PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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	163-167
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
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
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
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
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
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
17408600-4	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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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	12-17
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
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
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
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
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
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
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
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	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
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
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
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
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
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
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
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	117-147
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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	muscle associated receptor tyrosine kinase	Homo sapiens	90-94
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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	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	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	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
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
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	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	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	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	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	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	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	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
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
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
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
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
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
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
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
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
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
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	41-46
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
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
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
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
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
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
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
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
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
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
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	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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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	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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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