PMID-sentid Pub_year Sent_text compound_name comp_offset prot_official_name organism prot_offset 15632313-1 2004 The biosynthesis of the carbohydrate antigen sialyl Lewis X (sLe(x)) in human leukocytes is mediated by alpha1-3 fucosyltransferase-VII (FucT-VII), which catalyzes the transfer of fucose from GDP-beta-fucose to the 3-OH of alpha2-3 sialyl N-acetyllactosamine (SA-LN). N-acetyllactosamine 239-258 fucosyltransferase 7 Homo sapiens 137-145 14733546-1 2004 Chemical syntheses are reported for prostate specific antigen (PSA) N-linked glycopeptide fragments consisting of an uneicosapeptide (residues 27-47 of PSA) with di-, tri-, and tetrabranched N-acetyllactosamine-type glycans. N-acetyllactosamine 191-210 kallikrein related peptidase 3 Homo sapiens 36-61 14672941-4 2004 Recent sedimentation equilibrium and velocity studies show that murine galectin-3 is a monomer in the absence and presence of LacNAc, a monovalent sugar. N-acetyllactosamine 126-132 lectin, galactose binding, soluble 3 Mus musculus 71-81 14672941-5 2004 However, quantitative precipitation studies in the present report indicate that galectin-3 precipitates as a pentamer with a series of divalent pentasaccharides with terminal LacNAc residues. N-acetyllactosamine 175-181 lectin, galactose binding, soluble 3 Mus musculus 80-90 15009185-6 2004 Sugar binding assays revealed that N-acetyl-lactosamine, mannose and N-acetyl-glucosamine residues widely expressed in human placenta had the strongest binding affinity to both the purified and recombinant PP13/galectin-13, which also effectively agglutinated erythrocytes. N-acetyllactosamine 35-55 galectin 13 Homo sapiens 206-210 15009185-6 2004 Sugar binding assays revealed that N-acetyl-lactosamine, mannose and N-acetyl-glucosamine residues widely expressed in human placenta had the strongest binding affinity to both the purified and recombinant PP13/galectin-13, which also effectively agglutinated erythrocytes. N-acetyllactosamine 35-55 galectin 13 Homo sapiens 211-222 14693912-5 2004 Like mammalian prototype galectin-1, Drgal1-L2 preferentially binds to N-acetyllactosamine. N-acetyllactosamine 71-90 galectin 1 Homo sapiens 25-35 14693912-5 2004 Like mammalian prototype galectin-1, Drgal1-L2 preferentially binds to N-acetyllactosamine. N-acetyllactosamine 71-90 lectin, galactoside-binding, soluble, 2a Danio rerio 37-46 14698884-2 2004 Sialoadhesin (siglec-1) is expressed at much higher levels in inflammatory macrophages and specifically binds to alpha-2,3-sialylated N-acetyl lactosamine residues of glycan chains. N-acetyllactosamine 134-154 sialic acid binding Ig like lectin 1 Homo sapiens 0-12 14698884-2 2004 Sialoadhesin (siglec-1) is expressed at much higher levels in inflammatory macrophages and specifically binds to alpha-2,3-sialylated N-acetyl lactosamine residues of glycan chains. N-acetyllactosamine 134-154 sialic acid binding Ig like lectin 1 Homo sapiens 14-22 15148296-6 2004 In the present study, binding of bovine heart galectin-1 and recombinant murine galectin-3 to a series of synthetic analogs containing two LacNAc residues separated by a varying number of methylene groups, as well as biantennary analogs possessing two LacNAc residues, were examined using isothermal titration microcalorimetry (ITC) and hemagglutination inhibition measurements. N-acetyllactosamine 252-258 lectin, galactose binding, soluble 3 Mus musculus 80-90 14993226-6 2004 Subsequently, we determined the first x-ray crystal structures of human GlcAT-P, in the absence and presence of a donor substrate product UDP, catalytic Mn(2+), and an acceptor substrate analogue N-acetyllactosamine (Galbeta1-4GlcNAc) or an asparagine-linked biantennary nonasaccharide. N-acetyllactosamine 196-215 beta-1,3-glucuronyltransferase 1 Homo sapiens 72-79 15081009-1 2004 A range of N-acetyllactosamine derivatives, which are modified by a wide range of functionalities at C-2(") and C-6, have been synthesised and the kinetic parameters of transfer catalysed by recombinant alpha-2,6-sialyltransferase and alpha-1,3-fucoyltransferase VI determined. N-acetyllactosamine 11-30 complement C2 Homo sapiens 101-104 15081009-1 2004 A range of N-acetyllactosamine derivatives, which are modified by a wide range of functionalities at C-2(") and C-6, have been synthesised and the kinetic parameters of transfer catalysed by recombinant alpha-2,6-sialyltransferase and alpha-1,3-fucoyltransferase VI determined. N-acetyllactosamine 11-30 complement C6 Homo sapiens 112-115 14733546-1 2004 Chemical syntheses are reported for prostate specific antigen (PSA) N-linked glycopeptide fragments consisting of an uneicosapeptide (residues 27-47 of PSA) with di-, tri-, and tetrabranched N-acetyllactosamine-type glycans. N-acetyllactosamine 191-210 kallikrein related peptidase 3 Homo sapiens 63-66 14673092-5 2003 We found that the majority of the O-glycans that are linked to mZP3 are core type 2 sequences terminated with sialic acid, lacNAc (Galbeta1-4GlcNAc), lacdiNAc (Gal-NAcbeta1-4GlcNAc), Galalpha1-3Gal, and NeuAcalpha2-3[GalNAcbeta1-4]Galbeta1-4 (Sda antigen). N-acetyllactosamine 123-129 zona pellucida glycoprotein 3 Mus musculus 63-67 12714507-2 2003 Several glycosyltransferases act successively to extend the N-acetyl lactosamine repeats and to synthesize sLex, and beta-1,4-galactosyltransferase (beta4GalT) plays a key role in these processes. N-acetyllactosamine 60-80 UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 1 Mus musculus 117-147 14664380-1 2003 N-Acetyllactosamine derivative 4, which has a methylene amide tether between C-6 and C-2", was enzymatically glycosylated using rat liver alpha-2,6-sialyltransferase (ST6GalI) or recombinant human fucosyltransferase V (FucT-V) to give conformationally constrained trisaccharides 5 and 6, respectively. N-acetyllactosamine 0-19 complement C6 Rattus norvegicus 77-80 14664380-1 2003 N-Acetyllactosamine derivative 4, which has a methylene amide tether between C-6 and C-2", was enzymatically glycosylated using rat liver alpha-2,6-sialyltransferase (ST6GalI) or recombinant human fucosyltransferase V (FucT-V) to give conformationally constrained trisaccharides 5 and 6, respectively. N-acetyllactosamine 0-19 complement C2 Rattus norvegicus 85-88 14664380-1 2003 N-Acetyllactosamine derivative 4, which has a methylene amide tether between C-6 and C-2", was enzymatically glycosylated using rat liver alpha-2,6-sialyltransferase (ST6GalI) or recombinant human fucosyltransferase V (FucT-V) to give conformationally constrained trisaccharides 5 and 6, respectively. N-acetyllactosamine 0-19 ST6 beta-galactoside alpha-2,6-sialyltransferase 1 Rattus norvegicus 167-174 14664380-1 2003 N-Acetyllactosamine derivative 4, which has a methylene amide tether between C-6 and C-2", was enzymatically glycosylated using rat liver alpha-2,6-sialyltransferase (ST6GalI) or recombinant human fucosyltransferase V (FucT-V) to give conformationally constrained trisaccharides 5 and 6, respectively. N-acetyllactosamine 0-19 fucosyltransferase 5 Homo sapiens 197-217 14664380-1 2003 N-Acetyllactosamine derivative 4, which has a methylene amide tether between C-6 and C-2", was enzymatically glycosylated using rat liver alpha-2,6-sialyltransferase (ST6GalI) or recombinant human fucosyltransferase V (FucT-V) to give conformationally constrained trisaccharides 5 and 6, respectively. N-acetyllactosamine 0-19 fucosyltransferase 5 Homo sapiens 219-225 14664380-4 2003 The apparent kinetic parameters of transfer to LacNAc and conformationally constrained saccharides 3 and 4 indicates that fucosyltransferase V recognize LacNAc in its A-conformer whereas alpha-2,6-sialyltransferase recognizes the B-conformer of LacNAc. N-acetyllactosamine 47-53 fucosyltransferase 5 Homo sapiens 122-142 14664380-4 2003 The apparent kinetic parameters of transfer to LacNAc and conformationally constrained saccharides 3 and 4 indicates that fucosyltransferase V recognize LacNAc in its A-conformer whereas alpha-2,6-sialyltransferase recognizes the B-conformer of LacNAc. N-acetyllactosamine 153-159 fucosyltransferase 5 Homo sapiens 122-142 14664380-4 2003 The apparent kinetic parameters of transfer to LacNAc and conformationally constrained saccharides 3 and 4 indicates that fucosyltransferase V recognize LacNAc in its A-conformer whereas alpha-2,6-sialyltransferase recognizes the B-conformer of LacNAc. N-acetyllactosamine 153-159 fucosyltransferase 5 Homo sapiens 122-142 14517974-3 2003 A number of developmental and regulatory processes have been attributed to the ability of galectin-1 to bind a variety of oligosaccharides containing the Gal-beta-(1,4)-GlcNAc (LacNAc(II)) sequence. N-acetyllactosamine 177-183 galectin 1 Homo sapiens 90-100 14517974-6 2003 The MD results indicate that a set of anchoring interactions between the galectin-1 carbohydrate recognition domain (CRD) and the LacNAc core are maintained for a diverse set of ligands and that substituents at the nonreducing terminus of the oligosaccharide extend into the remainder of a characteristic surface groove. N-acetyllactosamine 130-136 galectin 1 Homo sapiens 73-83 14624649-4 2003 Treatment of GlcNAc-DNA with beta-1,4-galactosyl transferase (GalT) and UDP-Gal produced N-acetyllactosamine-modified DNA (LacNAc-DNA), which could be converted quantitatively to the trisaccharide Lewis X (LeX)-DNA conjugate by alpha-1,3-fucosyltransferase VI (FucT) and GDP-Fuc. N-acetyllactosamine 89-108 galactose-1-phosphate uridylyltransferase Homo sapiens 29-60 14624649-4 2003 Treatment of GlcNAc-DNA with beta-1,4-galactosyl transferase (GalT) and UDP-Gal produced N-acetyllactosamine-modified DNA (LacNAc-DNA), which could be converted quantitatively to the trisaccharide Lewis X (LeX)-DNA conjugate by alpha-1,3-fucosyltransferase VI (FucT) and GDP-Fuc. N-acetyllactosamine 89-108 galactose-1-phosphate uridylyltransferase Homo sapiens 62-66 14624649-4 2003 Treatment of GlcNAc-DNA with beta-1,4-galactosyl transferase (GalT) and UDP-Gal produced N-acetyllactosamine-modified DNA (LacNAc-DNA), which could be converted quantitatively to the trisaccharide Lewis X (LeX)-DNA conjugate by alpha-1,3-fucosyltransferase VI (FucT) and GDP-Fuc. N-acetyllactosamine 89-108 fucosyltransferase 4 Homo sapiens 206-209 14624649-4 2003 Treatment of GlcNAc-DNA with beta-1,4-galactosyl transferase (GalT) and UDP-Gal produced N-acetyllactosamine-modified DNA (LacNAc-DNA), which could be converted quantitatively to the trisaccharide Lewis X (LeX)-DNA conjugate by alpha-1,3-fucosyltransferase VI (FucT) and GDP-Fuc. N-acetyllactosamine 123-129 galactose-1-phosphate uridylyltransferase Homo sapiens 29-60 14624649-4 2003 Treatment of GlcNAc-DNA with beta-1,4-galactosyl transferase (GalT) and UDP-Gal produced N-acetyllactosamine-modified DNA (LacNAc-DNA), which could be converted quantitatively to the trisaccharide Lewis X (LeX)-DNA conjugate by alpha-1,3-fucosyltransferase VI (FucT) and GDP-Fuc. N-acetyllactosamine 123-129 galactose-1-phosphate uridylyltransferase Homo sapiens 62-66 14624649-4 2003 Treatment of GlcNAc-DNA with beta-1,4-galactosyl transferase (GalT) and UDP-Gal produced N-acetyllactosamine-modified DNA (LacNAc-DNA), which could be converted quantitatively to the trisaccharide Lewis X (LeX)-DNA conjugate by alpha-1,3-fucosyltransferase VI (FucT) and GDP-Fuc. N-acetyllactosamine 123-129 fucosyltransferase 4 Homo sapiens 206-209 12714507-2 2003 Several glycosyltransferases act successively to extend the N-acetyl lactosamine repeats and to synthesize sLex, and beta-1,4-galactosyltransferase (beta4GalT) plays a key role in these processes. N-acetyllactosamine 60-80 UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 1 Mus musculus 149-158 12868597-9 2003 Binding of Galbeta1 - 3GalNAc- or LacNAc-specific reagents (lectins and antibodies) to apoptotic bodies abolished their engulfment by the THP-1 cells whereas blocking of Neu5Acalpha2 - 6 or Neu5Acalpha2 - 3 sites by the corresponding lectins was not effective. N-acetyllactosamine 34-40 GLI family zinc finger 2 Homo sapiens 138-143 12859199-2 2003 Restriction of conformational mobility was achieved by introducing tethers of different length and chemical composition between the C-6 and C-2" hydroxyl of LacNAc. N-acetyllactosamine 157-163 complement C2 Homo sapiens 140-143 12859199-5 2003 The ethylene-tethered 6 can attain conformations in the relatively large energy plateau of LacNAc that include syn conformations A and B, whereas compound 7, which is modified by a methylamide tether, can only reside in the B-conformer. N-acetyllactosamine 91-97 synemin Homo sapiens 111-114 12499401-1 2002 Alpha(1,3)Galactosyltransferase (GT) is a Golgi-localized enzyme that catalyzes the transfer of a terminal galactose to N-acetyllactosamine to create Galalpha(1,3)Gal. N-acetyllactosamine 120-139 N-acetyllactosaminide alpha-1,3-galactosyltransferase Sus scrofa 0-31 12382235-0 2002 Terminal alpha-linked galactose rather than N-acetyl lactosamine is ligand for bovine heart galectin-1 in N-linked oligosaccharides of glycoproteins. N-acetyllactosamine 44-64 galectin 1 Bos taurus 92-102 12244074-9 2002 Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. N-acetyllactosamine 79-85 tumor necrosis factor Homo sapiens 13-22 12244074-9 2002 Furthermore, TNF-alpha induced the expression of 6-sulfo N-acetyl lactosamine (LacNAc)/Lewis x on these cells, which was detected by a monoclonal antibody after neuraminidase treatment. N-acetyllactosamine 79-85 neuraminidase 1 Homo sapiens 161-174 12466366-3 2002 Using lectins as carbohydrate probes, we have identified two common mucin oligosaccharide structures, T antigen and N-acetyllactosamine, within secretory granules in human endocervical glands during the proliferative phase of the menstrual cycle. N-acetyllactosamine 116-135 LOC100508689 Homo sapiens 68-73 11988021-7 2002 Last, sialylated and nonsialylated variants of N-acetyllactosamine differentially modulated AChR clustering and agrin activity, and these changes correlated with the ability of MuSK, an agrin-stimulated kinase, to bind to these structures. N-acetyllactosamine 47-66 agrin Homo sapiens 112-117 12107078-1 2002 alpha1,3-Fucosyltransferases (Fuc-Ts) convert N-acetyllactosamine (LN, Galbeta1-4GlcNAc) to Galbeta1-4(Fucalpha1-3)GlcNAc, the Lewis x (CD15, SSEA-1) epitope, which is involved in various recognition phenomena. N-acetyllactosamine 46-65 fucosyltransferase 4 Homo sapiens 136-140 11891229-2 2002 The HNK-1 glycan synthesis is initiated by the addition of beta1,3-linked GlcA to N-acetyllactosamine followed by sulfation of the C-3 position of GlcA. N-acetyllactosamine 82-101 beta-1,3-glucuronyltransferase 1 Homo sapiens 4-9 11891229-2 2002 The HNK-1 glycan synthesis is initiated by the addition of beta1,3-linked GlcA to N-acetyllactosamine followed by sulfation of the C-3 position of GlcA. N-acetyllactosamine 82-101 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 59-66 12042249-7 2002 The soluble form of CD59, expressed in CHO cells without the GPI anchor signal sequence, consisted almost entirely (97%) of biantennary glycans, of which 81% were unmodified, 17% contained one N-acetyllactosamine extension, and 2% contained two extensions. N-acetyllactosamine 193-212 CD59 glycoprotein Cricetulus griseus 20-24 11988021-7 2002 Last, sialylated and nonsialylated variants of N-acetyllactosamine differentially modulated AChR clustering and agrin activity, and these changes correlated with the ability of MuSK, an agrin-stimulated kinase, to bind to these structures. N-acetyllactosamine 47-66 agrin Homo sapiens 186-191 11921396-0 2002 Low micromolar inhibitors of galectin-3 based on 3"-derivatization of N-acetyllactosamine. N-acetyllactosamine 70-89 galectin 3 Homo sapiens 29-39 11737213-4 2001 Evidence could be provided that polysialylated murine N-CAM glycans comprise diantennary, triantennary and tetraantennary core structures carrying, in part, type-1 N-acetyllactosamine antennae, sulfate groups linked to terminal galactose or subterminal N-acetylglucosamine residues and, as a characteristic feature, a sulfated glucuronic acid unit which was bound exclusively to C3 of terminal galactose in Manalpha3-linked type-2 antennae. N-acetyllactosamine 164-183 neural cell adhesion molecule 1 Mus musculus 54-59 11604544-1 2001 The binding of a nitroxide spin-labeled analog of N-acetyllactosamine to galectin-3, a mammalian lectin of 26 kD size, is studied to map the binding sites of this small oligosaccharide on the protein surface. N-acetyllactosamine 50-69 spindlin 1 Homo sapiens 27-31 11604544-1 2001 The binding of a nitroxide spin-labeled analog of N-acetyllactosamine to galectin-3, a mammalian lectin of 26 kD size, is studied to map the binding sites of this small oligosaccharide on the protein surface. N-acetyllactosamine 50-69 galectin 3 Homo sapiens 73-83 11604544-2 2001 Perturbation of intensities of cross-peaks in the (15)N heteronuclear single quantum coherence (HSQC) spectrum of full-length galectin-3 owing to the bound spin label is used qualitatively to identify protein residues proximate to the binding site for N-acetyllactosamine. N-acetyllactosamine 252-271 galectin 3 Homo sapiens 126-136 11604544-2 2001 Perturbation of intensities of cross-peaks in the (15)N heteronuclear single quantum coherence (HSQC) spectrum of full-length galectin-3 owing to the bound spin label is used qualitatively to identify protein residues proximate to the binding site for N-acetyllactosamine. N-acetyllactosamine 252-271 spindlin 1 Homo sapiens 156-160 11217864-5 2001 Mgat5 initiates GlcNAc beta1,6 branching on N-glycans, thereby increasing N-acetyllactosamine, the ligand for galectins, which are proteins known to modulate T-cell proliferation and apoptosis. N-acetyllactosamine 74-93 alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase Homo sapiens 0-5 11742106-7 2001 By docking simulations PP13 possessed sugar-binding activity with highest affinity to N-acetyllactosamine and lactose typical of most galectins. N-acetyllactosamine 86-105 galectin 13 Homo sapiens 23-27 11323440-9 2001 Northern blot analysis demonstrated that transcripts for Gal3ST-3 are predominantly expressed in the brain, kidney, and thyroid where the presence of 3"-sulfation of N-acetyllactosamine has been reported. N-acetyllactosamine 166-185 galactose-3-O-sulfotransferase 3 Homo sapiens 57-65 11323440-10 2001 These results indicate that the newly cloned Gal3ST-3 plays a critical role in 3"-sulfation of N-acetyllactosamine in both O- and N-glycans. N-acetyllactosamine 95-114 galactose-3-O-sulfotransferase 3 Homo sapiens 45-53 11384981-9 2001 In addition to the initiating activity for lacto-chain synthesis, the Lc3 synthase could extend the terminal N-acetyllactosamine unit of nLc4 and also had a broad specificity for gangliosides GA1, GM1, and GD1b to generate neolacto-ganglio hybrid structures. N-acetyllactosamine 109-128 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5 Mus musculus 70-82 11323440-2 2001 The newly isolated cDNA encodes a novel 3-O-sulfotransferase, termed Gal3ST-3, that acts exclusively on N-acetyllactosamine present in N-glycans and core2-branched O-glycans. N-acetyllactosamine 104-123 galactose-3-O-sulfotransferase 3 Homo sapiens 69-77 11217864-5 2001 Mgat5 initiates GlcNAc beta1,6 branching on N-glycans, thereby increasing N-acetyllactosamine, the ligand for galectins, which are proteins known to modulate T-cell proliferation and apoptosis. N-acetyllactosamine 74-93 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 23-30 11511812-4 2000 The GlcAT-P is highly specific for the terminal N-acetyllactosamine structure and no glucuronic acid was incorporated into a Galbeta1-3GlcNAc moiety. N-acetyllactosamine 48-67 beta-1,3-glucuronyltransferase 1 Rattus norvegicus 4-11 11114588-3 2001 Intact ZPB and ZPC cannot be separated from each other unless acidic N-acetyllactosamine regions of their carbohydrate chains are removed by endo-beta-galactosidase digestion. N-acetyllactosamine 69-88 zona pellucida glycoprotein 4 Sus scrofa 7-10 11511812-5 2000 The GlcAT-P transferred glucuronic acid to the galactose residues in the N-acetyllactosamine branches of bi-, tri-, and tetra-antennary oligosaccharide chains, with different efficiencies and most preferentially to those in the Galbeta1-4GlcNAcbeta1-4Manalpha1-3 branch. N-acetyllactosamine 73-92 beta-1,3-glucuronyltransferase 1 Rattus norvegicus 4-11 11087716-3 2000 Hydrazine/nitrous acid/NaBH(4) treatment of the HA from the subcellular fractions indicated that C-3 of the galactose as well as C-6 of the N-acetylglucosamine residues of the N-acetyllactosamine chains became sulfated in these post ER fractions, as did the C-6 of the outer N-acetylglucosamine of the di-N-acetylchitobiose core. N-acetyllactosamine 176-195 complement C3 Canis lupus familiaris 97-100 11087716-3 2000 Hydrazine/nitrous acid/NaBH(4) treatment of the HA from the subcellular fractions indicated that C-3 of the galactose as well as C-6 of the N-acetylglucosamine residues of the N-acetyllactosamine chains became sulfated in these post ER fractions, as did the C-6 of the outer N-acetylglucosamine of the di-N-acetylchitobiose core. N-acetyllactosamine 176-195 complement C6 Canis lupus familiaris 129-132 11087716-3 2000 Hydrazine/nitrous acid/NaBH(4) treatment of the HA from the subcellular fractions indicated that C-3 of the galactose as well as C-6 of the N-acetylglucosamine residues of the N-acetyllactosamine chains became sulfated in these post ER fractions, as did the C-6 of the outer N-acetylglucosamine of the di-N-acetylchitobiose core. N-acetyllactosamine 176-195 complement C6 Canis lupus familiaris 258-261 10652309-3 2000 While both CTB and LTB bind to the GM1 ganglioside, LTB also binds to N-acetyllactosamine-terminated glycoconjugates. N-acetyllactosamine 70-89 lymphotoxin beta Homo sapiens 52-55 10766765-6 2000 By using a newly established method, we found that ST8Sia IV, ST8Sia II, and ST8Sia III all add oligosialic and polysialic acid on various sialylated N-acetyllactosaminyl oligosaccharides, including NCAM N-glycans, fetuin N-glycans, synthetic sialylated N-acetyllactosamines, and on alpha(2)-HS-glycoprotein. N-acetyllactosamine 254-274 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 4 Homo sapiens 51-60 10766765-6 2000 By using a newly established method, we found that ST8Sia IV, ST8Sia II, and ST8Sia III all add oligosialic and polysialic acid on various sialylated N-acetyllactosaminyl oligosaccharides, including NCAM N-glycans, fetuin N-glycans, synthetic sialylated N-acetyllactosamines, and on alpha(2)-HS-glycoprotein. N-acetyllactosamine 254-274 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 2 Homo sapiens 62-71 10766765-6 2000 By using a newly established method, we found that ST8Sia IV, ST8Sia II, and ST8Sia III all add oligosialic and polysialic acid on various sialylated N-acetyllactosaminyl oligosaccharides, including NCAM N-glycans, fetuin N-glycans, synthetic sialylated N-acetyllactosamines, and on alpha(2)-HS-glycoprotein. N-acetyllactosamine 254-274 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 3 Homo sapiens 77-87 10766765-6 2000 By using a newly established method, we found that ST8Sia IV, ST8Sia II, and ST8Sia III all add oligosialic and polysialic acid on various sialylated N-acetyllactosaminyl oligosaccharides, including NCAM N-glycans, fetuin N-glycans, synthetic sialylated N-acetyllactosamines, and on alpha(2)-HS-glycoprotein. N-acetyllactosamine 254-274 neural cell adhesion molecule 1 Homo sapiens 199-203 10845774-0 2000 N-acetyllactosamine and the CT carbohydrate antigen mediate agrin-dependent activation of MuSK and acetylcholine receptor clustering in skeletal muscle. N-acetyllactosamine 0-19 agrin Homo sapiens 60-65 10845774-0 2000 N-acetyllactosamine and the CT carbohydrate antigen mediate agrin-dependent activation of MuSK and acetylcholine receptor clustering in skeletal muscle. N-acetyllactosamine 0-19 muscle associated receptor tyrosine kinase Homo sapiens 90-94 10913832-6 2000 From the glycovariant mTf-III two isomers of a conventional biantennary N-acetyllactosamine type were isolated, in which two N-glycolylneuraminic acid (Neu5Gc) residues are linked to galactose either by a (alpha 2-6) or (alpha 2-3) linkage. N-acetyllactosamine 72-91 immunoglobulin binding protein 1 Homo sapiens 206-215 10929806-3 2000 As a set of convenient fluorogenic substrates for continuous monitoring of sialyltransferase activities, we designed and synthesized a novel CMP-Neu5Ac derivative with a naphthylmethyl group at the C-9 position and N-acetyllactosamine derivative containing a dansyl group at the terminal position of aglycon. N-acetyllactosamine 215-234 ST6 beta-galactoside alpha-2,6-sialyltransferase 2 Homo sapiens 75-92 10891123-8 2000 Double reciprocal analysis showed that the inhibition of Fuc-TVI by 1 displays a mixed pattern with respect to both the donor sugar GDP-fucose and the acceptor LacNAc with K(i) of 123 and 128 microM, respectively. N-acetyllactosamine 160-166 fucosyltransferase 6 Homo sapiens 57-64 10839980-0 2000 Glycosylation-site-selective synthesis of N-acetyl-lactosamine repeats in bis-glycosylated human lysozyme. N-acetyllactosamine 42-62 lysozyme Homo sapiens 97-105 10747980-4 2000 We also found that iGnT acts less efficiently on acceptors containing increasing numbers of N-acetyllactosamine repeats, in contrast to beta4Gal-TI, which exhibits no significant change. N-acetyllactosamine 92-111 beta-1,4-glucuronyltransferase 1 Homo sapiens 19-23 10747980-5 2000 In O-glycan biosynthesis, N-acetyllactosamine extension of core 4 branches was found to be synthesized most efficiently by iGnT and beta4Gal-TI, in contrast to core 2 branch synthesis, which requires iGnT and beta4Gal-TIV. N-acetyllactosamine 26-45 beta-1,4-glucuronyltransferase 1 Homo sapiens 123-127 10747980-5 2000 In O-glycan biosynthesis, N-acetyllactosamine extension of core 4 branches was found to be synthesized most efficiently by iGnT and beta4Gal-TI, in contrast to core 2 branch synthesis, which requires iGnT and beta4Gal-TIV. N-acetyllactosamine 26-45 beta-1,4-glucuronyltransferase 1 Homo sapiens 200-204 10747980-5 2000 In O-glycan biosynthesis, N-acetyllactosamine extension of core 4 branches was found to be synthesized most efficiently by iGnT and beta4Gal-TI, in contrast to core 2 branch synthesis, which requires iGnT and beta4Gal-TIV. N-acetyllactosamine 26-45 beta-1,4-galactosyltransferase 5 Homo sapiens 209-221 10737323-3 1999 The fragment ions B1 produced by the cleavage of alpha2-3 sialyl linkages indicate much higher intensity than those produced by the cleavage of alpha2-6 sialyl linkages in sialyllactoses and sialyl-N-acetyllactosamines. N-acetyllactosamine 198-218 immunoglobulin binding protein 1 Homo sapiens 144-152 10601850-5 2000 We assume that H-type alpha(1,2)-fucosyltransferase competes with the endogenous alpha(2,3)-sialyltransferase for the N-acetyllactosamine structures assigned to further serve as acceptors for alpha(1, 3)fucosyltransferase. N-acetyllactosamine 118-137 adrenoceptor alpha 1D Homo sapiens 22-31 10601850-5 2000 We assume that H-type alpha(1,2)-fucosyltransferase competes with the endogenous alpha(2,3)-sialyltransferase for the N-acetyllactosamine structures assigned to further serve as acceptors for alpha(1, 3)fucosyltransferase. N-acetyllactosamine 118-137 fucosyltransferase 7 Homo sapiens 192-221 10567735-7 1999 In adult rat, the galectin-1 ligand, N-acetyl-lactosamine, was expressed by primary olfactory axons that terminated in glomeruli present in the ventromedial and lateral olfactory bulb. N-acetyllactosamine 37-57 galectin 1 Rattus norvegicus 18-28 10536036-8 1999 Once an N -acetyllactosamine unit is synthesized, alpha1-3-fucosylation of the GlcNAc residue to generate a Lewis x structure blocks any further substitution. N-acetyllactosamine 8-28 adrenoceptor alpha 1D Homo sapiens 50-58 11003555-3 1999 We found bi-, tri- and tetraantennary complex-type sugar chains with one or two N-acetyllactosamine repeats, which are common to recombinant human EPO produced in CHO cells. N-acetyllactosamine 80-99 erythropoietin Homo sapiens 147-150 11003555-4 1999 On the other hand, there were triantennary sugar chains with one or two N-acetyllactosamine repeats that were specific to the recombinant human TPO, and their distributions of branch structures were also different. N-acetyllactosamine 72-91 thrombopoietin Homo sapiens 144-147 10504403-6 1999 Most glycan structures are proximally alpha1-6-fucosylated, diantennary complex-type bearing nonsialylated or alpha2-6-sialylated N-acetyllactosamine or di-N-acetyllactosamine antennae. N-acetyllactosamine 130-149 immunoglobulin binding protein 1 Homo sapiens 110-118 10504403-7 1999 The majority of nonsialylated N-acetyllactosamine antennae bear terminal alpha1-3-linked Gal residues. N-acetyllactosamine 30-49 adrenoceptor alpha 1D Homo sapiens 73-81 10350056-6 1999 These results suggest that beta4-GalT V may function in the synthesis of lacNAc units on O-linked chains, particularly in tissues which do not express beta4-GalT I, such as brain. N-acetyllactosamine 73-79 beta-1,4-galactosyltransferase 5 Homo sapiens 27-39 10358011-7 1999 Taken together, these results indicate that the complemental branch specificity of iGnT and beta4Gal-TI leads to efficient and equal addition of N-acetyllactosamine repeats on both side chains of GlcNAcbeta1-->6(GlcNAcbeta1-->2)Manalpha1-->6Manbet a-->R structure, which is consistent with the structures found in nature. N-acetyllactosamine 145-164 glucosaminyl (N-acetyl) transferase 2 (I blood group) Homo sapiens 83-87 10350056-6 1999 These results suggest that beta4-GalT V may function in the synthesis of lacNAc units on O-linked chains, particularly in tissues which do not express beta4-GalT I, such as brain. N-acetyllactosamine 73-79 galactose-1-phosphate uridylyltransferase Homo sapiens 33-37 10089209-8 1999 These results indicate that, for oligomers containing up to eight sugars, the principal interaction of the binding site of galectin-1 is with the terminal N-acetyllactosamine residues. N-acetyllactosamine 155-174 galectin 1 Homo sapiens 123-133 10369126-1 1999 Galectin-1 binds preferentially to N-acetyllactosamine residues on oligosaccharides associated with several cell surface glycoconjugates. N-acetyllactosamine 35-54 galectin 1 Homo sapiens 0-10 10092606-1 1999 Concerted actions by I-extension enzyme, I-branching enzyme, and beta1,4-galactosyltransferase I. I-branched poly-N-acetyllactosamine is a unique carbohydrate composed of N-acetyllactosamine branches attached to linear poly-N-acetyllactosamine, which is synthesized by I-branching beta1, 6-N-acetylglucosaminyltransferase. N-acetyllactosamine 114-133 glucosaminyl (N-acetyl) transferase 1 Homo sapiens 281-321 10092606-3 1999 In the present study, we first demonstrate that I-branching beta1, 6-N-acetylglucosaminyltransferase cloned from human PA-1 embryonic carcinoma cells transfers beta1,6-linked GlcNAc preferentially to galactosyl residues of N-acetyllactosamine close to nonreducing terminals. N-acetyllactosamine 223-242 glucosaminyl (N-acetyl) transferase 1 Homo sapiens 60-100 10089214-5 1999 Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. N-acetyllactosamine 67-73 motor neuron and pancreas homeobox 1 Homo sapiens 81-84 10360315-1 1999 The I antigen appears on human cells in the postnatal period, by addition of N-acetyllactosamine (beta 1-6) branching to the fetal i antigen structure, which is specified by linear oligo N-acetyllactosamine (beta 1-3) chain. N-acetyllactosamine 77-96 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 98-104 9760227-2 1998 Here we report the crystal structure of human galectin-7 (hGal-7), in free form and in the presence of galactose, galactosamine, lactose, and N-acetyl-lactosamine at high resolution. N-acetyllactosamine 142-162 galectin 7 Homo sapiens 46-56 10091584-6 1999 ZPB and ZPC can not be separated from each other unless the acidic N-acetyllactosamine regions of their carbohydrate chains are removed by endo-beta-galactosidase digestion. N-acetyllactosamine 67-86 zona pellucida glycoprotein 4 Sus scrofa 0-3 10091584-6 1999 ZPB and ZPC can not be separated from each other unless the acidic N-acetyllactosamine regions of their carbohydrate chains are removed by endo-beta-galactosidase digestion. N-acetyllactosamine 67-86 zona pellucida sperm-binding protein 3 Sus scrofa 8-11 9888793-0 1999 Dual affinity labeling of the active site of human lysozyme with an N-acetyllactosamine derivative: first ligand assisted recognition of the second ligand. N-acetyllactosamine 68-87 lysozyme Homo sapiens 51-59 10580653-0 1999 Differences in N-acetyllactosamine synthesis between beta-1,4-galactosyltransferases I and V. N-acetyllactosamine 15-34 beta-1,4-galactosyltransferase 5 Homo sapiens 53-92 9857011-7 1998 In contrast to beta4Gal-TI, the efficiency of beta4Gal-TIV decreased dramatically as the acceptors contained more N-acetyllactosamine repeats, consistent with the fact that core 2 branched O-glycans contain fewer and shorter poly-N-acetyllactosamines than N-glycans in many cells. N-acetyllactosamine 114-133 beta-1,4-galactosyltransferase 5 Homo sapiens 46-58 9760227-2 1998 Here we report the crystal structure of human galectin-7 (hGal-7), in free form and in the presence of galactose, galactosamine, lactose, and N-acetyl-lactosamine at high resolution. N-acetyllactosamine 142-162 galectin 7 Homo sapiens 58-64 10211703-3 1998 Approximately 91% of the radioactivity released from PSGL-1 was recovered in five O-linked glycans: GalNAc (approximately 4% of the total structures), Galp, 3GalNAc (36%), and Galbeta, 3GalNAc substituted with one (45%), two (6%), or three (3%) N-acetyllactosamine repeat units. N-acetyllactosamine 245-264 selectin P ligand Homo sapiens 53-59 10211704-0 1998 Increased elongation of N-acetyllactosamine repeats in doubly glycosylated lysozyme with a particular spacing of the glycosylation sites. N-acetyllactosamine 24-43 lysozyme Homo sapiens 75-83 10211704-2 1998 Glycosylated mutant human lysozyme has been used as a model in studies on the biosynthesis of N-acetyllactosamine repeats in N-linked oligosaccharides. N-acetyllactosamine 94-113 lysozyme Homo sapiens 26-34 9648922-1 1998 UDP-GlcNAc:Galbet1 --> 3GalNAc-R beta1 --> 6N-acetylglucosaminyltransferase (Core2 N-acetyl-glucosaminyltransferase, C2GnT; EC 2.4.1.102) forms beta1 --> 6N-acetyl-glucosaminyl linkages in O-glycoproteins and creates branches for the addition of N-acetyl-lactosamine antennae. N-acetyllactosamine 255-275 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 9 Mus musculus 36-41 9870766-3 1998 We studied developmental aspects of complex carbohydrate expression by white matter glia in the foetal rabbit brain using the tomato lectin Lycopersicon esculentum, which has affinity for components of the extracellular matrix proteins and cell surface proteins (N-acetylglucosamine) and activated lysosomal membrane glycoproteins (N-acetyllactosamine). N-acetyllactosamine 332-351 LTL Solanum lycopersicum 133-139 9751793-1 1998 Previously, treatment of Tamm-Horsfall glycoprotein (THp) from different donors with endo-beta-galactosidase has been shown to liberate a tetra- and a Sd(a)-active pentasaccharide, concluding the presence of N-linked carbohydrate chains containing additional N -acetyllactosamine units. N-acetyllactosamine 259-279 uromodulin Homo sapiens 53-56 9751793-7 1998 The tetraantennary fraction, which accounts for more than 33% of the total carbohydrate moiety of THp, was used to isolate oligosaccharides containing additional N -acetyllactosamine units. N-acetyllactosamine 162-182 uromodulin Homo sapiens 98-101 9648922-1 1998 UDP-GlcNAc:Galbet1 --> 3GalNAc-R beta1 --> 6N-acetylglucosaminyltransferase (Core2 N-acetyl-glucosaminyltransferase, C2GnT; EC 2.4.1.102) forms beta1 --> 6N-acetyl-glucosaminyl linkages in O-glycoproteins and creates branches for the addition of N-acetyl-lactosamine antennae. N-acetyllactosamine 255-275 glucosaminyl (N-acetyl) transferase 1, core 2 Mus musculus 123-128 9648922-1 1998 UDP-GlcNAc:Galbet1 --> 3GalNAc-R beta1 --> 6N-acetylglucosaminyltransferase (Core2 N-acetyl-glucosaminyltransferase, C2GnT; EC 2.4.1.102) forms beta1 --> 6N-acetyl-glucosaminyl linkages in O-glycoproteins and creates branches for the addition of N-acetyl-lactosamine antennae. N-acetyllactosamine 255-275 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 9 Mus musculus 150-155 9637505-10 1998 Removal of polylactosamine chains by endo-beta D-galactosidase digestion significantly reduced the electrophoretic mobility of the immunoreactive bands, suggesting that HLA-G, unlike class Ib molecules studied to date, carries N-acetyllactosamine units. N-acetyllactosamine 227-246 major histocompatibility complex, class I, G Homo sapiens 169-174 9546665-3 1998 Intact ZPB and ZPC cannot be separated from each other unless acidic N-acetyllactosamine regions of their carbohydrate chains are removed by endo-beta-galactosidase digestion. N-acetyllactosamine 69-88 zona pellucida glycoprotein 4 Sus scrofa 7-10 9582341-2 1998 We report here the x-ray crystal structure of the human galectin-3 CRD, in complex with lactose and N-acetyllactosamine, at 2.1-A resolution. N-acetyllactosamine 100-119 galectin 3 Homo sapiens 56-66 9579803-6 1998 The molecular mass of transferrin species V and VI (78,678 and 78,971 Da) suggests that one of their two glycans contains an additional N-acetyllactosamine and a sialylated N-acetyllactosamine units, respectively. N-acetyllactosamine 136-155 transferrin Homo sapiens 22-33 9579803-6 1998 The molecular mass of transferrin species V and VI (78,678 and 78,971 Da) suggests that one of their two glycans contains an additional N-acetyllactosamine and a sialylated N-acetyllactosamine units, respectively. N-acetyllactosamine 173-192 transferrin Homo sapiens 22-33 9461592-4 1998 We find that Fuc-TIV can transfer fucose effectively to all N-acetyllactosamine (LN) units in neutral polylactosamines, and to the "inner" LN units of alpha2,3-sialylated acceptors but is ineffective in transfer to the distal alpha2,3-sialylated LN unit in alpha2,3-sialylated acceptors. N-acetyllactosamine 60-79 fucosyltransferase 4 Homo sapiens 13-20 9268723-4 1997 One enzyme, which utilises N-acetyllactosamine as substrate, has a pH optimum of 7.0, is resistant to heat inactivation, and has been tentatively identified as an alpha1,3-fucosyltransferase. N-acetyllactosamine 27-46 fucosyltransferase 11 Homo sapiens 163-190 9597546-2 1998 We report here that endothelial cells stimulated with lipopolysaccharide or inflammatory cytokines modulate their expression of UPD-Gal: beta-D-Gal alpha 1,3-galactosyltransferase (alpha 1,3GT), the Golgi enzyme that attaches a galactose in alpha 1,3 configuration to an N-acetyllactosamine acceptor. N-acetyllactosamine 271-290 adrenoceptor alpha 1D Homo sapiens 148-155 9597546-2 1998 We report here that endothelial cells stimulated with lipopolysaccharide or inflammatory cytokines modulate their expression of UPD-Gal: beta-D-Gal alpha 1,3-galactosyltransferase (alpha 1,3GT), the Golgi enzyme that attaches a galactose in alpha 1,3 configuration to an N-acetyllactosamine acceptor. N-acetyllactosamine 271-290 adrenoceptor alpha 1D Homo sapiens 181-192 9597546-2 1998 We report here that endothelial cells stimulated with lipopolysaccharide or inflammatory cytokines modulate their expression of UPD-Gal: beta-D-Gal alpha 1,3-galactosyltransferase (alpha 1,3GT), the Golgi enzyme that attaches a galactose in alpha 1,3 configuration to an N-acetyllactosamine acceptor. N-acetyllactosamine 271-290 adrenoceptor alpha 1D Homo sapiens 181-188 9648266-3 1997 The third one, nonasaccharide Neu5Ac(alpha 2-3)Gal(beta 1-4)GlcNAc(beta 1-3)Gal(beta 1-4)[Fuc(alpha 1-3)] GlcNAc(beta 1-3)Gal(beta 1-4)[Fuc(alpha 1-3)]GlcNAc, is a sialylated and internally difucosylated derivative of a trimeric N-acetyllactosamine. N-acetyllactosamine 229-248 tubulin beta 3 class III Homo sapiens 51-59 9648266-3 1997 The third one, nonasaccharide Neu5Ac(alpha 2-3)Gal(beta 1-4)GlcNAc(beta 1-3)Gal(beta 1-4)[Fuc(alpha 1-3)] GlcNAc(beta 1-3)Gal(beta 1-4)[Fuc(alpha 1-3)]GlcNAc, is a sialylated and internally difucosylated derivative of a trimeric N-acetyllactosamine. N-acetyllactosamine 229-248 eukaryotic translation elongation factor 1 beta 2 pseudogene 2 Homo sapiens 67-75 9134435-2 1997 IGnT converts a linear carbohydrate structure, the i antigen, to a branched structure, the I antigen in N-acetyllactosamines. N-acetyllactosamine 104-124 glucosaminyl (N-acetyl) transferase 2, I-branching enzyme Mus musculus 0-4 9188700-3 1997 A prototype of their backbones is represented by the decasaccharide LacNAc beta1-3"(LacNAc beta1-6")LacNAc beta1-3"(LacNAc beta1-6")LacNAc (5), where LacNAc is the disaccharide Gal beta1-4GlcNAc. N-acetyllactosamine 84-90 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 123-130 9188700-3 1997 A prototype of their backbones is represented by the decasaccharide LacNAc beta1-3"(LacNAc beta1-6")LacNAc beta1-3"(LacNAc beta1-6")LacNAc (5), where LacNAc is the disaccharide Gal beta1-4GlcNAc. N-acetyllactosamine 84-90 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 75-82 9188700-3 1997 A prototype of their backbones is represented by the decasaccharide LacNAc beta1-3"(LacNAc beta1-6")LacNAc beta1-3"(LacNAc beta1-6")LacNAc (5), where LacNAc is the disaccharide Gal beta1-4GlcNAc. N-acetyllactosamine 84-90 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 91-98 9188700-3 1997 A prototype of their backbones is represented by the decasaccharide LacNAc beta1-3"(LacNAc beta1-6")LacNAc beta1-3"(LacNAc beta1-6")LacNAc (5), where LacNAc is the disaccharide Gal beta1-4GlcNAc. N-acetyllactosamine 84-90 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 107-114 9188700-3 1997 A prototype of their backbones is represented by the decasaccharide LacNAc beta1-3"(LacNAc beta1-6")LacNAc beta1-3"(LacNAc beta1-6")LacNAc (5), where LacNAc is the disaccharide Gal beta1-4GlcNAc. N-acetyllactosamine 84-90 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 123-130 9188700-3 1997 A prototype of their backbones is represented by the decasaccharide LacNAc beta1-3"(LacNAc beta1-6")LacNAc beta1-3"(LacNAc beta1-6")LacNAc (5), where LacNAc is the disaccharide Gal beta1-4GlcNAc. N-acetyllactosamine 84-90 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 75-82 9188700-3 1997 A prototype of their backbones is represented by the decasaccharide LacNAc beta1-3"(LacNAc beta1-6")LacNAc beta1-3"(LacNAc beta1-6")LacNAc (5), where LacNAc is the disaccharide Gal beta1-4GlcNAc. N-acetyllactosamine 84-90 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 91-98 9188700-3 1997 A prototype of their backbones is represented by the decasaccharide LacNAc beta1-3"(LacNAc beta1-6")LacNAc beta1-3"(LacNAc beta1-6")LacNAc (5), where LacNAc is the disaccharide Gal beta1-4GlcNAc. N-acetyllactosamine 84-90 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 107-114 9188700-3 1997 A prototype of their backbones is represented by the decasaccharide LacNAc beta1-3"(LacNAc beta1-6")LacNAc beta1-3"(LacNAc beta1-6")LacNAc (5), where LacNAc is the disaccharide Gal beta1-4GlcNAc. N-acetyllactosamine 84-90 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 123-130 9191848-0 1997 Specification of receptor-binding phenotypes of influenza virus isolates from different hosts using synthetic sialylglycopolymers: non-egg-adapted human H1 and H3 influenza A and influenza B viruses share a common high binding affinity for 6"-sialyl(N-acetyllactosamine). N-acetyllactosamine 250-269 H1.5 linker histone, cluster member Homo sapiens 153-190 9099986-2 1997 In the course of studying the mechanisms underlying this variability, we have isolated from pig cDNA four sequences corresponding to four isoforms of alpha1,3-galactosyltransferase (alpha1,3GT), the Golgi enzyme that links galactose in alpha1,3 on the galactose residue of N-acetyllactosamine. N-acetyllactosamine 273-292 N-acetyllactosaminide alpha-1,3-galactosyltransferase Sus scrofa 150-180 9099986-2 1997 In the course of studying the mechanisms underlying this variability, we have isolated from pig cDNA four sequences corresponding to four isoforms of alpha1,3-galactosyltransferase (alpha1,3GT), the Golgi enzyme that links galactose in alpha1,3 on the galactose residue of N-acetyllactosamine. N-acetyllactosamine 273-292 N-acetyllactosaminide alpha-1,3-galactosyltransferase Sus scrofa 182-192 9472388-8 1997 The suggestion of a functional relevance for NALA glycosylation of retinal cells is supported by the labelling pattern for HNK-1 in these species, which was different from the pattern found in rod-dominated mammalian retinas. N-acetyllactosamine 45-49 beta-1,3-glucuronyltransferase 1 Homo sapiens 123-128 9256173-1 1997 BACKGROUND: Inactivation of the alpha1,3-galactosyltransferase (GalT) gene by homologous recombination (knockout [KO] mice) and competition for the enzyme"s N-acetyllactosamine substrate by transgenically expressed alpha1,2-fucosyltransferase (H-transferase) are two genetic approaches to elimination of the Gal alpha1,3Gal (alphaGal) epitope, which is the major xenoantigen in pigs against which humans have preformed antibodies. N-acetyllactosamine 157-176 galactose-1-phosphate uridyl transferase Mus musculus 64-68 9188700-3 1997 A prototype of their backbones is represented by the decasaccharide LacNAc beta1-3"(LacNAc beta1-6")LacNAc beta1-3"(LacNAc beta1-6")LacNAc (5), where LacNAc is the disaccharide Gal beta1-4GlcNAc. N-acetyllactosamine 68-74 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 75-82 9188700-3 1997 A prototype of their backbones is represented by the decasaccharide LacNAc beta1-3"(LacNAc beta1-6")LacNAc beta1-3"(LacNAc beta1-6")LacNAc (5), where LacNAc is the disaccharide Gal beta1-4GlcNAc. N-acetyllactosamine 68-74 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 91-98 9188700-3 1997 A prototype of their backbones is represented by the decasaccharide LacNAc beta1-3"(LacNAc beta1-6")LacNAc beta1-3"(LacNAc beta1-6")LacNAc (5), where LacNAc is the disaccharide Gal beta1-4GlcNAc. N-acetyllactosamine 68-74 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 107-114 9188700-3 1997 A prototype of their backbones is represented by the decasaccharide LacNAc beta1-3"(LacNAc beta1-6")LacNAc beta1-3"(LacNAc beta1-6")LacNAc (5), where LacNAc is the disaccharide Gal beta1-4GlcNAc. N-acetyllactosamine 68-74 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 123-130 9188700-3 1997 A prototype of their backbones is represented by the decasaccharide LacNAc beta1-3"(LacNAc beta1-6")LacNAc beta1-3"(LacNAc beta1-6")LacNAc (5), where LacNAc is the disaccharide Gal beta1-4GlcNAc. N-acetyllactosamine 84-90 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 75-82 9188700-3 1997 A prototype of their backbones is represented by the decasaccharide LacNAc beta1-3"(LacNAc beta1-6")LacNAc beta1-3"(LacNAc beta1-6")LacNAc (5), where LacNAc is the disaccharide Gal beta1-4GlcNAc. N-acetyllactosamine 84-90 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 91-98 9188700-3 1997 A prototype of their backbones is represented by the decasaccharide LacNAc beta1-3"(LacNAc beta1-6")LacNAc beta1-3"(LacNAc beta1-6")LacNAc (5), where LacNAc is the disaccharide Gal beta1-4GlcNAc. N-acetyllactosamine 84-90 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 107-114 9188700-3 1997 A prototype of their backbones is represented by the decasaccharide LacNAc beta1-3"(LacNAc beta1-6")LacNAc beta1-3"(LacNAc beta1-6")LacNAc (5), where LacNAc is the disaccharide Gal beta1-4GlcNAc. N-acetyllactosamine 84-90 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 123-130 9188700-3 1997 A prototype of their backbones is represented by the decasaccharide LacNAc beta1-3"(LacNAc beta1-6")LacNAc beta1-3"(LacNAc beta1-6")LacNAc (5), where LacNAc is the disaccharide Gal beta1-4GlcNAc. N-acetyllactosamine 84-90 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 75-82 9188700-3 1997 A prototype of their backbones is represented by the decasaccharide LacNAc beta1-3"(LacNAc beta1-6")LacNAc beta1-3"(LacNAc beta1-6")LacNAc (5), where LacNAc is the disaccharide Gal beta1-4GlcNAc. N-acetyllactosamine 84-90 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 91-98 9188700-3 1997 A prototype of their backbones is represented by the decasaccharide LacNAc beta1-3"(LacNAc beta1-6")LacNAc beta1-3"(LacNAc beta1-6")LacNAc (5), where LacNAc is the disaccharide Gal beta1-4GlcNAc. N-acetyllactosamine 84-90 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 107-114 9188700-3 1997 A prototype of their backbones is represented by the decasaccharide LacNAc beta1-3"(LacNAc beta1-6")LacNAc beta1-3"(LacNAc beta1-6")LacNAc (5), where LacNAc is the disaccharide Gal beta1-4GlcNAc. N-acetyllactosamine 84-90 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 123-130 9188700-3 1997 A prototype of their backbones is represented by the decasaccharide LacNAc beta1-3"(LacNAc beta1-6")LacNAc beta1-3"(LacNAc beta1-6")LacNAc (5), where LacNAc is the disaccharide Gal beta1-4GlcNAc. N-acetyllactosamine 84-90 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 75-82 9188700-3 1997 A prototype of their backbones is represented by the decasaccharide LacNAc beta1-3"(LacNAc beta1-6")LacNAc beta1-3"(LacNAc beta1-6")LacNAc (5), where LacNAc is the disaccharide Gal beta1-4GlcNAc. N-acetyllactosamine 84-90 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 91-98 9188700-3 1997 A prototype of their backbones is represented by the decasaccharide LacNAc beta1-3"(LacNAc beta1-6")LacNAc beta1-3"(LacNAc beta1-6")LacNAc (5), where LacNAc is the disaccharide Gal beta1-4GlcNAc. N-acetyllactosamine 84-90 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 107-114 9201300-6 1997 IL-8 mRNA expressed by HT-29 cells in response to E. histolytica trophozoites was downregulated in the presence of galactose, N-acetylgalactosamine or N-acetyl-lactosamine (0.1-100 mM), and this was paralleled by decreased IL-8 protein secretion. N-acetyllactosamine 151-171 C-X-C motif chemokine ligand 8 Homo sapiens 0-4 9201300-6 1997 IL-8 mRNA expressed by HT-29 cells in response to E. histolytica trophozoites was downregulated in the presence of galactose, N-acetylgalactosamine or N-acetyl-lactosamine (0.1-100 mM), and this was paralleled by decreased IL-8 protein secretion. N-acetyllactosamine 151-171 C-X-C motif chemokine ligand 8 Homo sapiens 223-227 8593630-0 1995 Site-directed enzymatic alpha-(1-->3)-L-fucosylation of the tetrasaccharide Gal beta(1-->4)GlcNAc beta(1-->3)Gal beta(1-->4)GlcNAc at the distal N-acetyllactosamine unit. N-acetyllactosamine 157-176 galanin and GMAP prepropeptide Homo sapiens 79-82 9007276-5 1996 By molecular modeling of this tetrasaccharide in the known binding site of LT, the saccharide-peptide interaction was shown to be limited to the terminal disaccharide (N-acetyllactosamine). N-acetyllactosamine 168-187 Leucine transport, high Homo sapiens 75-77 8885835-4 1996 On the other hand, the hydrogen-bonding pattern and the stacking interaction at subsite B were remarkably different between the HL/NAG-NAG-EPO complex and human lysozyme labeled by the 2",3"-epoxypropyl beta-glycoside of N-acetyllactosamine (HL/GAL-NAG-EPO complex). N-acetyllactosamine 221-240 NBAS subunit of NRZ tethering complex Homo sapiens 131-134 8885835-5 1996 The reduced number of possible hydrogen bonds as well as the less favorable stacking between the side chain of Tyr63 in human lysozyme and the galactose residue in the HL/GAL-NAG-EPO complex reasonably explained the less efficient ability of the 2",3"-epoxypropyl beta-glycoside of N-acetyllactosamine as compared to that of N,N"-diacetylchitobiose as an affinity labeling reagent toward human lysozyme. N-acetyllactosamine 282-301 lysozyme Homo sapiens 126-134 8885835-5 1996 The reduced number of possible hydrogen bonds as well as the less favorable stacking between the side chain of Tyr63 in human lysozyme and the galactose residue in the HL/GAL-NAG-EPO complex reasonably explained the less efficient ability of the 2",3"-epoxypropyl beta-glycoside of N-acetyllactosamine as compared to that of N,N"-diacetylchitobiose as an affinity labeling reagent toward human lysozyme. N-acetyllactosamine 282-301 NBAS subunit of NRZ tethering complex Homo sapiens 175-178 8855944-8 1996 In equilibrium dialysis, N-Gal-1 and V5D-Gal-1 bind N-acetyllactosamine with a Kd approximately 90 microM, which is similar to that of native lectin. N-acetyllactosamine 52-71 galectin 1 Homo sapiens 27-32 8855944-8 1996 In equilibrium dialysis, N-Gal-1 and V5D-Gal-1 bind N-acetyllactosamine with a Kd approximately 90 microM, which is similar to that of native lectin. N-acetyllactosamine 52-71 galectin 1 Homo sapiens 41-46 8647179-6 1996 The N-linked carbohydrates are of the branched, complex type, containing repeating N-acetylglycosamine or N-acetyllactosamine units which mediate the reactivity of the F4/80 molecule with Datura stramonium lectin. N-acetyllactosamine 106-125 adhesion G protein-coupled receptor E1 Mus musculus 168-173 9020882-1 1997 UDP-GlcNAc: alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I (EC 2.4.1.101; GlcNAc-T I) is a medial-Golgi enzyme which catalyses the first step in the conversion of oligomannose-type to N-acetyl-lactosamine- and hybrid-type N-glycans and is essential for normal embryogenesis in the mouse. N-acetyllactosamine 200-220 mannoside acetylglucosaminyltransferase 1 Mus musculus 90-100 8955156-6 1996 Unlike the X. laevis galectin, the binding activity of the B. arenarum galectin for N-acetyllactosamine, the human blood group A tetrasaccharide and Galbeta1,3GalNAc relative to lactose, was in agreement with that observed for the galectin-1 subgroup and those galectins having "conserved" (type I) CRDs (Ahmed, H., and Vasta, G. R. (1994) Glycobiology 4, 545-549). N-acetyllactosamine 84-103 galectin 1 Homo sapiens 231-241 9022688-6 1996 The follitropin beta chain showed the presence of N-acetyllactosamine repeats on the antennae. N-acetyllactosamine 50-69 follicle stimulating hormone subunit beta Homo sapiens 4-26 8952472-6 1996 Gal-1 and the plant lectins possess essentially the same affinities for N-acetyllactosamine; however, the animal lectin shows a lower -delta H value and more favorable binding entropy for the disaccharide. N-acetyllactosamine 72-91 galectin-1 Cricetulus griseus 0-5 8952472-7 1996 While Gal-1, C2S-Gal-1, and N-Gal-1 all possess essentially the same affinities for N-acetyllactosamine, the two mutants possess much lower -delta H values, even though the mutation site(s) are far removed from the carbohydrate binding site. N-acetyllactosamine 84-103 galectin-1 Cricetulus griseus 6-11 8619828-1 1996 The synthesis of N-acetyllactosamine (D-Galp beta 1-4D-GlcpNAc) with very low contamination of its isomer N-acetyllactosamine (D-Galp beta 1-6D-GlcpNAc) was obtained by use of regioselective transglycosylation activity of beta-galactosidase from Bacillus circulans using lactose as the donor of D-Galp and D-GlcpNAc as the acceptor. N-acetyllactosamine 17-36 galanin like peptide Homo sapiens 40-44 8619828-1 1996 The synthesis of N-acetyllactosamine (D-Galp beta 1-4D-GlcpNAc) with very low contamination of its isomer N-acetyllactosamine (D-Galp beta 1-6D-GlcpNAc) was obtained by use of regioselective transglycosylation activity of beta-galactosidase from Bacillus circulans using lactose as the donor of D-Galp and D-GlcpNAc as the acceptor. N-acetyllactosamine 17-36 galanin like peptide Homo sapiens 129-133 8619828-1 1996 The synthesis of N-acetyllactosamine (D-Galp beta 1-4D-GlcpNAc) with very low contamination of its isomer N-acetyllactosamine (D-Galp beta 1-6D-GlcpNAc) was obtained by use of regioselective transglycosylation activity of beta-galactosidase from Bacillus circulans using lactose as the donor of D-Galp and D-GlcpNAc as the acceptor. N-acetyllactosamine 17-36 galanin like peptide Homo sapiens 129-133 8619828-1 1996 The synthesis of N-acetyllactosamine (D-Galp beta 1-4D-GlcpNAc) with very low contamination of its isomer N-acetyllactosamine (D-Galp beta 1-6D-GlcpNAc) was obtained by use of regioselective transglycosylation activity of beta-galactosidase from Bacillus circulans using lactose as the donor of D-Galp and D-GlcpNAc as the acceptor. N-acetyllactosamine 106-125 galanin like peptide Homo sapiens 129-133 8619828-1 1996 The synthesis of N-acetyllactosamine (D-Galp beta 1-4D-GlcpNAc) with very low contamination of its isomer N-acetyllactosamine (D-Galp beta 1-6D-GlcpNAc) was obtained by use of regioselective transglycosylation activity of beta-galactosidase from Bacillus circulans using lactose as the donor of D-Galp and D-GlcpNAc as the acceptor. N-acetyllactosamine 106-125 galanin like peptide Homo sapiens 129-133 8547257-11 1996 Thus, the E-selectin binding epitope in HL60 cells is carried by unbranched terminally alpha 2-->3 sialylated polylactosamine having at least 10 monosaccharide units (4 N-acetyllactosamine units) with internal multiple fucosylation at GlcNAc. N-acetyllactosamine 172-191 selectin E Homo sapiens 10-20 8536711-6 1995 We report here enzymic synthesis of a large oligosaccharide fulfilling several of the features characteristic to the L-selectin ligands: it is a dodecameric O-glycosidic core-2-type oligosaccharide alditol with a branched polylactosamine backbone carrying two distal alpha-2,3"-sialylated and alpha-1,3-fucosylated N-acetyl-lactosamine groups (sialyl Lewis x, sialyl Le(x)). N-acetyllactosamine 315-335 selectin L Rattus norvegicus 117-127 8770386-2 1995 Treatment of delipidated hen egg yolk with the protease Orientase and neuraminidase gave a dimeric N-acetyllactosamine-containing oligosaccharide linked to asparagine. N-acetyllactosamine 99-118 neuraminidase 1 Homo sapiens 70-83 8719880-5 1995 Further investigations using glycosidases, glycosylation inhibitors and lectin-affinity chromatography demonstrated that the tumor-associated glycosylation change in GLUT1 was mainly due to the increase in N-acetyl-lactosamine repeats in the N-linked oligosaccharides. N-acetyllactosamine 206-226 solute carrier family 2 member 1 Homo sapiens 166-171 7592613-6 1995 It is possible that the oligosaccharides bearing sialylated lacNAc or lacdiNAc antennae may manifest immunosuppressive effects by specifically blocking adhesive and activation-related events mediated by CD22, the human B cell associated receptor. N-acetyllactosamine 60-66 CD22 molecule Homo sapiens 203-207 7499214-0 1995 Characterization of a sulfotransferase from human airways responsible for the 3-O-sulfation of terminal galactose in N-acetyllactosamine-containing mucin carbohydrate chains. N-acetyllactosamine 117-136 LOC100508689 Homo sapiens 148-153 7664637-1 1995 Lack of completion of N-acetyllactosamine-type glycosylation on thyroglobulin (Tg) has been implicitly considered as an etiological factor of some thyroid disorders, i.e. goiter and hypothyroidism. N-acetyllactosamine 22-41 thyroglobulin Rattus norvegicus 64-77 7496141-5 1995 A galactose-terminated triantennary N-glycoside, having one N-acetyl-lactosamine unit on the 6 branch and two N-acetyl-lactosamine units on the 3 branch of the trimannosyl core structure, showed affinity enhancement of approximately 10(5) over a monovalent ligand for HHL, while the same glycopeptide showed enhancement of about 2000-fold for rM-ASGP-BP. N-acetyllactosamine 60-80 C-type lectin domain containing 10A Rattus norvegicus 343-353 7541354-6 1995 The major oligosaccharides of human vitronectin were of the diantennary N-acetyllactosamine type, with a lesser amount of the tri- and a small amount of the mono-antennary type, to which 1-3 mol sialic acid residues were linked, mostly through alpha 2-6 linkages, although alpha 2-3 linkages were also present. N-acetyllactosamine 72-91 vitronectin Homo sapiens 36-47 7607222-9 1995 Elongation was found to proceed from a common tetrasaccharidic core: Gal(beta 1-4)GlcNAc(beta 1-6)[Gal(beta 1-3)]GalNAc-ol through N-acetyllactosamine units. N-acetyllactosamine 131-150 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 73-81 7607222-9 1995 Elongation was found to proceed from a common tetrasaccharidic core: Gal(beta 1-4)GlcNAc(beta 1-6)[Gal(beta 1-3)]GalNAc-ol through N-acetyllactosamine units. N-acetyllactosamine 131-150 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 89-97 7607222-9 1995 Elongation was found to proceed from a common tetrasaccharidic core: Gal(beta 1-4)GlcNAc(beta 1-6)[Gal(beta 1-3)]GalNAc-ol through N-acetyllactosamine units. N-acetyllactosamine 131-150 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 103-111 7496141-5 1995 A galactose-terminated triantennary N-glycoside, having one N-acetyl-lactosamine unit on the 6 branch and two N-acetyl-lactosamine units on the 3 branch of the trimannosyl core structure, showed affinity enhancement of approximately 10(5) over a monovalent ligand for HHL, while the same glycopeptide showed enhancement of about 2000-fold for rM-ASGP-BP. N-acetyllactosamine 110-130 C-type lectin domain containing 10A Rattus norvegicus 343-353 7528213-3 1994 Fuc-TIII transfers a fucose to both sialylated and nonsialylated N-acetyllactosamine, but Fuc-TIV apparently transfers a fucose only to neutral N-acetyllactosamine. N-acetyllactosamine 65-84 fucosyltransferase 3 (Lewis blood group) Homo sapiens 0-8 7737204-9 1995 Tetraantennary oligosaccharides with N-acetyllactosamine repeats could be digested quantitatively with endo-beta-galactosidase from Bacteroides fragilis, whereas under the same conditions tri" antennary oligosaccharides hardly reacted (< 15%). N-acetyllactosamine 37-56 galactosidase beta 1 Homo sapiens 108-126 7867650-3 1995 hCG derivatives were obtained by enzymic removal of the alpha 3-linked sialic acid residues followed by alpha 6-sialylation, alpha 3-galactosylation or alpha 3-fucosylation of uncovered Gal beta 1-->4GlcNAc (LacNAc) termini, or alpha 3-sialylation of Gal beta 1-->3GalNAc sequences. N-acetyllactosamine 211-217 chorionic gonadotropin subunit beta 5 Homo sapiens 0-3 7713918-6 1995 Recombinant forms of both FucT-III and FucT-V were irreversibly inactivated by N-ethylmaleimide and could be effectively protected from inactivation by GDP-fucose and GDP but not by UDP-galactose, fucose, or N-acetyllactosamine. N-acetyllactosamine 208-227 fucosyltransferase 3 (Lewis blood group) Homo sapiens 26-34 7713918-6 1995 Recombinant forms of both FucT-III and FucT-V were irreversibly inactivated by N-ethylmaleimide and could be effectively protected from inactivation by GDP-fucose and GDP but not by UDP-galactose, fucose, or N-acetyllactosamine. N-acetyllactosamine 208-227 fucosyltransferase 5 Homo sapiens 39-45 7881179-8 1994 By contrast, the enzymatic properties of the schistosome beta 4-GalNAcT (except for the sugar-donor specificity) strongly resemble those of the beta 4-galactosyltransferase of higher animals, an enzyme which is known to control the synthesis of Gal1-->4GlcNAc (lacNAc)-type oligosaccharide chains. N-acetyllactosamine 264-270 chondroitin sulfate N-acetylgalactosaminyltransferase 2 Homo sapiens 57-71 7773775-3 1994 The high resolution X-ray crystallographic analyses of three crystal forms of bovine galectin-1 in complex with biantennary saccharides of N-acetyllactosamine type reveal infinite chains of lectin dimers cross-linked through N-acetyllactosamine units located at the end of the oligosaccharide antenna. N-acetyllactosamine 139-158 galectin 1 Bos taurus 85-95 7773775-3 1994 The high resolution X-ray crystallographic analyses of three crystal forms of bovine galectin-1 in complex with biantennary saccharides of N-acetyllactosamine type reveal infinite chains of lectin dimers cross-linked through N-acetyllactosamine units located at the end of the oligosaccharide antenna. N-acetyllactosamine 225-244 galectin 1 Bos taurus 85-95 8179322-6 1994 The structures are as follows: [formula: see text] Gangliosides such as G-1, G-2, and G-3, with branched oligosaccharide chains comprising a number of N-acetyllactosamine (Gal-GlcNAc) moieties, are abundant in erythrocytes from various mammalian species. N-acetyllactosamine 151-170 proline rich protein BstNI subfamily 3 Homo sapiens 72-89 8039189-1 1994 N-Acetyl-lactosamine(beta-D-Gal p-(1-->4)-D-Glc pNAc) was synthesized regioselectively with the aid of the transglycosylation activity of beta-galactosidase isolated from Diplococcus pneumoniae using p-nitrophenyl beta-D-galactopyranoside as the donor. N-acetyllactosamine 0-20 galactosidase beta 1 Homo sapiens 141-159 1328669-5 1992 The broad size distribution of GL results from heterogeneous N-acetyllactosamine addition since it is susceptible to digestion by endo-beta-galactosidase. N-acetyllactosamine 61-80 galactosidase beta 1 Homo sapiens 135-153 7948482-5 1994 When exhaustively digested with endo-beta-galactosidase, an enzyme known to cleave repeating units of acetyllactosamine (3Gal beta 1, 4GlcNAc beta 1), mZP2 and mZP3 showed an apparent reduction in size by 23 kDa and 16 kDa, respectively. N-acetyllactosamine 102-119 galactosidase, beta 1 Mus musculus 37-55 7948482-5 1994 When exhaustively digested with endo-beta-galactosidase, an enzyme known to cleave repeating units of acetyllactosamine (3Gal beta 1, 4GlcNAc beta 1), mZP2 and mZP3 showed an apparent reduction in size by 23 kDa and 16 kDa, respectively. N-acetyllactosamine 102-119 zona pellucida glycoprotein 3 Mus musculus 160-164 8323955-5 1993 When incubated in optimized conditions with type 1, 2 or 6 oligosaccharide acceptors (10 mM), hepatocellular alpha 1-3 FT efficiently transferred fucose to N-acetyllactosamine and its 3" sialylated derivative, but poorly to lactose. N-acetyllactosamine 156-175 adrenoceptor alpha 1D Homo sapiens 109-116 1400309-4 1992 The product from LGBn was isolated in microgram quantities and identified by fast atom bombardment mass spectrometry as LacNAc beta 1,6(Gal beta 1,3)GalNAc alpha-O-Bn. N-acetyllactosamine 120-126 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 127-133 1400309-4 1992 The product from LGBn was isolated in microgram quantities and identified by fast atom bombardment mass spectrometry as LacNAc beta 1,6(Gal beta 1,3)GalNAc alpha-O-Bn. N-acetyllactosamine 120-126 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 140-148 1663364-8 1991 The binding of SSA-M to sialidase-treated porcine mucin was inhibited strongly by GalNAc and disaccharides containing galactose (lactose, melibiose, and N-acetyllactosamine) but not by free galactose (Gal), suggesting that the glycan for optimum binding is Gal beta(1-3)GalNAc. N-acetyllactosamine 153-172 LOC100508689 Homo sapiens 50-55 1404396-1 1992 Isolectin II (LOL II) isolated from the seeds of Lathyrus ochrus has been crystallized in the presence of the N2 fragment (18,500 Da) isolated from human lactotransferrin, which contains an N-acetyllactosamine type biantennary glycan linked to Asn137. N-acetyllactosamine 190-209 lactotransferrin Homo sapiens 154-170 1429877-6 1992 The sensitivity of the high-M(r) oligosaccharides to endo-beta-galactosidase and their incorporation of [3H]glucosamine suggest that they could contain repeating N-acetyllactosamine units. N-acetyllactosamine 162-181 galactosidase beta 1 Homo sapiens 58-76 1386213-6 1992 HLBP14 was eluted from a murine laminin column by lactose, N-acetyllactosamine, and galactose but not by other control saccharides, including glucose, fucose, mannose, and melibiose. N-acetyllactosamine 59-78 galectin 1 Homo sapiens 0-6 1576211-0 1992 Molecular dynamics simulations of a monofucosylated biantennary glycan of the N-acetyllactosamine type: the human lactotransferrin glycan. N-acetyllactosamine 78-97 lactotransferrin Homo sapiens 114-130 1429720-5 1992 When ovarian cancer serum was the enzyme source, either the sulfate group or a sialyl moiety at C-3" of LacNAc enhanced the acceptor ability (341 and 242%, respectively), whereas the sulfate group at C-2" or C-6" reduced the activity (22-36%); sulfate at C-6 or fucose at C-2" increased the activity (172 and 253%). N-acetyllactosamine 104-110 complement C6 Homo sapiens 208-211 1429720-5 1992 When ovarian cancer serum was the enzyme source, either the sulfate group or a sialyl moiety at C-3" of LacNAc enhanced the acceptor ability (341 and 242%, respectively), whereas the sulfate group at C-2" or C-6" reduced the activity (22-36%); sulfate at C-6 or fucose at C-2" increased the activity (172 and 253%). N-acetyllactosamine 104-110 complement C6 Homo sapiens 255-258 1429720-10 1992 Thus, the ovarian cancer serum alpha 1,3-fucosyltransferase acts equally well on H-type 2,3"-sialyl LacNAc and 3"-sulfo LacNAc, but not on H-type 1. N-acetyllactosamine 100-106 fucosyltransferase 11 Homo sapiens 31-59 1601853-8 1992 261, 5625-5630), and this is the first description of the occurrence of the ganglioside with the branched structure with two N-acetyllactosamines linked to lactosylceramide via beta 1-6 and beta 1-3 in human linked to lactosylceramide via beta 1-6 and beta 1-3 in human tissues. N-acetyllactosamine 125-145 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 177-185 1824844-5 1991 The action of core 2 GlcNAc-transferase followed by beta 1-4Gal-transferase provides an N-acetyllactosamine antenna that can be extended with polylactosamine (i.e. repeating Gal beta 1-4GlcNAc beta 1-3) provided UDP-GlcNAc:Gal beta-R beta 1-3GlcNAc-transferase (GlcNAc-transferase) (i)) activity is present. N-acetyllactosamine 88-107 glucosaminyl (N-acetyl) transferase 1, core 2 Mus musculus 14-39 1856221-10 1991 This size variability of glycosylated lysozyme from CHO cells may be explained by the presence of biantennary and triantennary endo-beta-N-acetylglucosaminidase H-resistant oligosaccharides with N-acetyllactosamine repeats of variable length and by the presence of hybrid oligosaccharides, as suggested by affinity to several lectins and sensitivity to endo-beta-galactosidase. N-acetyllactosamine 195-214 lysozyme C Cricetulus griseus 38-46 2043765-2 1991 EPO is heavily glycosylated with three asparagine (N)-linked tetraantennary oligosaccharides that may contain N-acetyl-lactosamine repeats and a single serine (O)-linked oligosaccharide. N-acetyllactosamine 110-130 erythropoietin Cricetulus griseus 0-3 1705026-7 1991 Monosaccharide composition, linkage analysis, and fast atom bombardment mass spectrometry of the glycolipids indicate that the ligands for ELAM-1 are terminally sialylated lactosylceramides with a variable number of N-acetyllactosamine repeats and at least one fucosylated N-acetylglucosamine residue. N-acetyllactosamine 216-235 selectin E Homo sapiens 139-145 2116309-8 1990 The recombinant alpha 1----3-galactosyltransferase showed the expected preference for the acceptor substrate N-acetyllactosamine (Gal beta 1----4GlcNAc), and demonstrated enzyme kinetics identical to those previously reported for affinity-purified calf thymus alpha 1----3-galactosyltransferase [Blanken, W. M. & Van den Eijnden, D. H. (1985) J. Biol. N-acetyllactosamine 109-128 N-acetyllactosaminide alpha-1,3-galactosyltransferase Bos taurus 16-50 2249984-8 1990 The purified r epsilon BP exhibits binding activity to various saccharides, with affinity for N-acetyllactosamine greater than thiodigalactoside greater than lactose much greater than D-galactose greater than L-arabinose, an order identical to that exhibited by native epsilon BP isolated from RBL cells. N-acetyllactosamine 94-113 galectin 3 Rattus norvegicus 15-25 2124546-2 1990 Structural analysis by 500 MHz1H-NMR spectroscopy, of the enzymatically released N-linked carbohydrate chains of chimeric plasminogen activator and of erythropoietin, showed that alpha 2-3 linked N-glycolylneuraminic acid can occur in different N-acetyllactosamine type antennary structures. N-acetyllactosamine 245-264 erythropoietin Homo sapiens 151-165 2116309-8 1990 The recombinant alpha 1----3-galactosyltransferase showed the expected preference for the acceptor substrate N-acetyllactosamine (Gal beta 1----4GlcNAc), and demonstrated enzyme kinetics identical to those previously reported for affinity-purified calf thymus alpha 1----3-galactosyltransferase [Blanken, W. M. & Van den Eijnden, D. H. (1985) J. Biol. N-acetyllactosamine 109-128 N-acetyllactosaminide alpha-1,3-galactosyltransferase Bos taurus 260-294 2335508-9 1990 Although the galaptin did not appear to recognize N-acetylglucosamine as a monosaccharide, the presence of this sugar penultimate to galactose increased the binding affinity by as much as 500-fold, as was the case for N-acetyllactosamine. N-acetyllactosamine 218-237 galectin 1 Homo sapiens 13-21 2395332-8 1990 Digestion of the glycopeptides with endo-beta-galactosidase, which specifically cleaves polylactosaminoglycans, showed the presence of material containing N-acetyllactosamine repeating units in Gaucher liver glycopeptide fractions, but not in control and Niemann-Pick type C derived glycopeptide fractions. N-acetyllactosamine 155-174 galactosidase beta 1 Homo sapiens 41-59 2395332-8 1990 Digestion of the glycopeptides with endo-beta-galactosidase, which specifically cleaves polylactosaminoglycans, showed the presence of material containing N-acetyllactosamine repeating units in Gaucher liver glycopeptide fractions, but not in control and Niemann-Pick type C derived glycopeptide fractions. N-acetyllactosamine 155-174 protein interacting with PRKCA 1 Homo sapiens 263-267 2180441-7 1990 The fucosylated and sialylated derivate of N-acetyllactosamine, sialylated Lex, had the same distribution as N-acetyllactosamine and T structures. N-acetyllactosamine 43-62 fucosyltransferase 4 Homo sapiens 75-78 2180441-7 1990 The fucosylated and sialylated derivate of N-acetyllactosamine, sialylated Lex, had the same distribution as N-acetyllactosamine and T structures. N-acetyllactosamine 109-128 fucosyltransferase 4 Homo sapiens 75-78 34073528-3 2021 The galectin-3 protein is also highly expressed in tumor cells and N-acetyllactosamine is a well-established ligand of this receptor. N-acetyllactosamine 67-86 galectin 3 Homo sapiens 4-14 34619151-4 2021 To this end, we employed extensive Molecular Dynamics simulations to unravel the complete binding event of human galectin-3 with its native natural ligand N-acetyllactosamine (LacNAc) at atomic precision. N-acetyllactosamine 155-174 galectin 3 Homo sapiens 113-123 34146732-7 2021 These two residues, Gly54 and Arg74 in galectin-1, would cooperatively contribute to the N-acetyllactosamine recognition. N-acetyllactosamine 89-108 lectin, galactoside-binding, soluble, 1, gene 1 L homeolog Xenopus laevis 39-49 34293617-2 2021 Galectin-1 (Gal-1), a prototype member of this family, presents a carbohydrate recognition domain (CRD) with specific affinity for beta-galactosides such as N-acetyllactosamine (beta-d-Galp-(1 4)-d-GlcpNAc), and mediate numerous physiological and pathological processes. N-acetyllactosamine 157-176 galectin 1 Homo sapiens 0-10 34293617-2 2021 Galectin-1 (Gal-1), a prototype member of this family, presents a carbohydrate recognition domain (CRD) with specific affinity for beta-galactosides such as N-acetyllactosamine (beta-d-Galp-(1 4)-d-GlcpNAc), and mediate numerous physiological and pathological processes. N-acetyllactosamine 157-176 galectin 1 Homo sapiens 12-17 35513489-4 2022 This fold with a beta-sheet clasping an alpha-helix represents a new fold for glycan recognition based on glycan array screening, which shows that VP8*B recognizes glycans containing N-acetyllactosamine moiety. N-acetyllactosamine 183-202 amyloid beta precursor protein Homo sapiens 15-21 3182859-3 1988 More than 80% of the sugar chains of natural interferon-beta 1 occur as biantennary complex-type sugar chains, approximately 10% of which contain N-acetyllactosamine repeating structure in their outer chain moieties. N-acetyllactosamine 146-165 interferon beta 1 Homo sapiens 45-62 35191576-1 2022 The interaction of the SARS CoV2 spike glycoprotein with two sialic acid-containing trisaccharides (a2,3 and a2,6 sialyl N-Acetyllactosamine) has been demonstrated by NMR. N-acetyllactosamine 121-140 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 33-38 2688463-2 1989 Since only the alpha 2,6-sialyltransferase is involved in the in vivo sialylation of transferrin, Gal beta 1,4GlcNAc was chosen as an acceptor and alpha 2,6-sialyl-N-acetyllactosamine was separated from the corresponding alpha 2,3-sialyl isomer present in the sialyltransferase reaction mixture by high-performance liquid chromatography. N-acetyllactosamine 163-183 transferrin Rattus norvegicus 85-96 2910371-6 1989 Erythropoietin also contains N-glycans with a few N-acetyllactosamine repeats, which can be enriched by tomato lectin affinity chromatography. N-acetyllactosamine 50-69 erythropoietin Homo sapiens 0-14 2910371-6 1989 Erythropoietin also contains N-glycans with a few N-acetyllactosamine repeats, which can be enriched by tomato lectin affinity chromatography. N-acetyllactosamine 50-69 LTL Solanum lycopersicum 111-117 3196789-6 1988 The susceptibility of HMWG to endo-beta-galactosidase suggests that at least some of these oligomers are substituted with galactose to form N-acetyllactosamine. N-acetyllactosamine 140-159 galactosidase beta 1 Bos taurus 35-53 3789744-0 1986 Evidence for the presence of an N-acetyllactosamine-type chain in epiglycanin. N-acetyllactosamine 32-51 mucin 21 Mus musculus 66-77 2458292-9 1988 The binding of the antibody to OTF9-63 cells was inhibited to 50% by 10-50 microM N-acetyllactosamine and lactose. N-acetyllactosamine 82-101 POU domain, class 3, transcription factor 4 Mus musculus 31-35 3285099-8 1988 Pretreatment of tissue sections with neuraminidase proved that Le(x) and N-acetyllactosamine could be partly substituted by sialic acid A type 3 chain and most of N-acetyllactosamine antigens were present only in cytoplasm, whereas all other examined antigens could be present both in cytoplasm and on cell membranes. N-acetyllactosamine 73-92 neuraminidase 1 Homo sapiens 37-50 3285099-8 1988 Pretreatment of tissue sections with neuraminidase proved that Le(x) and N-acetyllactosamine could be partly substituted by sialic acid A type 3 chain and most of N-acetyllactosamine antigens were present only in cytoplasm, whereas all other examined antigens could be present both in cytoplasm and on cell membranes. N-acetyllactosamine 163-182 neuraminidase 1 Homo sapiens 37-50 2965731-5 1988 These effectors were blocked in their ability to bind to YAC-1 targets by the addition of N-acetyllactosamine [Gal(beta 1,4)-GlcNAc] and chitobiose [GlcNAc(beta 1,4)GlcNAc], but not by saccharides lacking lactosamine-type linkages. N-acetyllactosamine 90-109 ADP-ribosyltransferase 1 Mus musculus 57-62 3208286-1 1988 A lectin activity inhibitable by thiodigalactose, N-acetyllactosamine, lactulose, lactose and by an antibody raised against CLL I (chicken-lactose lectin I) has been investigated in the chick embryo developing kidney. N-acetyllactosamine 50-69 galectin 3 Gallus gallus 2-8 3128279-1 1988 of oligosaccharides of N-acetyl-lactosamine-type released from human erythrocyte glycopeptides by endo-beta-galactosidase. N-acetyllactosamine 23-43 galactosidase beta 1 Homo sapiens 103-121 3128279-3 1988 spectroscopy has been used in structural studies of three linear and five branched oligosaccharides of N-acetyl-lactosamine-type that were released from desialylated blood group O erythrocyte glycopeptides by treatment with the endo-beta-galactosidase of Bacteroides fragilis followed by reduction. N-acetyllactosamine 103-123 galactosidase beta 1 Homo sapiens 233-251 3768898-3 1986 Substitution of the N-acetyllactosamine sequences by sialic acid residues, either at O-3 or O-6 of galactose completely abolishes the affinity of the lectins for the saccharides. N-acetyllactosamine 20-39 immunoglobulin kappa variable 2D-38 (pseudogene) Homo sapiens 85-95 2870429-3 1986 The research reported here suggests that the basis of the large Mr heterogeneity in Thy-1 of immature T-cells is the presence of repeating N-acetyllactosamine (R"Gal beta 1,4GlcNAc beta 1,3R") units in the oligosaccharide portion of the molecule. N-acetyllactosamine 139-158 thymus cell antigen 1, theta Mus musculus 84-89 3522754-7 1986 After this period N-acetyllactosamine could only be demonstrated on basal cells after treatment with neuraminidase, indicating a masking of N-acetyllactosamine by sialic acid. N-acetyllactosamine 18-37 neuraminidase 1 Homo sapiens 101-114 3522754-13 1986 Our study demonstrates that N-acetyllactosamine is maximally expressed at the early stages of development, but may later be modified either by sialylation or fucosylation into blood group H or Lex, or by Ley substances, respectively. N-acetyllactosamine 28-47 fucosyltransferase 4 Homo sapiens 193-196 2947572-6 1986 The spectra are consistent with an N-acetyl-lactosamine repeating unit that is predominantly sulphated at C-6 of both galactose and N-acetylglucosamine. N-acetyllactosamine 35-55 complement C6 Homo sapiens 106-109 3088498-5 1986 Treatment with endo-beta-galactosidase showed that the stored material contained N-acetyllactosamine repeating units. N-acetyllactosamine 81-100 galactosidase beta 1 Homo sapiens 20-38 3088498-7 1986 Treatment with exo-beta-galactosidase transformed the trisaccharide OS II into the disaccharide OS I, indicating that the deficiency of beta-galactosidase in GM1 gangliosidosis type I, but not in type II, also affects glycoprotein catabolism, leading to the accumulation of glycopeptides containing terminal beta-galactosyl residues and N-acetyllactosamine repeating units. N-acetyllactosamine 337-356 galactosidase beta 1 Homo sapiens 19-37 3160874-1 1985 Normal human urine was found to contain beta (1-3)N-acetylglucosaminyltransferase catalyzing the transfer of N-acetylglucosamine from UDP-GlcNAc to N-acetyllactosamine and lactose. N-acetyllactosamine 148-167 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 40-49 4066673-6 1985 The occurrence of repeating N-acetyllactosamine sequences in the N-linked carbohydrate units of GP-1 and GP-3 was suggested by the composition and size of the oligosaccharides released by hydrazinolysis and was demonstrated by endo-beta-galactosidase treatment. N-acetyllactosamine 28-47 galactosidase beta 1 Bos taurus 232-250 2994717-0 1985 The oligosaccharide moiety of the beta 1-adrenergic receptor from turkey erythrocytes has a biantennary, N-acetyllactosamine-containing structure. N-acetyllactosamine 105-124 beta-1 adrenergic receptor Meleagris gallopavo 34-60 3927048-10 1985 Galactosyltransferase and components F-1 and F-2 differed in their sensitivity to alpha-lactalbumin-induced inhibition of N-acetyllactosamine synthesis. N-acetyllactosamine 122-141 coagulation factor II, thrombin Homo sapiens 37-48 3927048-10 1985 Galactosyltransferase and components F-1 and F-2 differed in their sensitivity to alpha-lactalbumin-induced inhibition of N-acetyllactosamine synthesis. N-acetyllactosamine 122-141 lactalbumin alpha Homo sapiens 82-99 3886793-9 1985 In addition, both [35S]sulfate-labeled alpha- and beta-chains were susceptible to Keratanase and endo-beta-galactosidase digestions, indicating the presence of sulfated N-acetyllactosamine sequences. N-acetyllactosamine 169-188 galactosidase, beta 1 Mus musculus 102-120 3160874-3 1985 The product of the transferase reaction with N-acetyllactosamine as acceptor was identified by methylation analysis as GlcNAc beta (1-3)Gal beta (1-4)GlcNAc. N-acetyllactosamine 45-64 potassium calcium-activated channel subfamily M regulatory beta subunit 2 Homo sapiens 126-135 3872120-4 1985 When these intact vesicles containing the acceptor, N-acetylglucosamine, were incubated in the presence of UDP-galactose and two inhibitors of galactosyltransferase activity, the product, N-acetyl-lactosamine, formed within the vesicles. N-acetyllactosamine 188-208 glycoprotein alpha-galactosyltransferase 1 Rattus norvegicus 143-164 32798366-6 2021 The recombinant beta-galactosidase showed comparable hydrolyzing properties towards lactose, N-acetyllactosamine, and pNP-beta-D-galactoside. N-acetyllactosamine 93-112 galactosidase beta 1 Bos taurus 16-34 6088322-4 1984 Galactosyltransferase immobilized onto agarose through its sulfhydryl group retained its ability to catalyze the synthesis of N-acetyllactosamine and lactose. N-acetyllactosamine 126-145 N-acetyllactosaminide alpha-1,3-galactosyltransferase Bos taurus 0-21 6684483-1 1983 Sex hormone-binding globulin from human blood serum contains two biantennary N-linked oligosaccharide chains of the N-acetyllactosamine type and one O-linked oligosaccharide per one molecule of the glycoprotein. N-acetyllactosamine 116-135 sex hormone binding globulin Homo sapiens 0-28 6615729-6 1983 The CDA II anion transport protein had a substantially reduced content of N-acetylglucosamine and galactose, which probably reflects a reduction in the number of N-acetyl-lactosamine units carried by the protein. N-acetyllactosamine 162-182 SEC23 homolog B, COPII coat complex component Homo sapiens 4-10 7055606-1 1982 Methylation analysis of human transcortin showed that this glycoprotein contains N-glycosidically linked oligosaccharide chains of N-acetyllactosamine type, most of the chains being biantennary and others tri- and/or tetra-antennary. N-acetyllactosamine 131-150 serpin family A member 6 Homo sapiens 30-41 6932503-7 1980 The binding of the radioactive MGP to bacterial cells was specifically inhibited by galactose, lactose and N-acetyllactosamine. N-acetyllactosamine 107-126 matrix Gla protein Homo sapiens 31-34 1204653-6 1975 Differences in the rate of production of N-acetyllactosamine in the presence of alpha-lactalbumin were also observed. N-acetyllactosamine 41-60 lactalbumin alpha Homo sapiens 80-97 1204653-7 1975 For the lowest-molecular-weight species it was found that the inhibitory effect of alpha-lactalbumin upon N-acetyllactosamine synthesis becomes an activating effect at higher alpha-lactalbumin concentrations, while no such inversion was observed for the other species. N-acetyllactosamine 106-125 lactalbumin alpha Homo sapiens 83-100 1204653-7 1975 For the lowest-molecular-weight species it was found that the inhibitory effect of alpha-lactalbumin upon N-acetyllactosamine synthesis becomes an activating effect at higher alpha-lactalbumin concentrations, while no such inversion was observed for the other species. N-acetyllactosamine 106-125 lactalbumin alpha Homo sapiens 175-192 33978732-2 2021 Galectin-1, an endogenous lectin with affinity for N-acetyllactosamine (LacNAc)-containing glycans, has emerged as a regulator of inflammatory and metabolic disorders. N-acetyllactosamine 51-70 lectin, galactose binding, soluble 1 Mus musculus 0-10 6236210-2 1984 The reaction product was hydrolyzed by beta-N-acetylglucosaminidase and released [14C]N-acetylglucosamine, indicating that the N-acetylglucosaminyl residue was beta-linked to N-acetyllactosamine. N-acetyllactosamine 175-194 O-GlcNAcase Homo sapiens 39-67 6725252-3 1984 As described in this report, the latter lectin binds glycopeptides that contain either the repeating N-acetyllactosamine sequence or an outer mannose residue substituted at C-2 and C-6 by N-acetyllactosamine. N-acetyllactosamine 188-207 complement component 2 (within H-2S) Mus musculus 173-176 6725252-3 1984 As described in this report, the latter lectin binds glycopeptides that contain either the repeating N-acetyllactosamine sequence or an outer mannose residue substituted at C-2 and C-6 by N-acetyllactosamine. N-acetyllactosamine 188-207 complement component 6 Mus musculus 181-184 6370756-7 1984 The binding of J1 to adult testicular cells was inhibited specifically by N-acetylglucosamine and the binding of both C6 and A5 was inhibited by N-acetyllactosamine. N-acetyllactosamine 145-164 complement component 6 Mus musculus 118-127 6226355-9 1983 Methylation analysis of the products of 2-acetamido-2-deoxy-D-glucosyl transfer to N-acetyllactosamine [beta-D-Galp-(1 leads to 4)-D-GlcNAc] and lactose [beta-D-Galp-(1 leads to 4)-D-Glc] revealed that the terminal, nonreducing D-galactosyl group in both these acceptors had been 3-O-substituted with 2-acetamido-2-deoxy-D-glucose. N-acetyllactosamine 83-102 galanin like peptide Homo sapiens 111-115 6226355-9 1983 Methylation analysis of the products of 2-acetamido-2-deoxy-D-glucosyl transfer to N-acetyllactosamine [beta-D-Galp-(1 leads to 4)-D-GlcNAc] and lactose [beta-D-Galp-(1 leads to 4)-D-Glc] revealed that the terminal, nonreducing D-galactosyl group in both these acceptors had been 3-O-substituted with 2-acetamido-2-deoxy-D-glucose. N-acetyllactosamine 83-102 galanin like peptide Homo sapiens 161-165 818085-12 1976 This synergism also accounts for the activation of N-acetyllactosamine synthesis by alpha-lactalbumin at low concentrations (less than 2 mM) of N-acetylglucosamine. N-acetyllactosamine 51-70 lactalbumin alpha Bos taurus 84-101 31888963-9 2020 N38 and N74 of CD16a both contain highly processed complex-type N-glycans with N-acetyllactosamine repeats and complex-type biantennary N-glycans dominate at N169. N-acetyllactosamine 79-98 Fc gamma receptor IIIa Homo sapiens 15-20 31365668-2 2019 Galectin 3 is a unique ~31 kDa protein that recognizes the N-acetyl-lactosamine structure of several glycoconjugates. N-acetyllactosamine 59-79 galectin 3 Homo sapiens 0-10 31647490-3 2019 The probe employs tetraphenylethene (TPE) as the fluorescent core structure and N-acetyllactosamine (LacNAc) as galactoside residues and self-aggregates into uniform nanoparticles with multiple binding sites on the surface targeting galectin-3. N-acetyllactosamine 80-99 galectin 3 Homo sapiens 233-243 30823584-10 2019 Bacterial agglutination, anti-biofilm activity, cell adhesion, and p38 activation were all suppressed by co-presence of LacNAc. N-acetyllactosamine 120-126 mitogen-activated protein kinase 14 Homo sapiens 67-70 30736336-4 2019 Previously, LT from human- and porcine-infecting ETEC (hLT and pLT, respectively) were shown to have different carbohydrate-binding specificities, in particular with respect to N-acetyllactosamine-terminating glycosphingolipids. N-acetyllactosamine 177-196 N-acylethanolamine acid amidase Homo sapiens 63-66 30372040-4 2018 Here, the enzymatic addition of galactose to N-acetylglucosamine functionalized glycodendrimers reduced the requisite number of synthetic steps for the full chemical synthesis of N-acetyl lactosamine (Lac NAc) functionalized dendrimers to four steps. N-acetyllactosamine 179-199 synuclein alpha Homo sapiens 205-208 29087466-2 2018 Previous studies with monoclonal antibody have implicated a regulated expression of 6-sulfo-alpha2-6-sialyl LacNAc on B cells in peripheral lymph nodes and the circulating peripheral blood lymphocytes but its occurrence on leukemia cells or lymphomas have not been critically addressed. N-acetyllactosamine 108-114 immunoglobulin binding protein 1 Homo sapiens 92-100 29087466-6 2018 The GlcNAc-6-O-sulfated alpha2-6-sialyl LacNAc, which constitutes the higher affinity ligand for the human inhibitory co-receptor of B cells, CD22, was found to be commonly carried on a range of complex type N-glycans from human CD19+ and CD4+ lymphocytes. N-acetyllactosamine 40-46 immunoglobulin binding protein 1 Homo sapiens 24-32 29087466-6 2018 The GlcNAc-6-O-sulfated alpha2-6-sialyl LacNAc, which constitutes the higher affinity ligand for the human inhibitory co-receptor of B cells, CD22, was found to be commonly carried on a range of complex type N-glycans from human CD19+ and CD4+ lymphocytes. N-acetyllactosamine 40-46 CD22 molecule Homo sapiens 142-146 29087466-6 2018 The GlcNAc-6-O-sulfated alpha2-6-sialyl LacNAc, which constitutes the higher affinity ligand for the human inhibitory co-receptor of B cells, CD22, was found to be commonly carried on a range of complex type N-glycans from human CD19+ and CD4+ lymphocytes. N-acetyllactosamine 40-46 CD19 molecule Homo sapiens 229-233 29659839-1 2018 Siglec-F is a pro-apoptotic receptor on mouse eosinophils that recognizes 6"-sulfated sialyl Lewis X and 6"-sulfated sialyl N-acetyl-lactosamine as well as multivalent sialyl N-acetyl-lactosamine structures on glycan arrays. N-acetyllactosamine 124-144 sialic acid binding Ig-like lectin F Mus musculus 0-8 29659839-1 2018 Siglec-F is a pro-apoptotic receptor on mouse eosinophils that recognizes 6"-sulfated sialyl Lewis X and 6"-sulfated sialyl N-acetyl-lactosamine as well as multivalent sialyl N-acetyl-lactosamine structures on glycan arrays. N-acetyllactosamine 175-195 sialic acid binding Ig-like lectin F Mus musculus 0-8 28976746-8 2017 Furthermore, neo-glycoproteins with terminal biotinylated LacNAc glycan motif could be utilized as Gal-3 detection agents in a sandwich enzyme-linked immunosorbent assay format. N-acetyllactosamine 58-64 galectin 3 Homo sapiens 99-104 29807358-9 2018 RAP increased Gal-3 levels and activated the TGF-beta1/alpha-SMA/Col I pathway in rabbit left atria, while the Gal-3 inhibitor N-acetyllactosamine, injected at 4.5 mg/kg every 3 days, mitigated these adverse changes. N-acetyllactosamine 127-146 galectin-3 Oryctolagus cuniculus 111-116 29429899-6 2018 We discover that blocking access to LacNAc on Paneth cells leads to hyperproliferation of the neighboring Lgr5+ stem cells, which is accompanied by the downregulation of genes that are known as negative regulators of proliferation. N-acetyllactosamine 36-42 leucine rich repeat containing G protein coupled receptor 5 Mus musculus 106-110 29315388-1 2018 Over the last few decades galectin-3, a carbohydrate binding protein, with affinity for N-acetyllactosamine residues, has been unique due to the regulatory roles it performs in processes associated with tumor progression and metastasis such as cell proliferation, homotypic/heterotypic aggregation, dynamic cellular transformation, migration and invasion, survival and apoptosis. N-acetyllactosamine 88-107 galectin 3 Homo sapiens 26-36 29373511-3 2018 Gal-3 recognizes poly-N-acetyllactosamine (LacNAc)-based carbohydrate motifs of glycoproteins and glycolipids with a high specificity for internal LacNAc epitopes. N-acetyllactosamine 43-49 galectin 3 Homo sapiens 0-5 29373511-3 2018 Gal-3 recognizes poly-N-acetyllactosamine (LacNAc)-based carbohydrate motifs of glycoproteins and glycolipids with a high specificity for internal LacNAc epitopes. N-acetyllactosamine 147-153 galectin 3 Homo sapiens 0-5 27560716-1 2016 Alpha1,2-fucosyltransferases, FUT1 and FUT2, which transfer fucoses onto the terminal galactose of N-acetyl-lactosamine via alpha1,2-linkage have been shown to be highly expressed in various types of cancers. N-acetyllactosamine 99-119 fucosyltransferase 1 (H blood group) Homo sapiens 30-34 28796164-6 2017 We observed a significantly increased affinity of Gal-3 towards the multivalent neo-glycoprotein presenting LacNAc type 1 repeating units. N-acetyllactosamine 109-115 galectin 3 Homo sapiens 50-55 28487369-4 2017 Now, using MALDI-TOF mass spectrometry, we report that transmembrane mucin N-glycans in differentiated human corneal epithelial cells contain primarily complex-type structures with N-acetyllactosamine, a preferred galectin ligand. N-acetyllactosamine 181-200 LOC100508689 Homo sapiens 69-74 28952509-0 2017 Biotinylated N-Acetyllactosamine- and N,N-Diacetyllactosamine-Based Oligosaccharides as Novel Ligands for Human Galectin-3. N-acetyllactosamine 13-32 galectin 3 Homo sapiens 112-122 27315572-0 2017 Autocrine TNF-alpha and IL-1beta prime 6-sulfo LacNAc+ dendritic cells for high-level production of IL-23. N-acetyllactosamine 47-53 tumor necrosis factor Homo sapiens 10-19 27315572-0 2017 Autocrine TNF-alpha and IL-1beta prime 6-sulfo LacNAc+ dendritic cells for high-level production of IL-23. N-acetyllactosamine 47-53 interleukin 1 beta Homo sapiens 24-32 27315572-0 2017 Autocrine TNF-alpha and IL-1beta prime 6-sulfo LacNAc+ dendritic cells for high-level production of IL-23. N-acetyllactosamine 47-53 interleukin 23 subunit alpha Homo sapiens 100-105 27706921-7 2016 The study revealed that there was a wide range of glycoforms spaced by 365 Da intervals, namely, HexHexNAc units, which indicated that NESP biosimilars likely contained more N-acetyllactosamine units in their molecules. N-acetyllactosamine 174-193 GNAS complex locus Homo sapiens 135-139 28936496-2 2017 Noticeably, while difucosylation of tetrasaccharides was readily achieved using an excess amount of donor, the synthesis of LNFP III was achieved by Hp3/4FT-catalyzed selective fucosylation of the N-acetyllactosamine (LacNAc) component in lacto-N-neotetraose (LNnT). N-acetyllactosamine 197-216 defensin alpha 3 Homo sapiens 149-152 28947766-4 2017 The bifunctional lectin galectin-4 (Gal-4) organizes the transport of axon glycoproteins by binding to N-acetyllactosamine (LacNac) termini of N-glycans. N-acetyllactosamine 103-122 galectin 4 Homo sapiens 24-34 28947766-4 2017 The bifunctional lectin galectin-4 (Gal-4) organizes the transport of axon glycoproteins by binding to N-acetyllactosamine (LacNac) termini of N-glycans. N-acetyllactosamine 103-122 galectin 4 Homo sapiens 36-41 28947766-4 2017 The bifunctional lectin galectin-4 (Gal-4) organizes the transport of axon glycoproteins by binding to N-acetyllactosamine (LacNac) termini of N-glycans. N-acetyllactosamine 124-130 galectin 4 Homo sapiens 24-34 28947766-4 2017 The bifunctional lectin galectin-4 (Gal-4) organizes the transport of axon glycoproteins by binding to N-acetyllactosamine (LacNac) termini of N-glycans. N-acetyllactosamine 124-130 galectin 4 Homo sapiens 36-41 28769928-0 2017 Anaphylatoxin C5a Regulates 6-Sulfo-LacNAc Dendritic Cell Function in Human through Crosstalk with Toll-Like Receptor-Induced CREB Signaling. N-acetyllactosamine 36-42 complement C5a receptor 1 Homo sapiens 14-17 28374933-3 2017 Loss of CMAS activity resulted in an asialo cell surface accompanied by an increase in glycoconjugates with terminal galactosyl and oligo-LacNAc residues, as well as intracellular accumulation of free Sia. N-acetyllactosamine 138-144 cytidine monophospho-N-acetylneuraminic acid synthetase Mus musculus 8-12 27560716-1 2016 Alpha1,2-fucosyltransferases, FUT1 and FUT2, which transfer fucoses onto the terminal galactose of N-acetyl-lactosamine via alpha1,2-linkage have been shown to be highly expressed in various types of cancers. N-acetyllactosamine 99-119 fucosyltransferase 2 Homo sapiens 39-43 27427828-5 2016 The multifunctional human galectin-3 (Gal-3) is a beta-galactoside binding lectin that preferentially binds to N-acetyllactosamine moieties on glycoconjugates. N-acetyllactosamine 111-130 galectin 3 Homo sapiens 26-36 27427828-5 2016 The multifunctional human galectin-3 (Gal-3) is a beta-galactoside binding lectin that preferentially binds to N-acetyllactosamine moieties on glycoconjugates. N-acetyllactosamine 111-130 galectin 3 Homo sapiens 38-43 27427828-12 2016 Both observations strongly suggest that GAGs primarily occupy the lactose/LacNAc binding site of Gal-3. N-acetyllactosamine 74-80 galectin 3 Homo sapiens 97-102 27496330-2 2016 Here we show that galectin-1 (Gal-1), an endogenous lectin that recognizes glycans bearing N-acetyllactosamine (LacNAc) epitopes, induces branching migration of mammary epithelia in vivo, ex vivo, and in 3D organotypic cultures. N-acetyllactosamine 91-110 galectin 1 Homo sapiens 18-28 27496330-2 2016 Here we show that galectin-1 (Gal-1), an endogenous lectin that recognizes glycans bearing N-acetyllactosamine (LacNAc) epitopes, induces branching migration of mammary epithelia in vivo, ex vivo, and in 3D organotypic cultures. N-acetyllactosamine 91-110 galectin 1 Homo sapiens 30-35 26495044-9 2015 Galectin-1 binding to LacNAc-Q11 nanofibers was specific because it could be inhibited by excess soluble beta-lactose, a galectin-binding carbohydrate. N-acetyllactosamine 22-28 galectin 1 Homo sapiens 0-10 26804479-2 2016 alpha1,3-FucT from Helicobacter pylori 26695 (FutA) accepts lactose and LacNAc as glycan acceptors and has a very low level of expression in Escherichia coli, and it shows a low catalytic activity for lactose in the large-scale synthesis of 3-FL. N-acetyllactosamine 72-78 fucosyltransferase 11 Homo sapiens 0-13 26495044-7 2015 LacNAc-Q11 nanofibers bound galectin-1 and -3 in a LacNAc concentration-dependent manner, although nanofibers bound galectin-1 with higher affinity than galectin-3. N-acetyllactosamine 0-6 galectin 1 Homo sapiens 28-45 27269286-4 2016 Galectins bind N-acetyllactosamine (LacNAc) units within N-glycans initiated from UDP-GlcNAc by the medial-Golgi branching enzymes as well as the trans-Golgi poly-LacNAc extension enzyme beta1,3-N-acetylglucosaminyltransferase (B3GNT). N-acetyllactosamine 15-34 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 228-233 27269286-4 2016 Galectins bind N-acetyllactosamine (LacNAc) units within N-glycans initiated from UDP-GlcNAc by the medial-Golgi branching enzymes as well as the trans-Golgi poly-LacNAc extension enzyme beta1,3-N-acetylglucosaminyltransferase (B3GNT). N-acetyllactosamine 36-42 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 187-226 27269286-4 2016 Galectins bind N-acetyllactosamine (LacNAc) units within N-glycans initiated from UDP-GlcNAc by the medial-Golgi branching enzymes as well as the trans-Golgi poly-LacNAc extension enzyme beta1,3-N-acetylglucosaminyltransferase (B3GNT). N-acetyllactosamine 36-42 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 228-233 27172906-1 2016 A sialic acid-binding lectin (SRC) was created from the C-terminal domain of an R-type N-acetyl lactosamine-binding lectin (EW29Ch) by natural evolution-mimicry. N-acetyllactosamine 87-107 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 30-33 26968649-1 2016 beta1-3-N-Acetylglucosaminyltransferases (beta3GlcNAcTs) and beta1-4-galactosyltransferases (beta4GalTs) have been broadly used in enzymatic synthesis of N-acetyllactosamine (LacNAc)-containing oligosaccharides and glycoconjugates including poly-LacNAc, and lacto-N-neotetraose (LNnT) found in the milk of human and other mammals. N-acetyllactosamine 154-173 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 0-7 26968649-1 2016 beta1-3-N-Acetylglucosaminyltransferases (beta3GlcNAcTs) and beta1-4-galactosyltransferases (beta4GalTs) have been broadly used in enzymatic synthesis of N-acetyllactosamine (LacNAc)-containing oligosaccharides and glycoconjugates including poly-LacNAc, and lacto-N-neotetraose (LNnT) found in the milk of human and other mammals. N-acetyllactosamine 175-181 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 0-7 26168351-6 2015 Compared with that from MCF-7, the Gal-3BP from MDA-MB-231 cells had fewer tetra-antennary structures, only alpha1,6-linked core fucoses, and more LacNAc repeat structures; the MDA-MB-231 cells had no surface galectin-3 but used surface galectin-1 for interaction with Gal-3BP to form large oligomers and cell aggregates. N-acetyllactosamine 147-153 galectin 3 binding protein Homo sapiens 35-42 26495044-7 2015 LacNAc-Q11 nanofibers bound galectin-1 and -3 in a LacNAc concentration-dependent manner, although nanofibers bound galectin-1 with higher affinity than galectin-3. N-acetyllactosamine 0-6 galectin 1 Homo sapiens 28-38 26495044-10 2015 LacNAc-Q11 nanofibers inhibited galectin-1-mediated apoptosis of Jurkat T cells in a LacNAc concentration-dependent manner, but were unable to inhibit galectin-3 activity, consistent with galectin-binding affinity of the nanofibers. N-acetyllactosamine 0-6 galectin 1 Homo sapiens 32-42 26495044-10 2015 LacNAc-Q11 nanofibers inhibited galectin-1-mediated apoptosis of Jurkat T cells in a LacNAc concentration-dependent manner, but were unable to inhibit galectin-3 activity, consistent with galectin-binding affinity of the nanofibers. N-acetyllactosamine 85-91 galectin 1 Homo sapiens 32-42 25726973-6 2015 Mass spectrometric analysis (HPLC-ESI-MS/MS) of GP5 N-glycans revealed an abundance of N-acetylglucosamine (GlcNAc) and N-acetyllactosamine (LacNAc) oligomers in addition to sialic acids. N-acetyllactosamine 120-139 glycoprotein V platelet Homo sapiens 48-51 25726973-6 2015 Mass spectrometric analysis (HPLC-ESI-MS/MS) of GP5 N-glycans revealed an abundance of N-acetylglucosamine (GlcNAc) and N-acetyllactosamine (LacNAc) oligomers in addition to sialic acids. N-acetyllactosamine 141-147 glycoprotein V platelet Homo sapiens 48-51 25503732-4 2015 Male REN2 rats were treated with N-acetyllactosamine [galectin-3 inhibitor (Gal3i)] for 6 wk; untreated REN2 and Sprague-Dawley rats served as controls. N-acetyllactosamine 33-52 galectin 3 Rattus norvegicus 54-64 25498912-3 2015 We evaluated the role of 3 alpha(2,3)sialyltransferases, ST3Gal-3, -4, and -6, which act on the type II N-Acetyllactosamine structure (Galbeta1,4GlcNAc) to create sialyl Lewis-X (sLe(X)) and related sialofucosylated glycans on human leukocytes of myeloid lineage. N-acetyllactosamine 104-123 ST3 beta-galactoside alpha-2,3-sialyltransferase 3 Homo sapiens 57-77 25708191-5 2015 Here we show that GAL1/pre-BCR interaction modifies GAL1/glycan affinity and particularly inhibits binding to LacNAc containing epitopes. N-acetyllactosamine 110-116 galectin 1 Homo sapiens 18-22 25708191-5 2015 Here we show that GAL1/pre-BCR interaction modifies GAL1/glycan affinity and particularly inhibits binding to LacNAc containing epitopes. N-acetyllactosamine 110-116 galectin 1 Homo sapiens 52-56 24517196-7 2014 Unlike LDL, plasma lipoprotein(a) [Lp(a)] coated on polystyrene well and desialylated by neuraminidase was recognized by LIg through terminal LacNAc moieties exposed by the enzyme on its apo(a) subunit. N-acetyllactosamine 142-148 lipoprotein(a) Homo sapiens 35-40 24695395-10 2014 Blockage of galectin-3 activity by N-acetyllactosamine (LacNac 10 mmol/l) reduced both collagen I and O2(*-) production induced by leptin. N-acetyllactosamine 35-54 galectin 3 Rattus norvegicus 12-22 24695395-10 2014 Blockage of galectin-3 activity by N-acetyllactosamine (LacNac 10 mmol/l) reduced both collagen I and O2(*-) production induced by leptin. N-acetyllactosamine 35-54 leptin Rattus norvegicus 131-137 24695395-10 2014 Blockage of galectin-3 activity by N-acetyllactosamine (LacNac 10 mmol/l) reduced both collagen I and O2(*-) production induced by leptin. N-acetyllactosamine 56-62 galectin 3 Rattus norvegicus 12-22 24695395-10 2014 Blockage of galectin-3 activity by N-acetyllactosamine (LacNac 10 mmol/l) reduced both collagen I and O2(*-) production induced by leptin. N-acetyllactosamine 56-62 leptin Rattus norvegicus 131-137 24517196-7 2014 Unlike LDL, plasma lipoprotein(a) [Lp(a)] coated on polystyrene well and desialylated by neuraminidase was recognized by LIg through terminal LacNAc moieties exposed by the enzyme on its apo(a) subunit. N-acetyllactosamine 142-148 neuraminidase 1 Homo sapiens 89-102 24219248-8 2014 RESULTS: Characterization of the glycolipid expression in GalT-KO/FucT-TG intestine showed absence of Gal antigens and decreased/unchanged levels of the N-acetyllactosamine precursor and the blood group H type 2 expression, when compared with the wildtype. N-acetyllactosamine 153-172 galactose-1-phosphate uridylyltransferase Sus scrofa 58-62 22740701-2 2012 The beta1-4-galactosyltransferase-I (beta4Gal-T1) enzyme is responsible for the synthesis of the N-acetyllactosamine moiety. N-acetyllactosamine 97-116 beta-1,4-galactosyltransferase 1 Homo sapiens 37-48 23263199-1 2013 Human alpha1,3-fucosyltransferase IX catalyzes the transfer of l-fucose from guanosine diphosphate-beta-L-fucose to N-acetyllactosamine, generating a Lewis X epitope, and is thereby involved in the synthesis of fucosylated cell surface glycoconjugates. N-acetyllactosamine 116-135 fucosyltransferase 9 Homo sapiens 15-36 23219268-2 2013 When galectin-1 (Gal-1) binds N-acetyllactosamines on select membrane glycoproteins on antitumor T cells, these cells either undergo apoptosis or become immunoregulatory. N-acetyllactosamine 30-50 galectin 1 Homo sapiens 5-15 23219268-2 2013 When galectin-1 (Gal-1) binds N-acetyllactosamines on select membrane glycoproteins on antitumor T cells, these cells either undergo apoptosis or become immunoregulatory. N-acetyllactosamine 30-50 galectin 1 Homo sapiens 17-22 23219268-5 2013 Recent efforts have capitalized on the anti-N-acetyllactosamine action of fluorinated glucosamines to treat antitumor T cells, resulting in diminished Gal-1-binding and higher antitumor T cell levels. N-acetyllactosamine 44-63 galectin 1 Homo sapiens 151-156 23230309-4 2013 The efficacy of the galectin-3 inhibitor N-acetyllactosamine was evaluated in TGR(mREN2)27 (REN2) rats and in wild-type mice with the aim of reversing established cardiac remodeling after transverse aortic constriction. N-acetyllactosamine 41-60 galectin 3 Rattus norvegicus 20-30 23555773-8 2013 BGA and BGB showed higher affinity than LacNAc and lactose due to generally stronger hydrogen bond interactions and water mediated hydrogen bonds with alpha1-2 fucose respectively. N-acetyllactosamine 40-46 adrenoceptor alpha 1D Homo sapiens 151-159 24244290-7 2013 These results were confirmed by strong binding of VP8* to the Lec2 cell line that expresses LacNAc oligomers but not to the Lec8 cell line lacking the LacNAc. N-acetyllactosamine 92-98 adhesion G protein-coupled receptor L1 Homo sapiens 62-66 23595060-4 2013 In this paper we calculate MM/GBSA energies with two generalised Born models for snapshots generated by the same methods or by explicit-solvent simulations for five synthetic N-acetyllactosamine derivatives binding to galectin-3. N-acetyllactosamine 175-194 galectin 3 Homo sapiens 218-228 23311731-5 2013 Furthermore, we find that Gal-4 interacts with L1 by specifically binding to LacNAc branch ends of L1 N-glycans. N-acetyllactosamine 77-83 galectin 4 Homo sapiens 26-31 23311731-7 2013 In all, Gal-4 sorts to axon plasma membrane segments by binding to sulfatide-containing microtubule-associated carriers and being bivalent, it organizes the transport of L1, and likely other axonal glycoproteins, by attaching them to the carriers through their LacNAc termini. N-acetyllactosamine 261-267 galectin 4 Homo sapiens 8-13 22187312-3 2012 METHODS: Noninvasive imaging studies were performed using a gamma camera after the intravenous administration of (123)I-GLP-1 or (123)I-alpha2, 6-sialyl N-acetyllactosamine (glycosylated) GLP-1 in rats. N-acetyllactosamine 153-172 glucagon Rattus norvegicus 188-193 22019770-3 2012 It induces apoptosis in effector T cells through homodimeric binding of N-acetyllactosamines on membrane glycoproteins (Gal-1 ligands). N-acetyllactosamine 72-92 galectin 1 Homo sapiens 120-125 22158550-3 2012 Here, to test the Gal-1-mediated tumor immune evasion hypothesis and demonstrate the importance of Gal-1-binding N-acetyllactosamines in controlling the fate and function of antitumor immune cells, we treated melanoma- or lymphoma-bearing mice with peracetylated 4-fluoro-glucosamine (4-F-GlcNAc), a metabolic inhibitor of N-acetyllactosamine biosynthesis, and analyzed tumor growth and immune profiles. N-acetyllactosamine 113-133 lectin, galactose binding, soluble 1 Mus musculus 99-104 22271523-4 2012 Interestingly, lack of the Chst3 gene (chondroitin 6-sulfotransferase) appeared to influence markedly the expression of most N-glycans, especially highly modified glycoforms bearing multiple Neu5Gc, Fuc, and LacNAc units. N-acetyllactosamine 208-214 carbohydrate sulfotransferase 3 Homo sapiens 27-32 22158550-3 2012 Here, to test the Gal-1-mediated tumor immune evasion hypothesis and demonstrate the importance of Gal-1-binding N-acetyllactosamines in controlling the fate and function of antitumor immune cells, we treated melanoma- or lymphoma-bearing mice with peracetylated 4-fluoro-glucosamine (4-F-GlcNAc), a metabolic inhibitor of N-acetyllactosamine biosynthesis, and analyzed tumor growth and immune profiles. N-acetyllactosamine 113-132 lectin, galactose binding, soluble 1 Mus musculus 99-104 22158550-6 2012 Collectively, our data suggest that metabolic lowering of Gal-1-binding N-acetyllactosamines may attenuate tumor growth by boosting antitumor immune cell levels, representing a promising approach for cancer immunotherapy. N-acetyllactosamine 72-92 lectin, galactose binding, soluble 1 Mus musculus 58-63 22004528-8 2011 Interestingly, the Fc glycoforms carrying an unusual bisecting sugar moiety such as a mannose or a LacNAc moiety also demonstrated enhanced affinity to FcgammaRIIIa. N-acetyllactosamine 99-105 Fc gamma receptor IIIa Homo sapiens 152-164 20807768-5 2010 Galectin-3 R186S, which has selectively lost affinity for LacNAc, a disaccharide moiety commonly found on glycoprotein glycans, has lost the ability to activate neutrophil leukocytes and intracellular targeting into vesicles. N-acetyllactosamine 58-64 galectin 3 Homo sapiens 0-10 21154238-1 2011 Galectin-3 belongs to a family of highly conserved animal lectins characterized by their ability to recognize multiple N-acetyllactosamine sequences, which can be displayed on both N- and O-glycans on cell surface glycoconjugates. N-acetyllactosamine 119-138 galectin 3 Homo sapiens 0-10 21077635-5 2010 It was revealed that structures of O-glycans in human milk OPN were varied with habitual fucosylation and N-acetyllactosamine units. N-acetyllactosamine 106-125 secreted phosphoprotein 1 Homo sapiens 59-62 21753146-7 2011 Synthetic sulfomodified Galbeta1-3GlcNAc disaccharides (type 1 LacNAcs) selectively prevented Gal-8 binding, leading to a blockade of Ab production in Gal-1-deficient B cells. N-acetyllactosamine 63-70 galectin 8 Homo sapiens 94-99 21753146-8 2011 Furthermore, synthetic type 1 LacNAcs that were able to block the binding of both Gals greatly reduced the effect of exogenously added recombinant Gal-1 and Gal-8 on promoting Ab production. N-acetyllactosamine 30-37 galectin 1 Homo sapiens 147-152 21753146-8 2011 Furthermore, synthetic type 1 LacNAcs that were able to block the binding of both Gals greatly reduced the effect of exogenously added recombinant Gal-1 and Gal-8 on promoting Ab production. N-acetyllactosamine 30-37 galectin 8 Homo sapiens 157-162 21963509-9 2011 Additionally, DC2.3a/LEC-12a and LEC-6 showed higher affinities for the galactosebeta1 4fucose (Galbeta1 4Fuc) disaccharide than for N-acetyllactosamine. N-acetyllactosamine 133-152 Galectin Caenorhabditis elegans 33-38 20625591-2 2010 They have been used in an efficient one-pot multienzyme system to synthesize LacNAc, lactose, and their derivatives including those containing negatively charged 6-O-sulfated GlcNAc and C2-substituted GlcNAc or Glc, from monosaccharide derivatives and inexpensive Glc-1-P. N-acetyllactosamine 77-83 GLC1P Homo sapiens 264-271 19951367-7 2010 We also demonstrated that the binding of galectin-3 to host N-acetyllactosamine-containing glycans, was required for forming the structures. N-acetyllactosamine 60-79 galectin 3 Homo sapiens 41-51 20032467-3 2010 L-ficolin preferentially recognized disulfated N-acetyllactosamine and tri- and tetrasaccharides containing terminal galactose or N-acetylglucosamine. N-acetyllactosamine 47-66 ficolin 2 Homo sapiens 0-9 19819223-2 2009 We have employed a combination of cysteine mutagenesis with chemical crosslinking using a photoactivatable sulfhydryl reagent benzophenone-4-maleimide to obtain a covalent complex between human galectin-1 and the model glycoprotein ligands asialofetuin and laminin which contain an N-acetyllactosamine structure. N-acetyllactosamine 282-301 galectin 1 Homo sapiens 194-204 19996411-7 2010 A 70% to 85% reduction in HECA-452 binding epitope and N-acetyl lactosamine content in PSGL-1 was also noted on 4F-GalNAc addition. N-acetyllactosamine 55-75 selectin P ligand Homo sapiens 87-93 19361194-5 2009 Addition of sialyl LacNAc to GLP-1 greatly improved stability against DPP-IV and NEP 24.11 as compared to the native type. N-acetyllactosamine 19-25 glucagon Mus musculus 29-34 19729452-1 2009 HNK-1 (human natural killer-1) glyco-epitope, a sulfated glucuronic acid attached to N-acetyllactosamine on the nonreducing termini of glycans, is highly expressed in the nervous system. N-acetyllactosamine 85-104 beta-1,3-glucuronyltransferase 1 Homo sapiens 0-5 19437454-8 2009 CONCLUSION: In view of the fact that the carbohydrate recognition domain of GAL1 recognises the structural motif N-acetyl lactosamine (Gal beta 1-4 GlcNAc), which is similar to that of chitin (beta-1,4 N-acetyl-D-glucosamine), it is proposed that the insecticidal mechanism of GAL1 involves direct binding with chitin to interfere with the structure of the PM. N-acetyllactosamine 113-133 galectin 1 Homo sapiens 76-80 19437454-8 2009 CONCLUSION: In view of the fact that the carbohydrate recognition domain of GAL1 recognises the structural motif N-acetyl lactosamine (Gal beta 1-4 GlcNAc), which is similar to that of chitin (beta-1,4 N-acetyl-D-glucosamine), it is proposed that the insecticidal mechanism of GAL1 involves direct binding with chitin to interfere with the structure of the PM. N-acetyllactosamine 113-133 galectin 1 Homo sapiens 277-281 19426135-7 2009 Thus, N-glycans rather than O-glycans contain the N-acetyllactosamine recognition signals for the lipid raft-based galectin-4-dependent apical delivery. N-acetyllactosamine 50-69 galectin 4 Homo sapiens 115-125 19432560-2 2009 Although most structural studies with gal-1 have investigated its binding to simple carbohydrates, in particular lactose and N-acetyl-lactosamine, this view is limited, because gal-1 functions at the cell surface by interacting with more complex glycans that are heterogeneous in size and composition. N-acetyllactosamine 125-145 galectin 1 Homo sapiens 38-43 19476346-5 2009 Solid phase array analysis identified two HCR/F binding glycans: ganglioside GD1a and oligosaccharides containing an N-acetyllactosamine core. N-acetyllactosamine 117-136 coiled-coil alpha-helical rod protein 1 Rattus norvegicus 42-45 19515362-2 2009 A comparison with N-glycan profiles from plants expressing only the hybrid beta-(1-->4)-galactosyltransferase suggested that the fucosylation of the LacNAc residues in line xFxG1 protected galactosylated N-glycans from endogenous plant beta-galactosidase activity. N-acetyllactosamine 152-158 beta-galactosidase Nicotiana tabacum 239-257 19361194-5 2009 Addition of sialyl LacNAc to GLP-1 greatly improved stability against DPP-IV and NEP 24.11 as compared to the native type. N-acetyllactosamine 19-25 dipeptidylpeptidase 4 Mus musculus 70-76 19361194-5 2009 Addition of sialyl LacNAc to GLP-1 greatly improved stability against DPP-IV and NEP 24.11 as compared to the native type. N-acetyllactosamine 19-25 membrane metallo endopeptidase Mus musculus 81-84 19361194-8 2009 In addition, the stability of GLP-1 against both DPP-IV and NEP24.11 incrementally improved with an increase in the content of sialyl LacNAc in the peptide. N-acetyllactosamine 134-140 glucagon Mus musculus 30-35 18849325-5 2009 The effect was lactose-inhibitable and required galectin-3 affinity for N-acetyllactosamine, a saccharide typically found on cell surface glycoproteins, since a mutant lacking this activity was without effect. N-acetyllactosamine 72-91 galectin 3 Homo sapiens 48-58 18810635-6 2009 Glycan array screening indicated that galectin-14 recognizes terminal N-acetyllactosamine residues which can be modified with alpha1-2-fucosylation and, uniquely for a galectin, prefers alpha2- over alpha2-sialylation. N-acetyllactosamine 70-89 galectin 14 Homo sapiens 38-49 19191477-8 2009 The structure of BT1043 complexed with N-acetyllactosamine reveals that recognition is mediated via hydrogen bonding interactions with the reducing end of beta-N-acetylglucosamine, suggesting a role in binding glycans liberated from the mucin polypeptide. N-acetyllactosamine 39-58 LOC100508689 Homo sapiens 237-242 18977853-4 2009 Here we report the crystal structure of the human galectin-9 N-terminal carbohydrate recognition domain in complex with N-acetyllactosamine dimers and trimers. N-acetyllactosamine 120-139 galectin 9 Homo sapiens 50-60 18977853-5 2009 These complex structures revealed that the galectin-9 N-terminal carbohydrate recognition domain can recognize internal N-acetyllactosamine units within poly-N-acetyllactosamine chains. N-acetyllactosamine 120-139 galectin 9 Homo sapiens 43-53 19500344-9 2009 Fluorescently-labelled N-acetyllactosamine (LacNAc) glycoside containing dansyl group was synthesized chemo-enzymatically as high-sensitivity acceptor substrate for ST6Gal1. N-acetyllactosamine 23-42 ST6 beta-galactoside alpha-2,6-sialyltransferase 1 Rattus norvegicus 165-172 19500344-9 2009 Fluorescently-labelled N-acetyllactosamine (LacNAc) glycoside containing dansyl group was synthesized chemo-enzymatically as high-sensitivity acceptor substrate for ST6Gal1. N-acetyllactosamine 44-50 ST6 beta-galactoside alpha-2,6-sialyltransferase 1 Rattus norvegicus 165-172 19245254-6 2009 We show that the mutants (280)SGG(282) and (280)AGG(282) with the highest GalNAc-T activity can also transfer modified sugars such as 2-keto-galactose or GalNAz from their respective UDP-sugar derivatives to LacNAc moiety present at the nonreducing end of glycans of asialofetuin, thus enabling the detection of LacNAc moiety of glycoproteins and glycolipids by a chemiluminescence method. N-acetyllactosamine 208-214 beta-1,4-N-acetyl-galactosaminyltransferase 1 Homo sapiens 74-82 19245254-6 2009 We show that the mutants (280)SGG(282) and (280)AGG(282) with the highest GalNAc-T activity can also transfer modified sugars such as 2-keto-galactose or GalNAz from their respective UDP-sugar derivatives to LacNAc moiety present at the nonreducing end of glycans of asialofetuin, thus enabling the detection of LacNAc moiety of glycoproteins and glycolipids by a chemiluminescence method. N-acetyllactosamine 312-318 beta-1,4-N-acetyl-galactosaminyltransferase 1 Homo sapiens 74-82 18804089-7 2008 Furthermore, the N-glycan analysis indicated a lower heterogeneity from epoetin delta when compared with its CHO homologue, being predominantly tetraantennary without N-acetyllactosamine repeats in the former. N-acetyllactosamine 167-186 erythropoietin Homo sapiens 72-79 18838383-8 2008 N-Acetyllactosamine, but not sucrose, treatment of cells results in decreased RPTP retention, showing that galectin-1 binding contributes to the increased retention after GnT-Vb expression. N-acetyllactosamine 0-19 galectin 1 Homo sapiens 107-117 18838383-8 2008 N-Acetyllactosamine, but not sucrose, treatment of cells results in decreased RPTP retention, showing that galectin-1 binding contributes to the increased retention after GnT-Vb expression. N-acetyllactosamine 0-19 alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase B Homo sapiens 171-177 18579791-3 2008 We report here that sialylated glycosphingolipids with 5 N-acetyllactosamine (LacNAc, Galbeta1-4GlcNAcbeta1-3) repeats and 2 to 3 fucose residues are major functional E-selectin receptors on human neutrophils. N-acetyllactosamine 57-76 selectin E Homo sapiens 167-177 18579791-7 2008 Quantitatively minor terminally sialylated glycosphingolipids with 5 to 6 LacNAc repeats and 2 to 3 fucose residues were highly potent E-selectin receptors, constituting more than 60% of the E-selectin-binding activity in the extract. N-acetyllactosamine 74-80 selectin E Homo sapiens 135-145 18579791-7 2008 Quantitatively minor terminally sialylated glycosphingolipids with 5 to 6 LacNAc repeats and 2 to 3 fucose residues were highly potent E-selectin receptors, constituting more than 60% of the E-selectin-binding activity in the extract. N-acetyllactosamine 74-80 selectin E Homo sapiens 191-201 18725453-6 2008 The latter was shown using a galectin-3 mutant that lacked N-acetyllactosamine binding activity, and this protein was not active. N-acetyllactosamine 59-78 galectin 3 Homo sapiens 29-39 18056365-9 2007 Interestingly, the binding of the LacNAc-specific lectins galectin-3 and -8 increased during maturation and up-regulation of sialic acid expression by mDC correlated with an increased binding of siglec-1, -2, and -7. N-acetyllactosamine 34-40 chemokine (C-C motif) ligand 22 Mus musculus 151-154 18802059-7 2008 Lastly, we found that the sugar compound N-acetyllactosamine blocked the binding of galectin-1 to murine splenic B cells and inhibited their differentiation. N-acetyllactosamine 41-60 lectin, galactose binding, soluble 1 Mus musculus 84-94 18024472-3 2008 The HNK-1 carbohydrate has a unique structural feature, i.e. a sulfated glucuronic acid is attached to the non-reducing terminal of an N-acetyllactosamine residue (HSO(3)-3GlcAbeta1-3Galbeta1-4GlcNAc-). N-acetyllactosamine 135-154 beta-1,3-glucuronyltransferase 1 Homo sapiens 4-9 18725453-5 2008 The effect was inhibited by the competitor lactose and required the affinity of galectin-3 for N-acetyllactosamine, a saccharide typically found on cell surface glycoproteins. N-acetyllactosamine 95-114 galectin 3 Homo sapiens 80-90 18263896-8 2008 The binding of galectin-3 to serum glycoproteins requires affinity for LacNAc, since a mutant (R186S), which has lost this affinity, did not bind any serum glycoproteins. N-acetyllactosamine 71-77 galectin 3 Homo sapiens 15-25 18216021-8 2008 However, only Gal-3 bound internal LacNAc within poly(LacNAc). N-acetyllactosamine 35-41 galectin 3 Homo sapiens 14-19 18216021-8 2008 However, only Gal-3 bound internal LacNAc within poly(LacNAc). N-acetyllactosamine 54-60 galectin 3 Homo sapiens 14-19 18256179-5 2008 Using the most frequently studied galectins-1 and -3, application of this assay led to rather equal binding levels for linear and branched oligomers of N-acetyllactosamine. N-acetyllactosamine 152-171 galectin 1 Homo sapiens 34-52 17574526-4 2008 SPR imaging of an array of 40 sialylated and unsialylated glycans established the binding preference of hSiglec7 for alpha2-8-linked disialic acid structures over alpha2-6-sialyl-LacNAcs, which in turn were recognized and bound with greater affinity than alpha2-3-sialyl-LacNAcs. N-acetyllactosamine 179-186 sepiapterin reductase Homo sapiens 0-3 17574526-4 2008 SPR imaging of an array of 40 sialylated and unsialylated glycans established the binding preference of hSiglec7 for alpha2-8-linked disialic acid structures over alpha2-6-sialyl-LacNAcs, which in turn were recognized and bound with greater affinity than alpha2-3-sialyl-LacNAcs. N-acetyllactosamine 179-186 sialic acid binding Ig like lectin 7 Homo sapiens 104-112 17574526-4 2008 SPR imaging of an array of 40 sialylated and unsialylated glycans established the binding preference of hSiglec7 for alpha2-8-linked disialic acid structures over alpha2-6-sialyl-LacNAcs, which in turn were recognized and bound with greater affinity than alpha2-3-sialyl-LacNAcs. N-acetyllactosamine 271-278 sepiapterin reductase Homo sapiens 0-3 17574526-4 2008 SPR imaging of an array of 40 sialylated and unsialylated glycans established the binding preference of hSiglec7 for alpha2-8-linked disialic acid structures over alpha2-6-sialyl-LacNAcs, which in turn were recognized and bound with greater affinity than alpha2-3-sialyl-LacNAcs. N-acetyllactosamine 271-278 sialic acid binding Ig like lectin 7 Homo sapiens 104-112 17574526-4 2008 SPR imaging of an array of 40 sialylated and unsialylated glycans established the binding preference of hSiglec7 for alpha2-8-linked disialic acid structures over alpha2-6-sialyl-LacNAcs, which in turn were recognized and bound with greater affinity than alpha2-3-sialyl-LacNAcs. N-acetyllactosamine 271-278 immunoglobulin binding protein 1 Homo sapiens 117-125 17574526-4 2008 SPR imaging of an array of 40 sialylated and unsialylated glycans established the binding preference of hSiglec7 for alpha2-8-linked disialic acid structures over alpha2-6-sialyl-LacNAcs, which in turn were recognized and bound with greater affinity than alpha2-3-sialyl-LacNAcs. N-acetyllactosamine 271-278 immunoglobulin binding protein 1 Homo sapiens 163-171 18056365-9 2007 Interestingly, the binding of the LacNAc-specific lectins galectin-3 and -8 increased during maturation and up-regulation of sialic acid expression by mDC correlated with an increased binding of siglec-1, -2, and -7. N-acetyllactosamine 34-40 sialic acid binding Ig like lectin 1 Homo sapiens 195-215 17705309-2 2007 N-Acetyllactosamine [Galbeta(1-->4)GlcNAc; LacNAc] oxazoline derivatives with sulfate groups at the C-6 (1 a) and both the C-6 and the C-6" (1 b) were prepared as transition-state analogue substrate monomers for KSase II. N-acetyllactosamine 0-19 complement C6 Homo sapiens 103-106 17724458-3 2007 Genetically modified pigs have been established that have no functional alpha1,3-galactosyltransferase (alpha1,3GT), which transfers alphaGal to N-acetyllactosamine (LacNAc) type oligosaccharides. N-acetyllactosamine 145-164 N-acetyllactosaminide alpha-1,3-galactosyltransferase Sus scrofa 72-102 17724458-3 2007 Genetically modified pigs have been established that have no functional alpha1,3-galactosyltransferase (alpha1,3GT), which transfers alphaGal to N-acetyllactosamine (LacNAc) type oligosaccharides. N-acetyllactosamine 145-164 N-acetyllactosaminide alpha-1,3-galactosyltransferase Sus scrofa 104-114 17724458-3 2007 Genetically modified pigs have been established that have no functional alpha1,3-galactosyltransferase (alpha1,3GT), which transfers alphaGal to N-acetyllactosamine (LacNAc) type oligosaccharides. N-acetyllactosamine 166-172 N-acetyllactosaminide alpha-1,3-galactosyltransferase Sus scrofa 72-102 17724458-3 2007 Genetically modified pigs have been established that have no functional alpha1,3-galactosyltransferase (alpha1,3GT), which transfers alphaGal to N-acetyllactosamine (LacNAc) type oligosaccharides. N-acetyllactosamine 166-172 N-acetyllactosaminide alpha-1,3-galactosyltransferase Sus scrofa 104-114 17690104-5 2007 These glycosyltransferases produced only short, elongated carbohydrates when they were reacted with substrate in the absence of a carbohydrate sulfotransferase; however, they produced extended GlcNAc-sulfated poly-N-acetyllactosamine structures with more than four repeats of the GlcNAc-sulfated N-acetyllactosamine unit in the presence of corneal N-acetylglucosamine 6-O sulfotransferase (CGn6ST). N-acetyllactosamine 214-233 carbohydrate sulfotransferase 6 Homo sapiens 340-388 17690104-5 2007 These glycosyltransferases produced only short, elongated carbohydrates when they were reacted with substrate in the absence of a carbohydrate sulfotransferase; however, they produced extended GlcNAc-sulfated poly-N-acetyllactosamine structures with more than four repeats of the GlcNAc-sulfated N-acetyllactosamine unit in the presence of corneal N-acetylglucosamine 6-O sulfotransferase (CGn6ST). N-acetyllactosamine 214-233 carbohydrate sulfotransferase 6 Homo sapiens 390-396 18049121-13 2007 The alpha1,3-galactosyltransferase acceptor, N-acetyllactosamine determinant, was not increased in GalT-KO tissues. N-acetyllactosamine 45-64 N-acetyllactosaminide alpha-1,3-galactosyltransferase Sus scrofa 4-34 17728258-2 2007 Here we propose that the alpha2-6-sialylated and 6-GlcNAc-sulfated determinant serves as a preferred ligand for CD22 because the binding of a human B-cell line to CD22 was almost completely abrogated after incubating the cells with NaClO3, an inhibitor of cellular sulfate metabolism, and was also significantly inhibited by a newly generated monoclonal antibody specific to the alpha2-6-sialylated 6-sulfo-N-acetyllactosamine (LacNAc) determinant (KN343, murine IgM). N-acetyllactosamine 428-434 CD22 molecule Homo sapiens 112-116 17728258-2 2007 Here we propose that the alpha2-6-sialylated and 6-GlcNAc-sulfated determinant serves as a preferred ligand for CD22 because the binding of a human B-cell line to CD22 was almost completely abrogated after incubating the cells with NaClO3, an inhibitor of cellular sulfate metabolism, and was also significantly inhibited by a newly generated monoclonal antibody specific to the alpha2-6-sialylated 6-sulfo-N-acetyllactosamine (LacNAc) determinant (KN343, murine IgM). N-acetyllactosamine 428-434 CD22 molecule Homo sapiens 163-167 17978468-5 2007 Although both lectin domains have an affinity for N-acetyllactosamine (Galbeta1-4GlcNAc)-containing, N-linked, complex-type sugar chains, the N-terminal lectin domain of LEC-1 recognizes blood group A saccharide (GalNAcalpha1-3(Fucalpha1-2)Galbeta1-3GlcNAc), whereas this saccharide is only poorly recognized by the C-terminal domain. N-acetyllactosamine 50-69 32 kDa beta-galactoside-binding lectin;Galectin Caenorhabditis elegans 170-175 17705309-2 2007 N-Acetyllactosamine [Galbeta(1-->4)GlcNAc; LacNAc] oxazoline derivatives with sulfate groups at the C-6 (1 a) and both the C-6 and the C-6" (1 b) were prepared as transition-state analogue substrate monomers for KSase II. N-acetyllactosamine 0-19 complement C6 Homo sapiens 126-129 17705309-2 2007 N-Acetyllactosamine [Galbeta(1-->4)GlcNAc; LacNAc] oxazoline derivatives with sulfate groups at the C-6 (1 a) and both the C-6 and the C-6" (1 b) were prepared as transition-state analogue substrate monomers for KSase II. N-acetyllactosamine 0-19 C-X9-C motif containing 4 Homo sapiens 138-147 17705309-2 2007 N-Acetyllactosamine [Galbeta(1-->4)GlcNAc; LacNAc] oxazoline derivatives with sulfate groups at the C-6 (1 a) and both the C-6 and the C-6" (1 b) were prepared as transition-state analogue substrate monomers for KSase II. N-acetyllactosamine 46-52 complement C6 Homo sapiens 103-106 17705309-2 2007 N-Acetyllactosamine [Galbeta(1-->4)GlcNAc; LacNAc] oxazoline derivatives with sulfate groups at the C-6 (1 a) and both the C-6 and the C-6" (1 b) were prepared as transition-state analogue substrate monomers for KSase II. N-acetyllactosamine 46-52 complement C6 Homo sapiens 126-129 17705309-2 2007 N-Acetyllactosamine [Galbeta(1-->4)GlcNAc; LacNAc] oxazoline derivatives with sulfate groups at the C-6 (1 a) and both the C-6 and the C-6" (1 b) were prepared as transition-state analogue substrate monomers for KSase II. N-acetyllactosamine 46-52 C-X9-C motif containing 4 Homo sapiens 138-147 17408600-0 2007 The conformation of the C-glycosyl analogue of N-acetyl-lactosamine in the free state and bound to a toxic plant agglutinin and human adhesion/growth-regulatory galectin-1. N-acetyllactosamine 47-67 galectin 1 Homo sapiens 161-171 17408600-4 2007 Due to its conspicuous role in the regulation of adhesion, growth and tissue invasion of tumors and its avid binding to N-acetyl-lactosamine human, galectin-1 was tested as a receptor. N-acetyllactosamine 120-140 galectin 1 Homo sapiens 148-158 16774908-0 2006 Novel carbohydrate-binding activity of bovine liver beta-glucuronidase toward lactose/N-acetyllactosamine sequences. N-acetyllactosamine 86-105 beta-glucuronidase Bos taurus 52-70 16990264-8 2006 The galectin-9 NCRD can bind both N-acetyllactosamine (Galbeta1-4GlcNAc) and T-antigen (Galbeta1-3GalNAc) with the proper location of Arg-64. N-acetyllactosamine 34-53 lectin, galactose binding, soluble 9 Mus musculus 4-14 16990264-9 2006 Moreover, the structure of the N-acetyllactosamine dimer (Galbeta1-4GlcNAcbeta1-3Galbeta1-4GlcNAc) complex shows a unique binding mode of galectin-9. N-acetyllactosamine 31-50 lectin, galactose binding, soluble 9 Mus musculus 138-148 17054948-4 2006 Furthermore, expression of 2,3-sialylated N-acetyllactosamine increased gradually up to 48 h after IL-1 beta stimulation; this preceded the increase in sLeX expression. N-acetyllactosamine 42-61 interleukin 1 beta Homo sapiens 99-108 17587801-7 2007 All species had plentiful N-acetyl lactosamine sequences; at chain termini, binding to Galbeta1,4GlcNAc and Galbeta1,3GalNAc sequences was greatly enhanced after neuraminidase treatment. N-acetyllactosamine 26-46 neuraminidase 1 Homo sapiens 162-175 17279605-4 2007 The proposed approach was tested with two synthetic O-glycopeptides binding a sialyl Lewis x (sLe(x)) oligosaccharide and a 3"-sialyl N-acetyllactosamine (3"-SLN) on a serine (S) residue. N-acetyllactosamine 134-153 sarcolipin Homo sapiens 158-161 16774908-8 2006 Binding studies with biotinyl glycoproteins, lipids, and synthetic sugar probes revealed that beta-glucuronidase binds to N-acetyllactosamine/lactose-containing glycoconjugates at neutral pH. N-acetyllactosamine 122-141 beta-glucuronidase Bos taurus 94-112 16774908-9 2006 The results indicated the presence of N-acetyllactosamine/lactose-binding activity in BLG and provided an effective purification method utilizing the novel carbohydrate binding activity. N-acetyllactosamine 38-57 beta-lactoglobulin Bos taurus 86-89 16269626-4 2006 Significantly, PP14 reacts with N-acetyllactosamine (LacNAc) as was also found for members of the galectin family, such as the potent immunoregulatory protein, galectin-1. N-acetyllactosamine 32-51 progestagen associated endometrial protein Homo sapiens 15-19 16925668-8 2006 Exposing NAcLac on laminin, by alpha-galactosidase treatment, resulted in a significant increase in NKRP1A binding. N-acetyllactosamine 9-15 killer cell lectin like receptor B1 Homo sapiens 100-106 16687583-4 2006 LacNAc-BSA also effectively inhibited LA of the bfpF mutant EPEC. N-acetyllactosamine 0-6 Nucleotide binding protein Escherichia coli 48-52 16687583-7 2006 This observation indicated that either the major BFP structural subunit (BfpA) itself or, possibly, an accessory protein co-assembled with BfpA into the BFP filaments, contains a LacNAc-specific EPEC adhesin. N-acetyllactosamine 179-185 Major pilin structural unit bundlin Escherichia coli 73-77 16687583-7 2006 This observation indicated that either the major BFP structural subunit (BfpA) itself or, possibly, an accessory protein co-assembled with BfpA into the BFP filaments, contains a LacNAc-specific EPEC adhesin. N-acetyllactosamine 179-185 Major pilin structural unit bundlin Escherichia coli 139-143 16516177-2 2006 Further, the regioselective transfer of sulfate to an N-acetyllactosamine derivative could be realised with soluble chimeric GP3ST, also in combination with Lac transglycosylation by means of beta-galactosidase. N-acetyllactosamine 54-73 galactose-3-O-sulfotransferase 2 Homo sapiens 125-130 16516177-2 2006 Further, the regioselective transfer of sulfate to an N-acetyllactosamine derivative could be realised with soluble chimeric GP3ST, also in combination with Lac transglycosylation by means of beta-galactosidase. N-acetyllactosamine 54-73 galactosidase beta 1 Homo sapiens 192-210 16269626-4 2006 Significantly, PP14 reacts with N-acetyllactosamine (LacNAc) as was also found for members of the galectin family, such as the potent immunoregulatory protein, galectin-1. N-acetyllactosamine 53-59 progestagen associated endometrial protein Homo sapiens 15-19 16242339-3 2006 In particular, good inhibitors were discovered against galectin-7 and 9N (K(d) 23 and 47 microM, respectively, for a 3-pyridylmethylthiourea derivative), which represents more than an order of magnitude affinity enhancement over the parent natural N-acetyllactosamine. N-acetyllactosamine 248-267 galectin 7 Homo sapiens 55-72 15728736-2 2005 Here, the proinflammatory cytokine, TNF-alpha, induced the expression of 6-sulfo N-acetyllactosamine (LacNAc)/Lewis x on human peripheral blood monocytes (PBM). N-acetyllactosamine 102-108 tumor necrosis factor Homo sapiens 36-45 15963723-2 2005 The 3-(1H-[1,2,3]-triazol-1-yl)-1-thio-galactoside collection synthesized contained inhibitors of the tumor- and inflammation-related galectin-3 with Kd values as low as 107 microM, which is as potent as the natural disaccharide inhibitors lactose and N-acetyllactosamine. N-acetyllactosamine 252-271 galectin 3 Homo sapiens 134-144 15761024-10 2005 The oligosaccharide specificity pattern of xgalectin-VIIa was similar to that of the human homolog galectin-3, and it was also shown that the N-acetyllactosamine type, biantennary N-glycans exhibit high affinity for xgalectin-VIIa (Kd = 11 microM). N-acetyllactosamine 142-161 galectin 3 Homo sapiens 99-109 15556936-0 2005 Dimeric galectin-1 binds with high affinity to alpha2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans. N-acetyllactosamine 95-114 galectin 1 Homo sapiens 8-18 15862866-3 2005 In enzyme linked lectin assay and hemagglutination inhibition assay, human IgA1, bovine fetuin and other O-glycosylated T antigen-bearing glycoproteins bound to the lectin efficiently in contrast to single N-acetyl lactosamine (LacNAc)-bearing N-linked oligosaccharides released from them and to IgG which is not O-glycosylated. N-acetyllactosamine 206-226 immunoglobulin heavy constant alpha 1 Homo sapiens 75-79 15862866-3 2005 In enzyme linked lectin assay and hemagglutination inhibition assay, human IgA1, bovine fetuin and other O-glycosylated T antigen-bearing glycoproteins bound to the lectin efficiently in contrast to single N-acetyl lactosamine (LacNAc)-bearing N-linked oligosaccharides released from them and to IgG which is not O-glycosylated. N-acetyllactosamine 228-234 immunoglobulin heavy constant alpha 1 Homo sapiens 75-79 16033063-1 2005 Galectin-1 (gal-1), a member of the mammalian beta-galactoside-binding proteins, preferentially recognizes Galbeta1-4GlcNAc (LacNAc) sequences of oligosaccharides associated with several cell surface glycoconjugates. N-acetyllactosamine 125-131 galectin 1 Homo sapiens 0-10 16033063-1 2005 Galectin-1 (gal-1), a member of the mammalian beta-galactoside-binding proteins, preferentially recognizes Galbeta1-4GlcNAc (LacNAc) sequences of oligosaccharides associated with several cell surface glycoconjugates. N-acetyllactosamine 125-131 galectin 1 Homo sapiens 12-17 15701008-3 2005 Based on these structures, synthesis of second generation LacNAc derivatives carrying aromatic amides at 3"-C, followed by screening with a novel fluorescence polarization assay, has led to the identification of inhibitors with further enhanced affinity for galectin-3 (K(d) > or = 320 nM). N-acetyllactosamine 58-64 galectin 3 Homo sapiens 258-268 15470230-7 2005 Furthermore, acceptor specificity analysis involving various oligosaccarides revealed that GlcAT-P specifically recognized N-acetyllactosamine (Galbeta1-4GlcNAc) at the nonreducing terminals of acceptor substrates. N-acetyllactosamine 123-142 beta-1,3-glucuronyltransferase 1 Homo sapiens 91-98 16319516-2 2005 METHODS: ST6Gal I activity was determined in healthy, transitional and tumor tissues from the same patient using asialotransferrin and N-acetyllactosamine as acceptors. N-acetyllactosamine 135-154 ST6 beta-galactoside alpha-2,6-sialyltransferase 1 Homo sapiens 9-17 16319516-5 2005 A positive correlation was found between ST6Gal I activity with N-acetyllactosamine and asialotransferrin in healthy (n = 32), tumorous (n = 32) and transitional tissue (n = 27), supporting the fact that the same enzyme was detected using both acceptors. N-acetyllactosamine 64-83 ST6 beta-galactoside alpha-2,6-sialyltransferase 1 Homo sapiens 41-49