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1 osidic linkages of N-acetylgalactosamine and N-acetylglucosamine.
2 etic reactions involving uridine diphosphate N-acetylglucosamine.
3 e (OGT) modifies intracellular proteins with N-acetylglucosamine.
4 nnose, alpha-glucose, beta-glucose, and beta-N-acetylglucosamine.
5 or instantaneous reaction with substrate UDP-N-acetylglucosamine.
6 o increased binding capacity of ficolin-2 to N-acetylglucosamine.
7 glucosamine (neosamine) series prepared from N-acetylglucosamine.
8 as well as UDP-N-acetylgalactosamine and UDP-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
13 onstruction of a defined mutation in the UDP-N-acetylglucosamine-1-phosphate transferase gene, wecA,
14 onstruction of a defined mutation in the UDP-N-acetylglucosamine-1-phosphate transferase gene, wecA,
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 -phosphate uridylyltransferase (galU), a UDP-N-acetylglucosamine 2-epimerase (wecB) and a UDP-N-acety
23 e protein with key enzymatic activities, UDP-N-acetylglucosamine 2-epimerase and N-acetylmannosamine
25 the key enzyme of sialic acid biosynthesis, N-acetylglucosamine 2-epimerase/N-acetylmannosamine kina
27 hesis of sialic acid is the bifunctional UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kina
28 acetylmannosamine kinase (MNK) domain of UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kina
29 ate (UDP)-sugar donors, UDP-4-deoxy-4-fluoro-N-acetylglucosamine (4FGlcNAc) and UDP-4-deoxy-4-fluoro-
32 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 ent resulting in IgG molecules with only one N-acetylglucosamine and a fucose residue was fully able
39 C in a ligand-free form, in complex with the N-acetylglucosamine and N-acetylgalactosamine products o
41 in to catalyze the in vitro incorporation of N-acetylglucosamine and N-acetylgalactosamine to oligosa
43 typical M. xanthus lipids, fucose, mannose, N-acetylglucosamine and N-acetylgalactoseamine carbohydr
46 nT2 able to utilize both uridine diphosphate N-acetylglucosamine and uridine diphosphate N-acetylgala
47 ng cell wall precursors, UDP-Glucose and UDP-N-acetylglucosamine are efficiently used to initiate tra
52 nsfer of GalNAc to the simple sugar acceptor N-acetylglucosamine-beta-p-nitrophenol (GlcNAcbeta-pNP)
53 l trisaccharide [N-acetylgalactosamine-beta3-N-acetylglucosamine-beta4-(phosphate-6-)mannose] is requ
54 ty to the GalFuc-binding lectin CGL2 and the N-acetylglucosamine-binding lectin XCL, the mutant was r
55 flagellar and type III secretion systems and N-acetylglucosamine-binding protein GpbA while inducing
56 smembrane protein, as well as spermidine and N-acetylglucosamine biosynthesis, all contribute to sura
57 mutation using both the UDP-glucose and UDP-N-acetylglucosamine bound structures of the wild-type pr
58 eptor endocytosis and signaling by promoting N-acetylglucosamine branching of Asn (N)-linked glycans.
61 l for receptor function, and elongation with N-acetylglucosamine, catalyzed by members of the Fringe
64 f et al. (2016) report that detection of the N-acetylglucosamine component of peptidoglycan by the gl
65 hile the UT-A1 in lipid rafts was the mature N-acetylglucosamine-containing form, as detected by whea
66 ains confer recognitional specificity toward N-acetylglucosamine-containing signaling molecules, such
68 inhibitor of UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) in Gram-negative
69 s made of repeating N-acetylmuramic acid and N-acetylglucosamine disaccharides cross-linked by pentap
70 iosynthetic pathway (HBSP) that produces UDP-N-acetylglucosamine for O-linked N-acetylglucosamine mod
72 the pools of UDP-glucose, UDP-galactose, UDP-N-acetylglucosamine, GDP-mannose, and GDP-fucose in Plas
73 nthase 1-3 (HAS1-3) isoenzymes that transfer N-acetylglucosamine (GlcNAc) and glucuronic acid (GlcUA)
74 t sugar-aromatic interactions, with glucose, N-acetylglucosamine (GlcNAc) and mannose in between.
75 oglycan (PGN) consists of repeating units of N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid (M
76 tion of nucleocytoplasmic proteins with beta-N-acetylglucosamine (GlcNAc) and regulates numerous biol
78 tion is altered by deleting two Bdellovibrio N-acetylglucosamine (GlcNAc) deacetylases, one of which
81 diate addition and removal, respectively, of N-acetylglucosamine (GlcNAc) from intracellular protein
82 O-GlcNAc transferase (OGT), which transfers N-acetylglucosamine (GlcNAc) from the nucleotide sugar d
85 iously that varphi11 requires alpha- or beta-N-acetylglucosamine (GlcNAc) moieties on cell wall teich
86 erase that mediates the O-linked addition of N-acetylglucosamine (GlcNAc) moieties to Ser and Thr res
88 described here, is attached to the remaining N-acetylglucosamine (GlcNAc) of IgG, using a mutant endo
91 wide variety of substrates which contain an N-acetylglucosamine (GlcNAc) residue to act as an 'accep
92 -translationally modified by adding O-linked N-acetylglucosamine (GlcNAc) residue to serine or threon
93 modules recognize polysaccharides containing N-acetylglucosamine (GlcNAc) residues including peptidog
94 e reducing end glucose of CPS and the beta-D-N-acetylglucosamine (GlcNAc) residues of peptidoglycan (
96 polyrhamnose backbone with an immunodominant N-acetylglucosamine (GlcNAc) side chain, which is the ba
97 and consists of a polyrhamnose polymer, with N-acetylglucosamine (GlcNAc) side chains, which is an es
100 f core-2 O-glycan branch through addition of N-acetylglucosamine (GlcNAc) to a core-1 O-glycan struct
101 tic Fringe) and MFNG (Manic Fringe) transfer N-acetylglucosamine (GlcNAc) to O-fucose attached to EGF
103 modifies protein function by attaching beta-N-acetylglucosamine (GlcNAc) to serine and threonine res
104 ations of PgaB show a binding preference for N-acetylglucosamine (GlcNAc) to the N-terminal domain an
107 functional homologue of the Candida albicans N-acetylglucosamine (GlcNAc) transporter NGT1, and repre
108 rce for glycolysis and chitobiose to produce N-acetylglucosamine (GlcNAc), a key component of the bac
109 cribed to contain the sugars rhamnose (Rha), N-acetylglucosamine (GlcNAc), galactose (Gal), xylose (X
111 nthesis of a tetra-antennary glycan that has N-acetylglucosamine (GlcNAc), N-acetyllactosamine (LacNA
112 ementation of culture media with uridine and N-acetylglucosamine (GlcNAc), precursors for the hexosam
113 ranslational modification with O-linked beta-N-acetylglucosamine (GlcNAc), promoted apoptosis through
114 em to form hyphae in response to the inducer N-acetylglucosamine (GlcNAc), suggesting that a basal le
115 n death domain-containing host proteins with N-acetylglucosamine (GlcNAc), thereby blocking extrinsic
116 nary glycan [A3(2,4,2) type] terminated with N-acetylglucosamine (GlcNAc), which is generated by N-ac
120 lin, demonstrating that the 6-O-sulfation of N-acetylglucosamine (GlcNAc-6-O-sulfation) is highly con
122 -1 is functionally modified by O-linked beta-N-acetylglucosamine glycosylation (O-GlcNAcylation).
123 on is the presence of a nonreducing terminal N-acetylglucosamine; however, this residue is normally a
124 osamine transferase (OGT), and O-linked beta-N-acetylglucosamine hydrolase in control and IPAH cells
125 erial cells as demonstrated by inhibition of N-acetylglucosamine incorporation into polymeric cell wa
126 In H. jecorina-produced HjCel3A, a single N-acetylglucosamine is present at both sites, whereas in
129 sion of chitin, a beta-1,4 linked polymer of N-acetylglucosamine, is of major interest in areas varyi
131 izes residues that are already modified with N-acetylglucosamine, likely by converting into a relaxed
133 phosphate-N-acetylmuramic acid(pentapeptide)-N-acetylglucosamine (lipid II), which is readily accessi
134 s for a unique phosphotransferase system and N-acetylglucosamine metabolism suggests an important eco
135 roduces UDP-N-acetylglucosamine for O-linked N-acetylglucosamine modification (O-GlcNAcylation) of pr
136 ated by cAMP (EPAC), involving also O-linked N-acetylglucosamine modification downstream of the hexos
137 MCs resulted in reduced global O-linked beta-N-acetylglucosamine modification levels and abrogated PA
138 We measured the levels of O-linked beta-N-acetylglucosamine modification, O-linked beta-N-acetyl
140 the addition of the phosphothreonine to the N-acetylglucosamine moiety and CD0243 transfers the meth
141 trongest interactions are established by the N-acetylglucosamine moiety in the central region of the
142 composed of N-acetylmuramic acid-(beta-1,4)-N-acetylglucosamine (MurNAc-GlcNAc) disaccharides associ
143 ing amino sugars [i.e., N-acetylmuramic acid-N-acetylglucosamine (MurNAc-GlcNAc)] from attached pepti
144 he enzymes phosphomannomutase (PMM), phospho-N-acetylglucosamine mutase (PAGM) and phosphoglucomutase
145 ins was reduced by selective inactivation of N-acetylglucosamine N-deacetylase-N-sulfotransferase (Nd
146 g uniform responses (d-lactose, d-galactose, N-acetylglucosamine, N-acetylneuraminic acid), 'all-or-n
147 motility, decreased chemotactic responses to N-acetylglucosamine (NAG) and attenuated ability to diss
148 ing azides and alkynes were installed on tri-N-acetylglucosamine (NAG)3, a PG mimic, as well as PG is
149 tional addition and removal of O-linked beta-N-acetylglucosamine (O-GlcNAc) also occurs on serine res
150 e signaling pathway, terminating in O-linked-N-acetylglucosamine (O-GlcNAc) cycling, is a key sensor
152 ation controlled by the enzyme O-linked-beta-N-acetylglucosamine (O-GlcNAc) glycosyltransferase as co
153 lear and cytosolic proteins by O-linked beta-N-acetylglucosamine (O-GlcNAc) has been shown to play an
157 slational protein modification O-linked beta-N-acetylglucosamine (O-GlcNAc) is a proposed nutrient se
165 refute the hypothesis of extensive O-linked N-acetylglucosamine (O-GlcNAc) modification of endogenou
169 is study, we show that TAB1 is modified with N-acetylglucosamine (O-GlcNAc) on a single site, Ser395.
170 posttranslational addition of O-linked beta-N-acetylglucosamine (O-GlcNAc) on intracellular proteins
173 this study, we demonstrate that the O-linked N-acetylglucosamine (O-GlcNAc) processing enzymes, O-Glc
174 ost-translational modification O-linked beta-N-acetylglucosamine (O-GlcNAc) regulates thousands of nu
175 cess of interest is the addition of O-linked N-acetylglucosamine (O-GlcNAc) residues onto nuclear and
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 are reversibly glycosylated by O-linked beta-N-acetylglucosamine (O-GlcNAc) to regulate their functio
179 slational addition of a single O-linked beta-N-acetylglucosamine (O-GlcNAc) to serine or threonine re
180 post-translational addition of O-linked beta-N-acetylglucosamine (O-GlcNAc) to various nuclear and cy
185 how that DELLAs are modified by the O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT) SECRET
186 amine biosynthesis pathway and O-linked beta-N-acetylglucosamine (O-GlcNAc) transferase (OGT) to pote
187 t TET2 and TET3 associate with O-linked beta-N-acetylglucosamine (O-GlcNAc) transferase (OGT), an enz
193 ugh a modification in the amount of O-linked N-acetylglucosamine (O-GlcNAc)-modified proteins and in
199 al modification of proteins by O-linked beta-N-acetylglucosamine (O-GlcNAcylation) is a key metabolic
200 lity and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroi
201 al modification of proteins with beta-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression
203 ride beta-N-acetylmuramic acid, (1-->4)-beta-N-acetylglucosamine of staphylococcal peptidoglycan.
207 lammatory and stress responses, and O-linked N-acetylglucosamine (OGN) transferase (OGT), an enzyme t
208 the reaction of free MurA and substrate UDP-N-acetylglucosamine or isomer UDP-N-acetylgalactosamine.
209 o hydrolyze the beta-linkages joining either N-acetylglucosamine or N-acetylgalactosamine to a wide v
211 substrates (a mix of substrates, glutamine, N-acetylglucosamine, or pyruvate) revealed contrasting c
213 nally predicted putative miR-185 targets UDP-N-acetylglucosamine-peptide N-acetylglucosaminyltransfer
217 e conserved cell surface polysaccharide poly-N-acetylglucosamine (PNAG) were effective at mediating r
218 , encoding the biosynthesis of poly-beta-1,6-N-acetylglucosamine (PNAG), a major biofilm matrix compo
219 ne isolate and found to be negative for poly-N-acetylglucosamine (PNAG)-like material by immunoblot a
222 rase O-GlcNAc transferase (uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylaminyltrans
225 2-FGFR1c2 can tolerate an HS chain having an N-acetylglucosamine residue at its non-reducing end.
226 hed to the proximal (reducing-terminal) core N-acetylglucosamine residue of N-glycans by beta1,4-link
228 matode glycan cores, specifically the distal N-acetylglucosamine residue; this result is in accordanc
229 N-glycan structure of seven mannosyl and two N-acetylglucosamine residues (Man7GlcNAc2) on misfolded
230 a linear tetrasaccharide that contained two N-acetylglucosamine residues and a free OH group gave tw
232 olves the attachment of single beta-O-linked N-acetylglucosamine residues to serine and threonine res
233 bonds between N-acetylmuramic acid (NAM) and N-acetylglucosamine residues with concomitant formation
235 illus niger in deglycosylated and Asn-linked N-acetylglucosamine-stub forms reveal a 10(2/3)-turn par
236 r magnetic resonance and shown to contain an N-acetylglucosamine substituted with a phosphorylated N-
237 ble for the selective phosphorylation of the N-acetylglucosamine sugar in a teicoplanin A2-2 derivati
239 The enzymatic addition of a single beta-D-N-acetylglucosamine sugar molecule on serine and/or thre
240 ation consisting of the addition of a single N-acetylglucosamine sugar to serine and threonine residu
241 evated post-translational addition of beta-D-N-acetylglucosamine sugars to nuclear and cytoplasmic pr
242 Evidently, hexosamine pathway activation or N-acetylglucosamine supplementation induces distinct pro
245 esidue is in closer proximity (7.6 A) to the N-acetylglucosamine than the two other sugar rings prese
247 lammasome activation is caused by release of N-acetylglucosamine that is detected in the cytosol by t
248 lytic itineraries for other sugars; for beta-N-acetylglucosamine, the key N-acetyl arm confounds the
249 These results demonstrate that glucose and N-acetylglucosamine, the most readily available chiral b
250 seK3, which is essential for the transfer of N-acetylglucosamine to arginine residues (arginine-GlcNA
253 acetylmannosamine kinase that transforms UDP-N-acetylglucosamine to N-acetylmannosamine (ManNAc) foll
255 -BP1 is also subject to covalent addition of N-acetylglucosamine to Ser or Thr residues (O-GlcNAcylat
256 ne such modification is addition of O-linked N-acetylglucosamine to serine or threonine residues, kno
257 modification involving the O-linkage of beta-N-acetylglucosamine to serine/threonine residues of memb
259 functions as a ligase that adds the terminal N-acetylglucosamine to the lipooligosaccharide core of Y
260 The essential mammalian enzyme O-linked beta-N-acetylglucosamine transferase (O-GlcNAc transferase, h
261 s involved in cell metabolism: O-linked beta-N-acetylglucosamine transferase (OGT) and isocitrate deh
265 tumors from colon tumor cells with O-linked N-acetylglucosamine transferase (OGT) knockdown grew sig
266 cetylglucosamine modification, O-linked beta-N-acetylglucosamine transferase (OGT), and O-linked beta
267 ts with host cell factor-1 (HCF-1), O-linked N-acetylglucosamine transferase (OGT), and the polycomb
268 dues in proteins by the enzyme O-linked beta-N-acetylglucosamine transferase (OGT), whereas the enzym
269 ces an essential substrate for O-linked beta-N-acetylglucosamine transferase (OGT), which glycosylate
271 C also interacts with the O-GlcNAc (O-linked N-acetylglucosamine) transferase SPINDLY required for pr
272 GOLPH3 supports incorporation of both core 2 N-acetylglucosamine-transferase 1 and alpha-2,6-sialyltr
274 that EXTL2 exhibited much stronger in vitro N-acetylglucosamine-transferase activity related to elon
276 galactose transporter (UGT; SLC35A2) and UDP-N-acetylglucosamine transporter (NGT; SLC35A3) form hete
277 65000) as an ER-localized facilitator of UDP-N-acetylglucosamine (UDP-GlcNAc) and UDP-N-acetylgalacto
279 exosamine biosynthetic pathway, increase UDP-N-acetylglucosamine (UDP-GlcNAc) availability, and lead
280 d thatlymphostatin binds uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) but not UDP-glucose (UD
281 pathway (HBP) generates uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) for glycan synthesis an
285 rikingly, addition of the HBP metabolite UDP-N-acetylglucosamine (UDP-GlcNAc) to CRPC-like cells sign
286 the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine (UDP-GlcNAc) to serines and threonin
287 intracellular levels of uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc), a key precursor of Lac
288 tamine are precursors of uridine diphosphate N-acetylglucosamine (UDP-GlcNAc), a substrate for cellul
289 -biosynthesis precursor, uridine diphosphate N-acetylglucosamine (UDP-GlcNAc), was monitored by recor
294 DP-glucuronic acid, and UGT3 enzymes use UDP-N-acetylglucosamine, UDP-glucose, and UDP-xylose to conj
295 el, ChiA variants with weaker binding of the N-acetylglucosamine unit either in substrate-binding sit
296 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 step in the synthesis of uridine diphosphate N-acetylglucosamine, which is required for the biosynthe
299 version of UDP-N-acetylgalactosamine and UDP-N-acetylglucosamine while the bacterial enzyme cannot.
300 y beta4 addition of N-acetylgalactosamine to N-acetylglucosamine with formation of the N,N-diacetylla
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