muropeptides (N-acetylglucosamine-1,6-anhydro-N-acetylmuramyl pentapep
11 UDP-GlcNAc biosynthesis, converting UTP and N-acetylglucosamine-1-phosphate (GlcNAc-1P) to UDP-GlcNA
15 ical and chemoenzymatic syntheses relying on N-acetylglucosamine-1-phosphate uridylyltransferase (Glm
16 in the mammalian transmembrane glycoprotein N-acetylglucosamine-1-phosphodiester alpha-N-acetylgluco
18 beta subunits of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase (phosphotransfe
20 ngineered to carry a mutation in the Gnptab (N-acetylglucosamine-1-phosphotransferase subunits alpha/
21 lysosomal storage disorder caused by loss of N-acetylglucosamine-1-phosphotransferase, which tags lys
22 e protein with key enzymatic activities, UDP-N-acetylglucosamine 2-epimerase and N-acetylmannosamine
24 the key enzyme of sialic acid biosynthesis, N-acetylglucosamine 2-epimerase/N-acetylmannosamine kina
26 hesis of sialic acid is the bifunctional UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kina
27 acetylmannosamine kinase (MNK) domain of UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kina
28 ate (UDP)-sugar donors, UDP-4-deoxy-4-fluoro-N-acetylglucosamine (4FGlcNAc) and UDP-4-deoxy-4-fluoro-
31 nuclear cells and identified 2 autoantigens, N-acetylglucosamine-6-sulfatase (GNS) and filamin A (FLN
36 rease of the structures containing bisecting N-acetylglucosamine along with bi- and trisialylated tri
37 verted by epimerization to the corresponding N-acetylglucosamine analog by the epimerase N-acetylgala
38 ent resulting in IgG molecules with only one N-acetylglucosamine and a fucose residue was fully able
40 ide based NPs that incorporate both sulfated N-acetylglucosamine and hydrophobic monomers were optimi
41 C in a ligand-free form, in complex with the N-acetylglucosamine and N-acetylgalactosamine products o
43 in to catalyze the in vitro incorporation of N-acetylglucosamine and N-acetylgalactosamine to oligosa
45 typical M. xanthus lipids, fucose, mannose, N-acetylglucosamine and N-acetylgalactoseamine carbohydr
46 a repeating beta-1,4-linked disaccharide of N-acetylglucosamine and N-acetylmuramic acid appended wi
49 nT2 able to utilize both uridine diphosphate N-acetylglucosamine and uridine diphosphate N-acetylgala
51 ng cell wall precursors, UDP-Glucose and UDP-N-acetylglucosamine are efficiently used to initiate tra
54 utinin (HA) of influenza virus with a single N-acetylglucosamine at each of the N-glycosylation sites
56 nsfer of GalNAc to the simple sugar acceptor N-acetylglucosamine-beta-p-nitrophenol (GlcNAcbeta-pNP)
57 l trisaccharide [N-acetylgalactosamine-beta3-N-acetylglucosamine-beta4-(phosphate-6-)mannose] is requ
58 activity, resulting in higher levels of UDP-N-acetylglucosamine biosynthesis and protein O-GlcNAcyla
59 mutation using both the UDP-glucose and UDP-N-acetylglucosamine bound structures of the wild-type pr
60 eptor endocytosis and signaling by promoting N-acetylglucosamine branching of Asn (N)-linked glycans.
63 f et al. (2016) report that detection of the N-acetylglucosamine component of peptidoglycan by the gl
64 ains confer recognitional specificity toward N-acetylglucosamine-containing signaling molecules, such
65 inhibitor of UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) in Gram-negative
66 s made of repeating N-acetylmuramic acid and N-acetylglucosamine disaccharides cross-linked by pentap
67 iosynthetic pathway (HBSP) that produces UDP-N-acetylglucosamine for O-linked N-acetylglucosamine mod
68 the pools of UDP-glucose, UDP-galactose, UDP-N-acetylglucosamine, GDP-mannose, and GDP-fucose in Plas
69 nthase 1-3 (HAS1-3) isoenzymes that transfer N-acetylglucosamine (GlcNAc) and glucuronic acid (GlcUA)
70 t sugar-aromatic interactions, with glucose, N-acetylglucosamine (GlcNAc) and mannose in between.
71 tion of nucleocytoplasmic proteins with beta-N-acetylglucosamine (GlcNAc) and regulates numerous biol
73 e production of the high value nutraceutical N-acetylglucosamine (GlcNAc) could be balanced and optim
74 tion is altered by deleting two Bdellovibrio N-acetylglucosamine (GlcNAc) deacetylases, one of which
76 diate addition and removal, respectively, of N-acetylglucosamine (GlcNAc) from intracellular protein
77 O-GlcNAc transferase (OGT), which transfers N-acetylglucosamine (GlcNAc) from the nucleotide sugar d
80 iously that varphi11 requires alpha- or beta-N-acetylglucosamine (GlcNAc) moieties on cell wall teich
81 erase that mediates the O-linked addition of N-acetylglucosamine (GlcNAc) moieties to Ser and Thr res
83 described here, is attached to the remaining N-acetylglucosamine (GlcNAc) of IgG, using a mutant endo
86 wide variety of substrates which contain an N-acetylglucosamine (GlcNAc) residue to act as an 'accep
87 -translationally modified by adding O-linked N-acetylglucosamine (GlcNAc) residue to serine or threon
88 modules recognize polysaccharides containing N-acetylglucosamine (GlcNAc) residues including peptidog
89 e reducing end glucose of CPS and the beta-D-N-acetylglucosamine (GlcNAc) residues of peptidoglycan (
91 polyrhamnose backbone with an immunodominant N-acetylglucosamine (GlcNAc) side chain, which is the ba
92 and consists of a polyrhamnose polymer, with N-acetylglucosamine (GlcNAc) side chains, which is an es
94 f core-2 O-glycan branch through addition of N-acetylglucosamine (GlcNAc) to a core-1 O-glycan struct
96 modifies protein function by attaching beta-N-acetylglucosamine (GlcNAc) to serine and threonine res
97 ations of PgaB show a binding preference for N-acetylglucosamine (GlcNAc) to the N-terminal domain an
100 functional homologue of the Candida albicans N-acetylglucosamine (GlcNAc) transporter NGT1, and repre
101 rce for glycolysis and chitobiose to produce N-acetylglucosamine (GlcNAc), a key component of the bac
102 ieved by the treatment of P. aeruginosa with N-acetylglucosamine (GlcNAc), a widespread chemical pres
104 nthesis of a tetra-antennary glycan that has N-acetylglucosamine (GlcNAc), N-acetyllactosamine (LacNA
105 ementation of culture media with uridine and N-acetylglucosamine (GlcNAc), precursors for the hexosam
106 ranslational modification with O-linked beta-N-acetylglucosamine (GlcNAc), promoted apoptosis through
107 em to form hyphae in response to the inducer N-acetylglucosamine (GlcNAc), suggesting that a basal le
108 n death domain-containing host proteins with N-acetylglucosamine (GlcNAc), thereby blocking extrinsic
109 nary glycan [A3(2,4,2) type] terminated with N-acetylglucosamine (GlcNAc), which is generated by N-ac
115 lin, demonstrating that the 6-O-sulfation of N-acetylglucosamine (GlcNAc-6-O-sulfation) is highly con
117 osamine transferase (OGT), and O-linked beta-N-acetylglucosamine hydrolase in control and IPAH cells
118 erial cells as demonstrated by inhibition of N-acetylglucosamine incorporation into polymeric cell wa
120 In H. jecorina-produced HjCel3A, a single N-acetylglucosamine is present at both sites, whereas in
121 nitoring the relative abundance of bisecting N-acetylglucosamine is relevant to physiological process
124 sion of chitin, a beta-1,4 linked polymer of N-acetylglucosamine, is of major interest in areas varyi
126 izes residues that are already modified with N-acetylglucosamine, likely by converting into a relaxed
128 phosphate-N-acetylmuramic acid(pentapeptide)-N-acetylglucosamine (lipid II), which is readily accessi
129 s for a unique phosphotransferase system and N-acetylglucosamine metabolism suggests an important eco
130 roduces UDP-N-acetylglucosamine for O-linked N-acetylglucosamine modification (O-GlcNAcylation) of pr
131 ated by cAMP (EPAC), involving also O-linked N-acetylglucosamine modification downstream of the hexos
132 MCs resulted in reduced global O-linked beta-N-acetylglucosamine modification levels and abrogated PA
133 We measured the levels of O-linked beta-N-acetylglucosamine modification, O-linked beta-N-acetyl
135 the addition of the phosphothreonine to the N-acetylglucosamine moiety and CD0243 transfers the meth
136 trongest interactions are established by the N-acetylglucosamine moiety in the central region of the
137 composed of N-acetylmuramic acid-(beta-1,4)-N-acetylglucosamine (MurNAc-GlcNAc) disaccharides associ
138 ing amino sugars [i.e., N-acetylmuramic acid-N-acetylglucosamine (MurNAc-GlcNAc)] from attached pepti
139 he enzymes phosphomannomutase (PMM), phospho-N-acetylglucosamine mutase (PAGM) and phosphoglucomutase
140 to the monosaccharides l-fucose, d-mannose, N-acetylglucosamine, N-acetylgalactosamine, and galactos
141 g uniform responses (d-lactose, d-galactose, N-acetylglucosamine, N-acetylneuraminic acid), 'all-or-n
142 in vitro in the presence of acetyl-CoA, UDP- N-acetylglucosamine, NADPH, and ATP, we have developed a
143 ing azides and alkynes were installed on tri-N-acetylglucosamine (NAG)3, a PG mimic, as well as PG is
144 tional addition and removal of O-linked beta-N-acetylglucosamine (O-GlcNAc) also occurs on serine res
145 ation controlled by the enzyme O-linked-beta-N-acetylglucosamine (O-GlcNAc) glycosyltransferase as co
146 hesis and impaired addition of O-linked beta-N-acetylglucosamine (O-GlcNAc) groups to proteins import
147 lear and cytosolic proteins by O-linked beta-N-acetylglucosamine (O-GlcNAc) has been shown to play an
148 mic post-translational modification O-linked N-Acetylglucosamine (O-GlcNAc) has emerged as an attract
149 e (OGA) is an enzyme harboring O-linked beta-N-acetylglucosamine (O-GlcNAc) hydrolase and cryptic lys
153 slational protein modification O-linked beta-N-acetylglucosamine (O-GlcNAc) is a proposed nutrient se
160 refute the hypothesis of extensive O-linked N-acetylglucosamine (O-GlcNAc) modification of endogenou
165 osttranslational modification by beta-linked N-acetylglucosamine (O-GlcNAc) on HDAC4 were investigate
166 posttranslational addition of O-linked beta-N-acetylglucosamine (O-GlcNAc) on intracellular proteins
168 entification and precise mapping of O-linked N-acetylglucosamine (O-GlcNAc) post-translational modifi
170 this study, we demonstrate that the O-linked N-acetylglucosamine (O-GlcNAc) processing enzymes, O-Glc
171 ost-translational modification O-linked beta-N-acetylglucosamine (O-GlcNAc) regulates thousands of nu
172 cess of interest is the addition of O-linked N-acetylglucosamine (O-GlcNAc) residues onto nuclear and
173 i-inflammatory function of the O-linked beta-N-acetylglucosamine (O-GlcNAc) signaling associated with
174 ected role of nutrient-sensing O-linked beta-N-acetylglucosamine (O-GlcNAc) signaling in suppressing
175 d posttranslational modification by O-linked N-Acetylglucosamine (O-GlcNAc) stabilizes FOXP3 and acti
176 is the covalent addition of an O-linked beta-N-acetylglucosamine (O-GlcNAc) sugar moiety to hydroxyl
177 ined, in part, by the attachment of O-linked N-acetylglucosamine (O-GlcNAc) to proteins (O-GlcNAcylat
178 toplasmic and nuclear protein by transfer of N-acetylglucosamine (O-GlcNAc) to serine and threonine h
179 slational addition of a single O-linked beta-N-acetylglucosamine (O-GlcNAc) to serine or threonine re
184 how that DELLAs are modified by the O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT) SECRET
185 amine biosynthesis pathway and O-linked beta-N-acetylglucosamine (O-GlcNAc) transferase (OGT) to pote
186 t TET2 and TET3 associate with O-linked beta-N-acetylglucosamine (O-GlcNAc) transferase (OGT), an enz
191 osttranslational modification, O-linked beta-N-acetylglucosamine (O-GlcNAc), in NSCs promotes a glial
193 ugh a modification in the amount of O-linked N-acetylglucosamine (O-GlcNAc)-modified proteins and in
198 al modification of proteins with beta-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression
200 ride beta-N-acetylmuramic acid, (1-->4)-beta-N-acetylglucosamine of staphylococcal peptidoglycan.
203 lammatory and stress responses, and O-linked N-acetylglucosamine (OGN) transferase (OGT), an enzyme t
204 the reaction of free MurA and substrate UDP-N-acetylglucosamine or isomer UDP-N-acetylgalactosamine.
205 o hydrolyze the beta-linkages joining either N-acetylglucosamine or N-acetylgalactosamine to a wide v
207 substrates (a mix of substrates, glutamine, N-acetylglucosamine, or pyruvate) revealed contrasting c
208 nally predicted putative miR-185 targets UDP-N-acetylglucosamine-peptide N-acetylglucosaminyltransfer
213 served microbial surface polysaccharide poly-N-acetylglucosamine (PNAG) that is expressed on numerous
214 e conserved cell surface polysaccharide poly-N-acetylglucosamine (PNAG) were effective at mediating r
215 , encoding the biosynthesis of poly-beta-1,6-N-acetylglucosamine (PNAG), a major biofilm matrix compo
216 ne isolate and found to be negative for poly-N-acetylglucosamine (PNAG)-like material by immunoblot a
222 2-FGFR1c2 can tolerate an HS chain having an N-acetylglucosamine residue at its non-reducing end.
223 hed to the proximal (reducing-terminal) core N-acetylglucosamine residue of N-glycans by beta1,4-link
225 matode glycan cores, specifically the distal N-acetylglucosamine residue; this result is in accordanc
226 N-glycan structure of seven mannosyl and two N-acetylglucosamine residues (Man7GlcNAc2) on misfolded
227 a linear tetrasaccharide that contained two N-acetylglucosamine residues and a free OH group gave tw
228 ieties of N-acetylneuraminic acid as well as N-acetylglucosamine residues and nucleophilic sites of a
230 bonds between N-acetylmuramic acid (NAM) and N-acetylglucosamine residues with concomitant formation
232 arbon substrates, For example, for growth on N-acetylglucosamine, S. marcescens exhibits high pentose
233 illus niger in deglycosylated and Asn-linked N-acetylglucosamine-stub forms reveal a 10(2/3)-turn par
234 r magnetic resonance and shown to contain an N-acetylglucosamine substituted with a phosphorylated N-
235 tion of intracellular proteins with a single N-acetylglucosamine sugar (O-GlcNAcylation) regulates si
236 ble for the selective phosphorylation of the N-acetylglucosamine sugar in a teicoplanin A2-2 derivati
238 The enzymatic addition of a single beta-D-N-acetylglucosamine sugar molecule on serine and/or thre
239 ation consisting of the addition of a single N-acetylglucosamine sugar to serine and threonine residu
240 evated post-translational addition of beta-D-N-acetylglucosamine sugars to nuclear and cytoplasmic pr
241 Evidently, hexosamine pathway activation or N-acetylglucosamine supplementation induces distinct pro
242 ric forms of either N-acetylgalactosamine or N-acetylglucosamine target hepatic antigen-presenting ce
244 esidue is in closer proximity (7.6 A) to the N-acetylglucosamine than the two other sugar rings prese
246 lammasome activation is caused by release of N-acetylglucosamine that is detected in the cytosol by t
247 lytic itineraries for other sugars; for beta-N-acetylglucosamine, the key N-acetyl arm confounds the
248 These results demonstrate that glucose and N-acetylglucosamine, the most readily available chiral b
249 seK3, which is essential for the transfer of N-acetylglucosamine to arginine residues (arginine-GlcNA
250 acetylmannosamine kinase that transforms UDP-N-acetylglucosamine to N-acetylmannosamine (ManNAc) foll
251 nal modification involving O-linkage of beta-N-acetylglucosamine to Ser/Thr residues on target protei
252 ne such modification is addition of O-linked N-acetylglucosamine to serine or threonine residues, kno
253 modification involving the O-linkage of beta-N-acetylglucosamine to serine/threonine residues of memb
255 functions as a ligase that adds the terminal N-acetylglucosamine to the lipooligosaccharide core of Y
257 s involved in cell metabolism: O-linked beta-N-acetylglucosamine transferase (OGT) and isocitrate deh
261 tumors from colon tumor cells with O-linked N-acetylglucosamine transferase (OGT) knockdown grew sig
262 that TRIM28 was complexed with O-linked beta-N-acetylglucosamine transferase (OGT) only in cells that
263 cetylglucosamine modification, O-linked beta-N-acetylglucosamine transferase (OGT), and O-linked beta
264 dues in proteins by the enzyme O-linked beta-N-acetylglucosamine transferase (OGT), whereas the enzym
265 ces an essential substrate for O-linked beta-N-acetylglucosamine transferase (OGT), which glycosylate
267 amine biosynthetic pathway and OGT (O-linked N-acetylglucosamine transferase)-mediated protein O-GlcN
268 otentially encode an O-acetyltransferase, an N-acetylglucosamine transferase, and a KDO transferase c
269 C also interacts with the O-GlcNAc (O-linked N-acetylglucosamine) transferase SPINDLY required for pr
270 GOLPH3 supports incorporation of both core 2 N-acetylglucosamine-transferase 1 and alpha-2,6-sialyltr
272 that EXTL2 exhibited much stronger in vitro N-acetylglucosamine-transferase activity related to elon
274 galactose transporter (UGT; SLC35A2) and UDP-N-acetylglucosamine transporter (NGT; SLC35A3) form hete
276 65000) as an ER-localized facilitator of UDP-N-acetylglucosamine (UDP-GlcNAc) and UDP-N-acetylgalacto
278 exosamine biosynthetic pathway, increase UDP-N-acetylglucosamine (UDP-GlcNAc) availability, and lead
279 d thatlymphostatin binds uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) but not UDP-glucose (UD
280 pathway (HBP) generates uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) for glycan synthesis an
284 rikingly, addition of the HBP metabolite UDP-N-acetylglucosamine (UDP-GlcNAc) to CRPC-like cells sign
285 tamine are precursors of uridine diphosphate N-acetylglucosamine (UDP-GlcNAc), a substrate for cellul
286 -biosynthesis precursor, uridine diphosphate N-acetylglucosamine (UDP-GlcNAc), was monitored by recor
291 DP-glucuronic acid, and UGT3 enzymes use UDP-N-acetylglucosamine, UDP-glucose, and UDP-xylose to conj
292 el, ChiA variants with weaker binding of the N-acetylglucosamine unit either in substrate-binding sit
293 side the cell (to produce the monosaccharide N-acetylglucosamine), using this beta-glucan to obtain c
294 a five-member consortium of sialic acid and N-acetylglucosamine utilizers that impedes C. difficile'
295 t core alpha1,3-fucosylation of the proximal N-acetylglucosamine was abolished, the degree of galacto
297 nities for uncharged substrates (glucose and N-acetylglucosamine) were also enhanced, despite competi
298 ycans with different modifications including N-acetylglucosamine, which bisects the mannose core.
299 step in the synthesis of uridine diphosphate N-acetylglucosamine, which is required for the biosynthe
300 version of UDP-N-acetylgalactosamine and UDP-N-acetylglucosamine while the bacterial enzyme cannot.
301 y beta4 addition of N-acetylgalactosamine to N-acetylglucosamine with formation of the N,N-diacetylla