PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
8664259-4	1996	Instead, the results show a very small shift (1.3 ppm), indicating that C-6 of 2"-deoxyinosine retains its sp2 hybridization after binding by calf intestinal adenosine deaminase.	deoxyinosine	79-94	complement C6	Bos taurus	72-75
8033884-6	1994	Hydrogen-bonding interactions are almost exclusively restricted to the other side of the molecule: the C-4" and C-6" hydroxyl groups act as donors of the strongest hydrogen bonds to charged groups of the lectin, while the C-3 hydroxyl group participates in a strong hydrogen bond with a neutral group.	Hydrogen	0-8	complement C6	Bos taurus	112-115
8033884-6	1994	Hydrogen-bonding interactions are almost exclusively restricted to the other side of the molecule: the C-4" and C-6" hydroxyl groups act as donors of the strongest hydrogen bonds to charged groups of the lectin, while the C-3 hydroxyl group participates in a strong hydrogen bond with a neutral group.	Hydrogen	164-172	complement C6	Bos taurus	112-115
8033884-6	1994	Hydrogen-bonding interactions are almost exclusively restricted to the other side of the molecule: the C-4" and C-6" hydroxyl groups act as donors of the strongest hydrogen bonds to charged groups of the lectin, while the C-3 hydroxyl group participates in a strong hydrogen bond with a neutral group.	Hydroxyl Radical	117-125	complement C6	Bos taurus	112-115
8033884-6	1994	Hydrogen-bonding interactions are almost exclusively restricted to the other side of the molecule: the C-4" and C-6" hydroxyl groups act as donors of the strongest hydrogen bonds to charged groups of the lectin, while the C-3 hydroxyl group participates in a strong hydrogen bond with a neutral group.	Hydrogen	266-274	complement C6	Bos taurus	112-115
3456754-3	1986	The enzyme transfers sulfate groups from [35S]phosphoadenylylsulfate exclusively to C-6 OH groups of N-acetylgalactosamine units of the acceptor substrates.	Sulfates	21-28	complement C6	Bos taurus	84-87
3624221-5	1987	The 1H and 13C nuclear magnetic resonance data indicated that imidazole C-2 of histidine is linked to C-6 of norleucine (epsilon-deaminated lysine residue) which in turn is linked to the C-6 amino group of hydroxylysine.	Hydrogen	4-6	complement C6	Bos taurus	102-105
3624221-5	1987	The 1H and 13C nuclear magnetic resonance data indicated that imidazole C-2 of histidine is linked to C-6 of norleucine (epsilon-deaminated lysine residue) which in turn is linked to the C-6 amino group of hydroxylysine.	Hydrogen	4-6	complement C6	Bos taurus	187-190
3624221-5	1987	The 1H and 13C nuclear magnetic resonance data indicated that imidazole C-2 of histidine is linked to C-6 of norleucine (epsilon-deaminated lysine residue) which in turn is linked to the C-6 amino group of hydroxylysine.	13c	11-14	complement C6	Bos taurus	102-105
3624221-5	1987	The 1H and 13C nuclear magnetic resonance data indicated that imidazole C-2 of histidine is linked to C-6 of norleucine (epsilon-deaminated lysine residue) which in turn is linked to the C-6 amino group of hydroxylysine.	13c	11-14	complement C6	Bos taurus	187-190
3624221-5	1987	The 1H and 13C nuclear magnetic resonance data indicated that imidazole C-2 of histidine is linked to C-6 of norleucine (epsilon-deaminated lysine residue) which in turn is linked to the C-6 amino group of hydroxylysine.	imidazole	62-71	complement C6	Bos taurus	102-105
3624221-5	1987	The 1H and 13C nuclear magnetic resonance data indicated that imidazole C-2 of histidine is linked to C-6 of norleucine (epsilon-deaminated lysine residue) which in turn is linked to the C-6 amino group of hydroxylysine.	imidazole	62-71	complement C6	Bos taurus	187-190
3624221-5	1987	The 1H and 13C nuclear magnetic resonance data indicated that imidazole C-2 of histidine is linked to C-6 of norleucine (epsilon-deaminated lysine residue) which in turn is linked to the C-6 amino group of hydroxylysine.	Histidine	79-88	complement C6	Bos taurus	102-105
3624221-5	1987	The 1H and 13C nuclear magnetic resonance data indicated that imidazole C-2 of histidine is linked to C-6 of norleucine (epsilon-deaminated lysine residue) which in turn is linked to the C-6 amino group of hydroxylysine.	Histidine	79-88	complement C6	Bos taurus	187-190
3624221-5	1987	The 1H and 13C nuclear magnetic resonance data indicated that imidazole C-2 of histidine is linked to C-6 of norleucine (epsilon-deaminated lysine residue) which in turn is linked to the C-6 amino group of hydroxylysine.	Norleucine	109-119	complement C6	Bos taurus	102-105
3624221-5	1987	The 1H and 13C nuclear magnetic resonance data indicated that imidazole C-2 of histidine is linked to C-6 of norleucine (epsilon-deaminated lysine residue) which in turn is linked to the C-6 amino group of hydroxylysine.	Norleucine	109-119	complement C6	Bos taurus	187-190
3624221-5	1987	The 1H and 13C nuclear magnetic resonance data indicated that imidazole C-2 of histidine is linked to C-6 of norleucine (epsilon-deaminated lysine residue) which in turn is linked to the C-6 amino group of hydroxylysine.	Lysine	140-146	complement C6	Bos taurus	102-105
3624221-5	1987	The 1H and 13C nuclear magnetic resonance data indicated that imidazole C-2 of histidine is linked to C-6 of norleucine (epsilon-deaminated lysine residue) which in turn is linked to the C-6 amino group of hydroxylysine.	Lysine	140-146	complement C6	Bos taurus	187-190
3624221-5	1987	The 1H and 13C nuclear magnetic resonance data indicated that imidazole C-2 of histidine is linked to C-6 of norleucine (epsilon-deaminated lysine residue) which in turn is linked to the C-6 amino group of hydroxylysine.	Hydroxylysine	206-219	complement C6	Bos taurus	102-105
3624221-5	1987	The 1H and 13C nuclear magnetic resonance data indicated that imidazole C-2 of histidine is linked to C-6 of norleucine (epsilon-deaminated lysine residue) which in turn is linked to the C-6 amino group of hydroxylysine.	Hydroxylysine	206-219	complement C6	Bos taurus	187-190
2322563-4	1990	The results indicate that there is no protonation at N-5 in the binary complexes, and this was confirmed by 13C NMR studies with folate and dihydrofolate synthesized with 13C enrichment at C-6.	13c	171-174	complement C6	Bos taurus	189-192
3456754-3	1986	The enzyme transfers sulfate groups from [35S]phosphoadenylylsulfate exclusively to C-6 OH groups of N-acetylgalactosamine units of the acceptor substrates.	Sulfur-35	42-45	complement C6	Bos taurus	84-87
3456754-3	1986	The enzyme transfers sulfate groups from [35S]phosphoadenylylsulfate exclusively to C-6 OH groups of N-acetylgalactosamine units of the acceptor substrates.	phosphoadenylylsulfate	46-68	complement C6	Bos taurus	84-87
3456754-3	1986	The enzyme transfers sulfate groups from [35S]phosphoadenylylsulfate exclusively to C-6 OH groups of N-acetylgalactosamine units of the acceptor substrates.	Acetylgalactosamine	101-122	complement C6	Bos taurus	84-87
6224480-6	1983	spectrum of the tetrasaccharide (m = 1) shows that, whereas the extent of C-6 O-sulphation in the GlcNAc is approx.	tetrasaccharide	16-31	complement C6	Bos taurus	74-77
2985582-0	1985	The C-6 proton of tetrahydrobiopterin is acquired from water, not NADPH, during de novo biosynthesis.	sapropterin	18-37	complement C6	Bos taurus	4-7
2985582-0	1985	The C-6 proton of tetrahydrobiopterin is acquired from water, not NADPH, during de novo biosynthesis.	Water	55-60	complement C6	Bos taurus	4-7
2985582-3	1985	Tetrahydrobiopterin can be oxidized under conditions which yield pterin or pterin 6-carboxylate without exchange of the C-6 and C-7 protons.	sapropterin	0-19	complement C6	Bos taurus	120-123
2985582-3	1985	Tetrahydrobiopterin can be oxidized under conditions which yield pterin or pterin 6-carboxylate without exchange of the C-6 and C-7 protons.	Pterins	13-19	complement C6	Bos taurus	120-123
2985582-4	1985	Using these techniques, a gas chromatography/mass spectrometry method was developed to determine that in the biosynthesis of tetrahydrobiopterin de novo, in preparations of bovine adrenal medulla, the C-6 proton of tetrahydrobiopterin is derived from water and not from NADPH.	sapropterin	125-144	complement C6	Bos taurus	201-204
2985582-4	1985	Using these techniques, a gas chromatography/mass spectrometry method was developed to determine that in the biosynthesis of tetrahydrobiopterin de novo, in preparations of bovine adrenal medulla, the C-6 proton of tetrahydrobiopterin is derived from water and not from NADPH.	sapropterin	215-234	complement C6	Bos taurus	201-204
2985582-4	1985	Using these techniques, a gas chromatography/mass spectrometry method was developed to determine that in the biosynthesis of tetrahydrobiopterin de novo, in preparations of bovine adrenal medulla, the C-6 proton of tetrahydrobiopterin is derived from water and not from NADPH.	Water	251-256	complement C6	Bos taurus	201-204
2985582-4	1985	Using these techniques, a gas chromatography/mass spectrometry method was developed to determine that in the biosynthesis of tetrahydrobiopterin de novo, in preparations of bovine adrenal medulla, the C-6 proton of tetrahydrobiopterin is derived from water and not from NADPH.	NADP	270-275	complement C6	Bos taurus	201-204
2985582-5	1985	In contrast, the C-6 proton of tetrahydrobiopterin produced from sepiapterin (6-lactoyl-7,8-dihydropterin) comes from NADPH.	sapropterin	31-50	complement C6	Bos taurus	17-20
2985582-5	1985	In contrast, the C-6 proton of tetrahydrobiopterin produced from sepiapterin (6-lactoyl-7,8-dihydropterin) comes from NADPH.	sepiapterin	65-76	complement C6	Bos taurus	17-20
2985582-5	1985	In contrast, the C-6 proton of tetrahydrobiopterin produced from sepiapterin (6-lactoyl-7,8-dihydropterin) comes from NADPH.	sepiapterin	78-105	complement C6	Bos taurus	17-20
2985582-5	1985	In contrast, the C-6 proton of tetrahydrobiopterin produced from sepiapterin (6-lactoyl-7,8-dihydropterin) comes from NADPH.	NADP	118-123	complement C6	Bos taurus	17-20
2982838-3	1985	Distances between enzyme-bound Mn2+ and the phosphorus atoms at C-6 of fructose-6-P and alpha-methyl-D-fructofuranoside 1,6-bisphosphate were identical, and the enzyme-Mn to phosphorus distance determined for the C-6 phosphorus atom of Fru-2,6-P2 was very similar to these values.	Manganese(2+)	31-35	complement C6	Bos taurus	64-67
2982838-3	1985	Distances between enzyme-bound Mn2+ and the phosphorus atoms at C-6 of fructose-6-P and alpha-methyl-D-fructofuranoside 1,6-bisphosphate were identical, and the enzyme-Mn to phosphorus distance determined for the C-6 phosphorus atom of Fru-2,6-P2 was very similar to these values.	Phosphorus	44-54	complement C6	Bos taurus	64-67
6592165-5	1984	Sixty per cent of the sulfate ester groups formed by sulfotransferase I were linked to the C-6 atom of galactosyl residues, the other ones to the C-6 atom of N-acetylglucosamine.	sulfate ester	22-35	complement C6	Bos taurus	91-94
6592165-5	1984	Sixty per cent of the sulfate ester groups formed by sulfotransferase I were linked to the C-6 atom of galactosyl residues, the other ones to the C-6 atom of N-acetylglucosamine.	sulfate ester	22-35	complement C6	Bos taurus	146-149
6592165-5	1984	Sixty per cent of the sulfate ester groups formed by sulfotransferase I were linked to the C-6 atom of galactosyl residues, the other ones to the C-6 atom of N-acetylglucosamine.	Acetylglucosamine	158-177	complement C6	Bos taurus	146-149
6466706-0	1984	Evidence for the occurrence of oligosaccharides from bovine glycophorin having a branching point at C-6 of N-acetylgalactosamine.	Oligosaccharides	31-47	complement C6	Bos taurus	100-103
6466706-0	1984	Evidence for the occurrence of oligosaccharides from bovine glycophorin having a branching point at C-6 of N-acetylgalactosamine.	Acetylgalactosamine	107-128	complement C6	Bos taurus	100-103
6466706-3	1984	The occurrence of N-acetylglucosamine residue attached to C-6 of the reducing terminal N-acetylgalactosaminitol was demonstrated by isolating the disaccharide, GlcNAc(1----6)GalNAcol.	Acetylglucosamine	18-37	complement C6	Bos taurus	58-61
6466706-3	1984	The occurrence of N-acetylglucosamine residue attached to C-6 of the reducing terminal N-acetylgalactosaminitol was demonstrated by isolating the disaccharide, GlcNAc(1----6)GalNAcol.	N-acetylgalactosaminitol	87-111	complement C6	Bos taurus	58-61
6466706-3	1984	The occurrence of N-acetylglucosamine residue attached to C-6 of the reducing terminal N-acetylgalactosaminitol was demonstrated by isolating the disaccharide, GlcNAc(1----6)GalNAcol.	Disaccharides	146-158	complement C6	Bos taurus	58-61
6466706-3	1984	The occurrence of N-acetylglucosamine residue attached to C-6 of the reducing terminal N-acetylgalactosaminitol was demonstrated by isolating the disaccharide, GlcNAc(1----6)GalNAcol.	Acetylglucosamine	160-166	complement C6	Bos taurus	58-61
6466706-3	1984	The occurrence of N-acetylglucosamine residue attached to C-6 of the reducing terminal N-acetylgalactosaminitol was demonstrated by isolating the disaccharide, GlcNAc(1----6)GalNAcol.	1----6)galnacol	167-182	complement C6	Bos taurus	58-61
6224480-6	1983	spectrum of the tetrasaccharide (m = 1) shows that, whereas the extent of C-6 O-sulphation in the GlcNAc is approx.	Acetylglucosamine	98-104	complement C6	Bos taurus	74-77
6224480-9	1983	In the higher oligosaccharides (m = 2-5) the gross extent of C-6 O-sulphation of GlcNAc residues falls systematically with increasing oligosaccharide size, whereas that in the aManOH residues remains below 10%.	Oligosaccharides	14-30	complement C6	Bos taurus	61-64
6224480-9	1983	In the higher oligosaccharides (m = 2-5) the gross extent of C-6 O-sulphation of GlcNAc residues falls systematically with increasing oligosaccharide size, whereas that in the aManOH residues remains below 10%.	Acetylglucosamine	81-87	complement C6	Bos taurus	61-64
6224480-9	1983	In the higher oligosaccharides (m = 2-5) the gross extent of C-6 O-sulphation of GlcNAc residues falls systematically with increasing oligosaccharide size, whereas that in the aManOH residues remains below 10%.	Oligosaccharides	14-29	complement C6	Bos taurus	61-64
6224480-10	1983	There is also evidence that the C-6 O-sulphation of the GlcNAc residues is confined to the GlcNAc residue adjacent to the non-reducing terminal uronic acid residue.	Acetylglucosamine	56-62	complement C6	Bos taurus	32-35
6224480-10	1983	There is also evidence that the C-6 O-sulphation of the GlcNAc residues is confined to the GlcNAc residue adjacent to the non-reducing terminal uronic acid residue.	Acetylglucosamine	91-97	complement C6	Bos taurus	32-35
6224480-10	1983	There is also evidence that the C-6 O-sulphation of the GlcNAc residues is confined to the GlcNAc residue adjacent to the non-reducing terminal uronic acid residue.	Uronic Acids	144-155	complement C6	Bos taurus	32-35
6224480-12	1983	It is concluded that in the low-sulphated heparan sulphates GlcNSO3 residues that do not occur in (GlcNSO3-UA-)n blocks tend to have a significantly smaller extent of C-6 O-sulphation than do GlcNAc residues that occur in -GlcNSO3-UA-GlcNAc-GlcUA-GlcNSO3-sequences.	Heparitin Sulfate	42-59	complement C6	Bos taurus	167-170
6224480-12	1983	It is concluded that in the low-sulphated heparan sulphates GlcNSO3 residues that do not occur in (GlcNSO3-UA-)n blocks tend to have a significantly smaller extent of C-6 O-sulphation than do GlcNAc residues that occur in -GlcNSO3-UA-GlcNAc-GlcUA-GlcNSO3-sequences.	glcnso3	60-67	complement C6	Bos taurus	167-170
6224480-12	1983	It is concluded that in the low-sulphated heparan sulphates GlcNSO3 residues that do not occur in (GlcNSO3-UA-)n blocks tend to have a significantly smaller extent of C-6 O-sulphation than do GlcNAc residues that occur in -GlcNSO3-UA-GlcNAc-GlcUA-GlcNSO3-sequences.	Acetylglucosamine	192-198	complement C6	Bos taurus	167-170
6224480-12	1983	It is concluded that in the low-sulphated heparan sulphates GlcNSO3 residues that do not occur in (GlcNSO3-UA-)n blocks tend to have a significantly smaller extent of C-6 O-sulphation than do GlcNAc residues that occur in -GlcNSO3-UA-GlcNAc-GlcUA-GlcNSO3-sequences.	Acetylglucosamine	234-240	complement C6	Bos taurus	167-170
486504-10	1979	These observations can be explained by assuming that for attack at C-6, the enzyme must bind both to N-1 and N-2 in the pyrazole ring and causes tautomerisation, which places a double bond at position 5,6 in the pyrimidine ring.	pyrazole	120-128	complement C6	Bos taurus	67-70
6613726-3	1983	Tetrahydrofolate, tetrahydropteroyltriglutamate and tetrahydropteroylheptaglutamate, all having the natural configuration at C-6, all showed similar Km values near 15 microM.	5,6,7,8-tetrahydrofolic acid	0-16	complement C6	Bos taurus	125-128
6613726-3	1983	Tetrahydrofolate, tetrahydropteroyltriglutamate and tetrahydropteroylheptaglutamate, all having the natural configuration at C-6, all showed similar Km values near 15 microM.	tetrahydropteroyltriglutamate	18-47	complement C6	Bos taurus	125-128
6613726-3	1983	Tetrahydrofolate, tetrahydropteroyltriglutamate and tetrahydropteroylheptaglutamate, all having the natural configuration at C-6, all showed similar Km values near 15 microM.	tetrahydropteroylheptaglutamate	52-83	complement C6	Bos taurus	125-128
486504-10	1979	These observations can be explained by assuming that for attack at C-6, the enzyme must bind both to N-1 and N-2 in the pyrazole ring and causes tautomerisation, which places a double bond at position 5,6 in the pyrimidine ring.	pyrimidine	212-222	complement C6	Bos taurus	67-70
12825-9	1977	Methylation at C-6 in the pyrazine moiety enhances enzymic attack at C-2 in the pyrimidine ring.	Pyrazines	26-34	complement C6	Bos taurus	15-18
12825-9	1977	Methylation at C-6 in the pyrazine moiety enhances enzymic attack at C-2 in the pyrimidine ring.	pyrimidine	80-90	complement C6	Bos taurus	15-18
4306463-7	1969	Terminal sialic acid residues are attached to galactopyranose residues by 2,3-linkages, and to some N-acetylgalactosamine residues (at C-6).	N-Acetylneuraminic Acid	9-20	complement C6	Bos taurus	135-138
4306463-7	1969	Terminal sialic acid residues are attached to galactopyranose residues by 2,3-linkages, and to some N-acetylgalactosamine residues (at C-6).	Acetylgalactosamine	100-121	complement C6	Bos taurus	135-138
4306463-9	1969	Sequential Smith degradation indicates that N-acetylgalactosamine residues may be present as points of branching (linked in C-1, C-3 and C-6) and N-acetylglucosamine residues are located in the inner part of the structure, adjacent to the carbohydrate-peptide bond(s).	Acetylgalactosamine	44-65	complement C6	Bos taurus	137-140
5862402-15	1965	Therefore it was not possible to use [2-(14)C]glucose and [6-(3)H]glucose in a single experiment to measure the relative conversion of the C-2 and C-6 positions of glucose to glycerol.	Glycerol	175-183	complement C6	Bos taurus	147-150
23084885-11	2013	The most important contributors were found to be ethanol, short-chain fatty acids (C(2) to C(6)), diacetyl, and ethyl hexanoate.	Fatty Acids, Volatile	58-81	complement C6	Bos taurus	91-95
21869949-7	2011	The styrene particles, frequently used as particle size standards, gave unsatisfactory results for our DNA samples as did C-6 derivatized silica and positively charged amino polystyrene microspheres.	Silicon Dioxide	138-144	complement C6	Bos taurus	122-125