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1 idic linkages of N-acetylgalactosamine and N-acetylglucosamine.
2 ic reactions involving uridine diphosphate N-acetylglucosamine.
3 (OGT) modifies intracellular proteins with N-acetylglucosamine.
4 ose, alpha-glucose, beta-glucose, and beta-N-acetylglucosamine.
5 instantaneous reaction with substrate UDP-N-acetylglucosamine.
6 increased binding capacity of ficolin-2 to N-acetylglucosamine.
7 ucosamine (neosamine) series prepared from N-acetylglucosamine.
8 well as UDP-N-acetylgalactosamine and UDP-N-acetylglucosamine.
9 lipoprotein YceK, toxin HicA, or MurA (UDP-N-acetylglucosamine 1-carboxyvinyltransferase) suppressed
10 tic identified two signaling muropeptides (N-acetylglucosamine-1,6-anhydro-N-acetylmuramyl pentapepti
11 DP-GlcNAc biosynthesis, converting UTP and N-acetylglucosamine-1-phosphate (GlcNAc-1P) to UDP-GlcNAc.
13 struction of a defined mutation in the UDP-N-acetylglucosamine-1-phosphate transferase gene, wecA, in
14 struction of a defined mutation in the UDP-N-acetylglucosamine-1-phosphate transferase gene, wecA, in
15 al and chemoenzymatic syntheses relying on N-acetylglucosamine-1-phosphate uridylyltransferase (GlmU)
16 n the mammalian transmembrane glycoprotein N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosa
18 he Golgi enzyme UDP-GlcNAc:lysosomal enzymeN-acetylglucosamine-1-phosphotransferase (GlcNAc-1-phospho
19 ta subunits of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase (phosphotransfera
21 ineered to carry a mutation in the Gnptab (N-acetylglucosamine-1-phosphotransferase subunits alpha/be
22 sosomal storage disorder caused by loss of N-acetylglucosamine-1-phosphotransferase, which tags lysos
23 hosphate uridylyltransferase (galU), a UDP-N-acetylglucosamine 2-epimerase (wecB) and a UDP-N-acetyl-
24 protein with key enzymatic activities, UDP-N-acetylglucosamine 2-epimerase and N-acetylmannosamine ki
26 he key enzyme of sialic acid biosynthesis, N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
28 sis of sialic acid is the bifunctional UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase
29 etylmannosamine kinase (MNK) domain of UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase
30 e (UDP)-sugar donors, UDP-4-deoxy-4-fluoro-N-acetylglucosamine (4FGlcNAc) and UDP-4-deoxy-4-fluoro-N-
33 clear cells and identified 2 autoantigens, N-acetylglucosamine-6-sulfatase (GNS) and filamin A (FLNA)
37 ase of the structures containing bisecting N-acetylglucosamine along with bi- and trisialylated trian
38 t resulting in IgG molecules with only one N-acetylglucosamine and a fucose residue was fully able to
40 in a ligand-free form, in complex with the N-acetylglucosamine and N-acetylgalactosamine products of
42 to catalyze the in vitro incorporation of N-acetylglucosamine and N-acetylgalactosamine to oligosacc
44 ypical M. xanthus lipids, fucose, mannose, N-acetylglucosamine and N-acetylgalactoseamine carbohydrat
47 2 able to utilize both uridine diphosphate N-acetylglucosamine and uridine diphosphate N-acetylgalact
48 cell wall precursors, UDP-Glucose and UDP-N-acetylglucosamine are efficiently used to initiate trans
53 fer of GalNAc to the simple sugar acceptor N-acetylglucosamine-beta-p-nitrophenol (GlcNAcbeta-pNP) is
54 trisaccharide [N-acetylgalactosamine-beta3-N-acetylglucosamine-beta4-(phosphate-6-)mannose] is requir
55 to the GalFuc-binding lectin CGL2 and the N-acetylglucosamine-binding lectin XCL, the mutant was res
56 agellar and type III secretion systems and N-acetylglucosamine-binding protein GpbA while inducing ge
57 embrane protein, as well as spermidine and N-acetylglucosamine biosynthesis, all contribute to surami
58 utation using both the UDP-glucose and UDP-N-acetylglucosamine bound structures of the wild-type prot
59 tor endocytosis and signaling by promoting N-acetylglucosamine branching of Asn (N)-linked glycans.
62 for receptor function, and elongation with N-acetylglucosamine, catalyzed by members of the Fringe fa
65 et al. (2016) report that detection of the N-acetylglucosamine component of peptidoglycan by the glyc
66 le the UT-A1 in lipid rafts was the mature N-acetylglucosamine-containing form, as detected by wheat
67 ns confer recognitional specificity toward N-acetylglucosamine-containing signaling molecules, such a
69 nhibitor of UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) in Gram-negative ba
70 mined and found to be a member of the PIG-LN-acetylglucosamine deacetylase family; GalB is structural
71 made of repeating N-acetylmuramic acid and N-acetylglucosamine disaccharides cross-linked by pentapep
72 synthetic pathway (HBSP) that produces UDP-N-acetylglucosamine for O-linked N-acetylglucosamine modif
74 e pools of UDP-glucose, UDP-galactose, UDP-N-acetylglucosamine, GDP-mannose, and GDP-fucose in Plasmo
75 hase 1-3 (HAS1-3) isoenzymes that transfer N-acetylglucosamine (GlcNAc) and glucuronic acid (GlcUA) i
77 lycan (PGN) consists of repeating units of N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid (Mur
78 on of nucleocytoplasmic proteins with beta-N-acetylglucosamine (GlcNAc) and regulates numerous biolog
80 on is altered by deleting two Bdellovibrio N-acetylglucosamine (GlcNAc) deacetylases, one of which we
83 ate addition and removal, respectively, of N-acetylglucosamine (GlcNAc) from intracellular protein su
84 -GlcNAc transferase (OGT), which transfers N-acetylglucosamine (GlcNAc) from the nucleotide sugar don
87 usly that varphi11 requires alpha- or beta-N-acetylglucosamine (GlcNAc) moieties on cell wall teichoi
88 ase that mediates the O-linked addition of N-acetylglucosamine (GlcNAc) moieties to Ser and Thr resid
90 scribed here, is attached to the remaining N-acetylglucosamine (GlcNAc) of IgG, using a mutant endogl
93 ide variety of substrates which contain an N-acetylglucosamine (GlcNAc) residue to act as an 'accepto
94 ranslationally modified by adding O-linked N-acetylglucosamine (GlcNAc) residue to serine or threonin
95 dules recognize polysaccharides containing N-acetylglucosamine (GlcNAc) residues including peptidogly
96 reducing end glucose of CPS and the beta-D-N-acetylglucosamine (GlcNAc) residues of peptidoglycan (PG
97 Chitin, a homopolymer of beta1,4-linked N-acetylglucosamine (GlcNAc) residues, is a key component
98 lyrhamnose backbone with an immunodominant N-acetylglucosamine (GlcNAc) side chain, which is the basi
99 d consists of a polyrhamnose polymer, with N-acetylglucosamine (GlcNAc) side chains, which is an esse
101 core-2 O-glycan branch through addition of N-acetylglucosamine (GlcNAc) to a core-1 O-glycan structur
102 c Fringe) and MFNG (Manic Fringe) transfer N-acetylglucosamine (GlcNAc) to O-fucose attached to EGF-l
104 odifies protein function by attaching beta-N-acetylglucosamine (GlcNAc) to serine and threonine resid
105 ions of PgaB show a binding preference for N-acetylglucosamine (GlcNAc) to the N-terminal domain and
108 nctional homologue of the Candida albicans N-acetylglucosamine (GlcNAc) transporter NGT1, and represe
109 e for glycolysis and chitobiose to produce N-acetylglucosamine (GlcNAc), a key component of the bacte
110 ibed to contain the sugars rhamnose (Rha), N-acetylglucosamine (GlcNAc), galactose (Gal), xylose (Xyl
112 hesis of a tetra-antennary glycan that has N-acetylglucosamine (GlcNAc), N-acetyllactosamine (LacNAc)
113 entation of culture media with uridine and N-acetylglucosamine (GlcNAc), precursors for the hexosamin
114 nslational modification with O-linked beta-N-acetylglucosamine (GlcNAc), promoted apoptosis through a
115 to form hyphae in response to the inducer N-acetylglucosamine (GlcNAc), suggesting that a basal leve
116 death domain-containing host proteins with N-acetylglucosamine (GlcNAc), thereby blocking extrinsic a
117 ry glycan [A3(2,4,2) type] terminated with N-acetylglucosamine (GlcNAc), which is generated by N-acet
121 n, demonstrating that the 6-O-sulfation of N-acetylglucosamine (GlcNAc-6-O-sulfation) is highly conse
124 is the presence of a nonreducing terminal N-acetylglucosamine; however, this residue is normally abs
125 amine transferase (OGT), and O-linked beta-N-acetylglucosamine hydrolase in control and IPAH cells an
126 ial cells as demonstrated by inhibition of N-acetylglucosamine incorporation into polymeric cell wall
127 In H. jecorina-produced HjCel3A, a single N-acetylglucosamine is present at both sites, whereas in P
130 on of chitin, a beta-1,4 linked polymer of N-acetylglucosamine, is of major interest in areas varying
132 es residues that are already modified with N-acetylglucosamine, likely by converting into a relaxed c
134 osphate-N-acetylmuramic acid(pentapeptide)-N-acetylglucosamine (lipid II), which is readily accessibl
135 for a unique phosphotransferase system and N-acetylglucosamine metabolism suggests an important ecolo
136 duces UDP-N-acetylglucosamine for O-linked N-acetylglucosamine modification (O-GlcNAcylation) of prot
137 ed by cAMP (EPAC), involving also O-linked N-acetylglucosamine modification downstream of the hexosam
138 s resulted in reduced global O-linked beta-N-acetylglucosamine modification levels and abrogated PASM
139 We measured the levels of O-linked beta-N-acetylglucosamine modification, O-linked beta-N-acetylgl
141 he addition of the phosphothreonine to the N-acetylglucosamine moiety and CD0243 transfers the methyl
142 ongest interactions are established by the N-acetylglucosamine moiety in the central region of the en
143 omposed of N-acetylmuramic acid-(beta-1,4)-N-acetylglucosamine (MurNAc-GlcNAc) disaccharides associat
144 g amino sugars [i.e., N-acetylmuramic acid-N-acetylglucosamine (MurNAc-GlcNAc)] from attached peptido
145 enzymes phosphomannomutase (PMM), phospho-N-acetylglucosamine mutase (PAGM) and phosphoglucomutase (
146 s was reduced by selective inactivation of N-acetylglucosamine N-deacetylase-N-sulfotransferase (Ndst
147 uniform responses (d-lactose, d-galactose, N-acetylglucosamine, N-acetylneuraminic acid), 'all-or-non
148 tility, decreased chemotactic responses to N-acetylglucosamine (NAG) and attenuated ability to dissem
149 g azides and alkynes were installed on tri-N-acetylglucosamine (NAG)3, a PG mimic, as well as PG isol
150 onal addition and removal of O-linked beta-N-acetylglucosamine (O-GlcNAc) also occurs on serine resid
151 signaling pathway, terminating in O-linked-N-acetylglucosamine (O-GlcNAc) cycling, is a key sensor of
153 ion controlled by the enzyme O-linked-beta-N-acetylglucosamine (O-GlcNAc) glycosyltransferase as comp
154 ar and cytosolic proteins by O-linked beta-N-acetylglucosamine (O-GlcNAc) has been shown to play an i
158 ational protein modification O-linked beta-N-acetylglucosamine (O-GlcNAc) is a proposed nutrient sens
166 efute the hypothesis of extensive O-linked N-acetylglucosamine (O-GlcNAc) modification of endogenous
170 study, we show that TAB1 is modified with N-acetylglucosamine (O-GlcNAc) on a single site, Ser395.
171 osttranslational addition of O-linked beta-N-acetylglucosamine (O-GlcNAc) on intracellular proteins.
174 is study, we demonstrate that the O-linked N-acetylglucosamine (O-GlcNAc) processing enzymes, O-GlcNA
175 t-translational modification O-linked beta-N-acetylglucosamine (O-GlcNAc) regulates thousands of nucl
176 ss of interest is the addition of O-linked N-acetylglucosamine (O-GlcNAc) residues onto nuclear and c
177 the covalent addition of an O-linked beta-N-acetylglucosamine (O-GlcNAc) sugar moiety to hydroxyl gr
178 ed, in part, by the attachment of O-linked N-acetylglucosamine (O-GlcNAc) to proteins (O-GlcNAcylatio
179 e reversibly glycosylated by O-linked beta-N-acetylglucosamine (O-GlcNAc) to regulate their function,
180 ational addition of a single O-linked beta-N-acetylglucosamine (O-GlcNAc) to serine or threonine resi
181 st-translational addition of O-linked beta-N-acetylglucosamine (O-GlcNAc) to various nuclear and cyto
183 Here we demonstrate that O-linked beta-N-acetylglucosamine (O-GlcNAc) transferase (OGT) is requir
186 w that DELLAs are modified by the O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT) SECRET AG
187 ine biosynthesis pathway and O-linked beta-N-acetylglucosamine (O-GlcNAc) transferase (OGT) to potent
188 TET2 and TET3 associate with O-linked beta-N-acetylglucosamine (O-GlcNAc) transferase (OGT), an enzym
194 h a modification in the amount of O-linked N-acetylglucosamine (O-GlcNAc)-modified proteins and in th
200 modification of proteins by O-linked beta-N-acetylglucosamine (O-GlcNAcylation) is a key metabolic r
201 ty and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroiti
202 modification of proteins with beta-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression o
208 mmatory and stress responses, and O-linked N-acetylglucosamine (OGN) transferase (OGT), an enzyme tha
209 he reaction of free MurA and substrate UDP-N-acetylglucosamine or isomer UDP-N-acetylgalactosamine.
210 hydrolyze the beta-linkages joining either N-acetylglucosamine or N-acetylgalactosamine to a wide var
212 ubstrates (a mix of substrates, glutamine, N-acetylglucosamine, or pyruvate) revealed contrasting cap
214 lly predicted putative miR-185 targets UDP-N-acetylglucosamine-peptide N-acetylglucosaminyltransferas
218 conserved cell surface polysaccharide poly-N-acetylglucosamine (PNAG) were effective at mediating red
219 encoding the biosynthesis of poly-beta-1,6-N-acetylglucosamine (PNAG), a major biofilm matrix compone
220 isolate and found to be negative for poly-N-acetylglucosamine (PNAG)-like material by immunoblot ass
223 se O-GlcNAc transferase (uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylaminyltransfe
227 d to the proximal (reducing-terminal) core N-acetylglucosamine residue of N-glycans by beta1,4-linked
229 tode glycan cores, specifically the distal N-acetylglucosamine residue; this result is in accordance
230 glycan structure of seven mannosyl and two N-acetylglucosamine residues (Man7GlcNAc2) on misfolded gl
231 linear tetrasaccharide that contained two N-acetylglucosamine residues and a free OH group gave two
233 ves the attachment of single beta-O-linked N-acetylglucosamine residues to serine and threonine resid
234 nds between N-acetylmuramic acid (NAM) and N-acetylglucosamine residues with concomitant formation of
236 lus niger in deglycosylated and Asn-linked N-acetylglucosamine-stub forms reveal a 10(2/3)-turn paral
237 magnetic resonance and shown to contain an N-acetylglucosamine substituted with a phosphorylated N-me
238 e for the selective phosphorylation of the N-acetylglucosamine sugar in a teicoplanin A2-2 derivative
240 The enzymatic addition of a single beta-D-N-acetylglucosamine sugar molecule on serine and/or threon
241 ion consisting of the addition of a single N-acetylglucosamine sugar to serine and threonine residues
242 ated post-translational addition of beta-D-N-acetylglucosamine sugars to nuclear and cytoplasmic prot
243 vidently, hexosamine pathway activation or N-acetylglucosamine supplementation induces distinct prote
246 idue is in closer proximity (7.6 A) to the N-acetylglucosamine than the two other sugar rings present
248 mmasome activation is caused by release of N-acetylglucosamine that is detected in the cytosol by the
249 tic itineraries for other sugars; for beta-N-acetylglucosamine, the key N-acetyl arm confounds the pu
250 These results demonstrate that glucose and N-acetylglucosamine, the most readily available chiral bui
251 K3, which is essential for the transfer of N-acetylglucosamine to arginine residues (arginine-GlcNAcy
254 etylmannosamine kinase that transforms UDP-N-acetylglucosamine to N-acetylmannosamine (ManNAc) follow
256 such modification is addition of O-linked N-acetylglucosamine to serine or threonine residues, known
257 dification involving the O-linkage of beta-N-acetylglucosamine to serine/threonine residues of membra
259 nctions as a ligase that adds the terminal N-acetylglucosamine to the lipooligosaccharide core of Y.
260 e essential mammalian enzyme O-linked beta-N-acetylglucosamine transferase (O-GlcNAc transferase, her
261 involved in cell metabolism: O-linked beta-N-acetylglucosamine transferase (OGT) and isocitrate dehyd
265 umors from colon tumor cells with O-linked N-acetylglucosamine transferase (OGT) knockdown grew signi
266 tylglucosamine modification, O-linked beta-N-acetylglucosamine transferase (OGT), and O-linked beta-N
267 with host cell factor-1 (HCF-1), O-linked N-acetylglucosamine transferase (OGT), and the polycomb gr
268 es in proteins by the enzyme O-linked beta-N-acetylglucosamine transferase (OGT), whereas the enzyme
269 s an essential substrate for O-linked beta-N-acetylglucosamine transferase (OGT), which glycosylates
271 also interacts with the O-GlcNAc (O-linked N-acetylglucosamine) transferase SPINDLY required for prop
272 LPH3 supports incorporation of both core 2 N-acetylglucosamine-transferase 1 and alpha-2,6-sialyltran
274 hat EXTL2 exhibited much stronger in vitro N-acetylglucosamine-transferase activity related to elonga
276 lactose transporter (UGT; SLC35A2) and UDP-N-acetylglucosamine transporter (NGT; SLC35A3) form hetero
277 000) as an ER-localized facilitator of UDP-N-acetylglucosamine (UDP-GlcNAc) and UDP-N-acetylgalactosa
279 osamine biosynthetic pathway, increase UDP-N-acetylglucosamine (UDP-GlcNAc) availability, and lead to
280 thatlymphostatin binds uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) but not UDP-glucose (UDP-
281 athway (HBP) generates uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) for glycan synthesis and
285 kingly, addition of the HBP metabolite UDP-N-acetylglucosamine (UDP-GlcNAc) to CRPC-like cells signif
286 e transfer of N-acetylglucosamine from UDP-N-acetylglucosamine (UDP-GlcNAc) to serines and threonines
287 ntracellular levels of uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc), a key precursor of LacNA
288 mine are precursors of uridine diphosphate N-acetylglucosamine (UDP-GlcNAc), a substrate for cellular
289 iosynthesis precursor, uridine diphosphate N-acetylglucosamine (UDP-GlcNAc), was monitored by recordi
294 -glucuronic acid, and UGT3 enzymes use UDP-N-acetylglucosamine, UDP-glucose, and UDP-xylose to conjug
295 , ChiA variants with weaker binding of the N-acetylglucosamine unit either in substrate-binding site
296 core alpha1,3-fucosylation of the proximal N-acetylglucosamine was abolished, the degree of galactosy
297 ties for uncharged substrates (glucose and N-acetylglucosamine) were also enhanced, despite competiti
298 ep in the synthesis of uridine diphosphate N-acetylglucosamine, which is required for the biosynthesi
299 rsion of UDP-N-acetylgalactosamine and UDP-N-acetylglucosamine while the bacterial enzyme cannot.
300 beta4 addition of N-acetylgalactosamine to N-acetylglucosamine with formation of the N,N-diacetyllact
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