PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
2611236-3	1989	The latter two conformers may be distinguished by smaller but still significant differences in the carbon chemical shifts at the C-2" and C-4" positions.	Carbon	99-105	complement C2	Bos taurus	129-132
3410637-2	1988	The titration curves of the C-2 histidine protons of bovine pancreatic ribonuclease A in the presence of several dideoxynucleoside monophosphates (dNpdN) were studied by means of proton nuclear magnetic resonance at 270 MHz in order to obtain information on the ligand--RNase A interaction.	Histidine	32-41	complement C2	Bos taurus	28-31
2765479-3	1989	The secondary deuterium effects at C-2, C-3, and C-4 are 1.12, 1.13, and 1.00 per H, respectively.	Deuterium	14-23	complement C2	Bos taurus	35-43
3410637-2	1988	The titration curves of the C-2 histidine protons of bovine pancreatic ribonuclease A in the presence of several dideoxynucleoside monophosphates (dNpdN) were studied by means of proton nuclear magnetic resonance at 270 MHz in order to obtain information on the ligand--RNase A interaction.	dideoxynucleoside monophosphates	113-145	complement C2	Bos taurus	28-31
3410637-3	1988	The changes in the chemical shift and pKs of the C-2 proton resonances of His-12, -48, -119 in the complexes RNase A--dNpdN were smaller than those previously found when the enzyme interacted with mononucleotides.	Histidine	74-77	complement C2	Bos taurus	49-52
3410637-3	1988	The changes in the chemical shift and pKs of the C-2 proton resonances of His-12, -48, -119 in the complexes RNase A--dNpdN were smaller than those previously found when the enzyme interacted with mononucleotides.	dnpdn	118-123	complement C2	Bos taurus	49-52
3410637-3	1988	The changes in the chemical shift and pKs of the C-2 proton resonances of His-12, -48, -119 in the complexes RNase A--dNpdN were smaller than those previously found when the enzyme interacted with mononucleotides.	mononucleotides	197-212	complement C2	Bos taurus	49-52
3429448-8	1987	An alignment of P-450(11 beta) and P-450(SCC) to give maximum matching showed four highly conserved regions (C-1, C-2, C-3, and C-4).	Carbon	42-43	complement C2	Bos taurus	114-117
3429448-8	1987	An alignment of P-450(11 beta) and P-450(SCC) to give maximum matching showed four highly conserved regions (C-1, C-2, C-3, and C-4).	Carbon	43-44	complement C2	Bos taurus	114-117
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 C2	Bos taurus	72-75
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 C2	Bos taurus	72-75
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 C2	Bos taurus	72-75
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 C2	Bos taurus	72-75
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 C2	Bos taurus	72-75
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 C2	Bos taurus	72-75
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 C2	Bos taurus	72-75
3756304-8	1986	Since the ester compounds do not have hydrogen bond donating groups proximate to the aromatic ring, these results suggest a model for the A-T specificity of these compounds that involves a solvent-mediated hydrogen bond between the C-2 carbonyl of thymine and the carbonyl group of the intercalators.	Esters	10-15	complement C2	Bos taurus	232-235
3310334-4	1987	Approximate molecular weight was determined by the Sephadex gel chromatography to be 1,500 for A-1 and C-2 and 2,000 for C-1.	sephadex	51-59	complement C2	Bos taurus	95-112
3813569-2	1987	One of the histidine C-2 peaks titrated normally, with a pKa value of 6.8, but the other two histidines in this peptide had pKa values of 6.3.	Histidine	11-20	complement C2	Bos taurus	21-24
3098173-0	1986	Mechanism of the glycine cleavage reaction: retention of C-2 hydrogens of glycine on the intermediate attached to H-protein and evidence for the inability of serine hydroxymethyltransferase to catalyze the glycine decarboxylation.	Glycine	17-24	complement C2	Bos taurus	57-60
3098173-0	1986	Mechanism of the glycine cleavage reaction: retention of C-2 hydrogens of glycine on the intermediate attached to H-protein and evidence for the inability of serine hydroxymethyltransferase to catalyze the glycine decarboxylation.	Hydrogen	61-70	complement C2	Bos taurus	57-60
3098173-0	1986	Mechanism of the glycine cleavage reaction: retention of C-2 hydrogens of glycine on the intermediate attached to H-protein and evidence for the inability of serine hydroxymethyltransferase to catalyze the glycine decarboxylation.	Glycine	74-81	complement C2	Bos taurus	57-60
3098173-0	1986	Mechanism of the glycine cleavage reaction: retention of C-2 hydrogens of glycine on the intermediate attached to H-protein and evidence for the inability of serine hydroxymethyltransferase to catalyze the glycine decarboxylation.	Glycine	74-81	complement C2	Bos taurus	57-60
3098173-4	1986	The results presented in this paper indicate that the decarboxylation is not accompanied by the removal of a C-2 hydrogen atom of glycine and instead both C-2 hydrogens are transferred with the alpha carbon atom to the intermediate formed during the decarboxylation of glycine.	Hydrogen	159-168	complement C2	Bos taurus	155-158
3098173-4	1986	The results presented in this paper indicate that the decarboxylation is not accompanied by the removal of a C-2 hydrogen atom of glycine and instead both C-2 hydrogens are transferred with the alpha carbon atom to the intermediate formed during the decarboxylation of glycine.	Carbon	200-206	complement C2	Bos taurus	155-158
3098173-4	1986	The results presented in this paper indicate that the decarboxylation is not accompanied by the removal of a C-2 hydrogen atom of glycine and instead both C-2 hydrogens are transferred with the alpha carbon atom to the intermediate formed during the decarboxylation of glycine.	Glycine	269-276	complement C2	Bos taurus	155-158
3790504-0	1986	Stereochemical probes of bovine plasma amine oxidase: evidence for mirror image processing and a syn abstraction of hydrogens from C-1 and C-2 of dopamine.	Dopamine	146-154	complement C2	Bos taurus	139-142
3790504-2	1986	Analysis of products formed from incubation of dopamine with PAO in tritiated water indicates a stereospecific, pro-R, incorporation of label at C-2.	Dopamine	47-55	complement C2	Bos taurus	145-148
3790504-2	1986	Analysis of products formed from incubation of dopamine with PAO in tritiated water indicates a stereospecific, pro-R, incorporation of label at C-2.	oxophenylarsine	61-64	complement C2	Bos taurus	145-148
3790504-2	1986	Analysis of products formed from incubation of dopamine with PAO in tritiated water indicates a stereospecific, pro-R, incorporation of label at C-2.	Water	78-83	complement C2	Bos taurus	145-148
3790504-6	1986	From previously measured isotope effects, we predict the loss of tritium from the 1(R)-2H and 1(S)-2H samples to be 74:8 for a syn relationship between cleavage at C-1 and C-2 vs. 21:90 for an anti relationship.	Tritium	65-72	complement C2	Bos taurus	164-175
3790504-6	1986	From previously measured isotope effects, we predict the loss of tritium from the 1(R)-2H and 1(S)-2H samples to be 74:8 for a syn relationship between cleavage at C-1 and C-2 vs. 21:90 for an anti relationship.	1(r)-2h	82-89	complement C2	Bos taurus	164-175
3790504-6	1986	From previously measured isotope effects, we predict the loss of tritium from the 1(R)-2H and 1(S)-2H samples to be 74:8 for a syn relationship between cleavage at C-1 and C-2 vs. 21:90 for an anti relationship.	1(s)-2h	94-101	complement C2	Bos taurus	164-175
3790504-8	1986	The data support a mechanism in which a single base catalyzes a 1,3-prototrophic shift of hydrogen from C-1 of the substrate to cofactor, followed by exchange from C-2.	Hydrogen	90-98	complement C2	Bos taurus	164-167
3790504-8	1986	The data support a mechanism in which a single base catalyzes a 1,3-prototrophic shift of hydrogen from C-1 of the substrate to cofactor, followed by exchange from C-2.	Carbon	104-105	complement C2	Bos taurus	164-167
3756304-8	1986	Since the ester compounds do not have hydrogen bond donating groups proximate to the aromatic ring, these results suggest a model for the A-T specificity of these compounds that involves a solvent-mediated hydrogen bond between the C-2 carbonyl of thymine and the carbonyl group of the intercalators.	Hydrogen	206-214	complement C2	Bos taurus	232-235
3756304-8	1986	Since the ester compounds do not have hydrogen bond donating groups proximate to the aromatic ring, these results suggest a model for the A-T specificity of these compounds that involves a solvent-mediated hydrogen bond between the C-2 carbonyl of thymine and the carbonyl group of the intercalators.	Thymine	248-255	complement C2	Bos taurus	232-235
2932448-10	1985	The phosphate ester must be located to C-2 of xylose/xylitol as the 1-3H radioactivity could be released by periodate oxidation when it was preceded by alkaline phosphatase treatment.	phosphate ester	4-19	complement C2	Bos taurus	39-42
2932448-10	1985	The phosphate ester must be located to C-2 of xylose/xylitol as the 1-3H radioactivity could be released by periodate oxidation when it was preceded by alkaline phosphatase treatment.	Xylose	46-52	complement C2	Bos taurus	39-42
2932448-10	1985	The phosphate ester must be located to C-2 of xylose/xylitol as the 1-3H radioactivity could be released by periodate oxidation when it was preceded by alkaline phosphatase treatment.	Xylitol	53-60	complement C2	Bos taurus	39-42
2932448-10	1985	The phosphate ester must be located to C-2 of xylose/xylitol as the 1-3H radioactivity could be released by periodate oxidation when it was preceded by alkaline phosphatase treatment.	Tritium	70-72	complement C2	Bos taurus	39-42
2932448-10	1985	The phosphate ester must be located to C-2 of xylose/xylitol as the 1-3H radioactivity could be released by periodate oxidation when it was preceded by alkaline phosphatase treatment.	metaperiodate	108-117	complement C2	Bos taurus	39-42
2982838-4	1985	Likewise, the enzyme-Mn to phosphorus distances for Pi, the C-1 phosphorus atom of alpha-methyl-D-fructofuranoside 1,6-bisphosphate, and the C-2 phosphorus atom of Fru-2,6-P2 agreed within 0.5 A.	fru-2,6-p2	164-174	complement C2	Bos taurus	141-144
4030788-4	1985	Amino acid compositions, N-terminal sequences, and tryptic peptide maps show that C-1 and C-2 are isozymes of differing primary structure and that the adult form of the enzyme is identical to C-2.	Peptides	59-66	complement C2	Bos taurus	82-93
435461-1	1979	The stereochemistry of the bovine plasma amine oxidase catalyzed oxidation of 2-(3,4-dihydroxyphenyl)-ethylamine (domapine) has been investigated by comparing 3H/14C ratios of 3,4-dibenzyloxyphenethyl alcohols, derived from 3,4-dihydroxyphenylacetaldehydes, to starting dopamines chirally labeled at C-1 and C-2.	domapine	114-122	complement C2	Bos taurus	308-311
6289876-1	1982	The titration curves of the C-2 histidine protons of RNase A and of derivative II--a covalent derivative obtained by reaction of the enzyme with the halogenated nucleotide 9-beta-D-ribofuranosyl-6-chloropurine 5"-phosphate--in the presence of a number of purine nucleosides, nucleoside monophosphates, and nucleoside diphosphates were studied by means of proton nuclear magnetic resonance at 270 MHz.	Histidine	32-41	complement C2	Bos taurus	28-31
6289876-1	1982	The titration curves of the C-2 histidine protons of RNase A and of derivative II--a covalent derivative obtained by reaction of the enzyme with the halogenated nucleotide 9-beta-D-ribofuranosyl-6-chloropurine 5"-phosphate--in the presence of a number of purine nucleosides, nucleoside monophosphates, and nucleoside diphosphates were studied by means of proton nuclear magnetic resonance at 270 MHz.	nucleotide 9-beta-d-ribofuranosyl-6-chloropurine 5"-phosphate	161-222	complement C2	Bos taurus	28-31
6289876-1	1982	The titration curves of the C-2 histidine protons of RNase A and of derivative II--a covalent derivative obtained by reaction of the enzyme with the halogenated nucleotide 9-beta-D-ribofuranosyl-6-chloropurine 5"-phosphate--in the presence of a number of purine nucleosides, nucleoside monophosphates, and nucleoside diphosphates were studied by means of proton nuclear magnetic resonance at 270 MHz.	Purine Nucleosides	255-273	complement C2	Bos taurus	28-31
6289876-1	1982	The titration curves of the C-2 histidine protons of RNase A and of derivative II--a covalent derivative obtained by reaction of the enzyme with the halogenated nucleotide 9-beta-D-ribofuranosyl-6-chloropurine 5"-phosphate--in the presence of a number of purine nucleosides, nucleoside monophosphates, and nucleoside diphosphates were studied by means of proton nuclear magnetic resonance at 270 MHz.	nucleoside monophosphates	275-300	complement C2	Bos taurus	28-31
6289876-1	1982	The titration curves of the C-2 histidine protons of RNase A and of derivative II--a covalent derivative obtained by reaction of the enzyme with the halogenated nucleotide 9-beta-D-ribofuranosyl-6-chloropurine 5"-phosphate--in the presence of a number of purine nucleosides, nucleoside monophosphates, and nucleoside diphosphates were studied by means of proton nuclear magnetic resonance at 270 MHz.	nucleoside diphosphates	306-329	complement C2	Bos taurus	28-31
7263186-2	1981	The major innovations are: 1) precipitation in 2 M ammonium sulfate at pH 7.9 instead of pH 7.0 to obtain the extract designated as C-2 by Reichert and 2) early gel-chromatography on Sephacryl S-200 of the C-2 extract.	sephacryl s	183-194	complement C2	Bos taurus	132-135
3847279-4	1985	After incubation of UTI with this enzyme in various molar ratios, two complexes (C1 and C2) could be visualized in alkaline polyacrylamide gel electrophoresis.	polyacrylamide	124-138	complement C2	Bos taurus	81-90
4043440-3	1985	The effect of the NSP fraction and its four peptide constituents (A, C2, D and G) on the 3H-thymidine incorporation into REF and R-XC cells in vitro was described.	3h-thymidine	89-101	complement C2	Bos taurus	69-80
6230046-14	1984	The results also suggest a role for iduronosyl residues, and perhaps the stereochemical relationship of the carboxyl group to the O-sulfate moiety at C-2, in the recognition process.	o-sulfate	130-139	complement C2	Bos taurus	150-153
6189517-5	1983	Baumycins B1, B2, C1, and C2 showed high IC50 values on three polymerases.	baumycins	0-9	complement C2	Bos taurus	10-28
393248-0	1979	The exchange of histidine C-2 protons in superoxide dismutases.	Histidine	16-25	complement C2	Bos taurus	26-29
393248-2	1979	The rates of exchange of the C-2 protons of histidine residues in copper-zinc superoxide dismutase are substantially decreased by metal ion binding.	Histidine	44-53	complement C2	Bos taurus	29-32
393248-2	1979	The rates of exchange of the C-2 protons of histidine residues in copper-zinc superoxide dismutase are substantially decreased by metal ion binding.	Metals	130-135	complement C2	Bos taurus	29-32
435461-4	1979	The configurational purity of tritium at C-2 of dopamine and C-1 of the dopamine precursor 3-methoxy-4-hydroxyphenethylamine has been confirmed employing dopamine-beta-hydroxylase (specific for the pro-R hydrogen at C-2) and pea seedling amine oxidase (specific for the pro-S hydrogen at C-1).	Tritium	30-37	complement C2	Bos taurus	41-44
435461-4	1979	The configurational purity of tritium at C-2 of dopamine and C-1 of the dopamine precursor 3-methoxy-4-hydroxyphenethylamine has been confirmed employing dopamine-beta-hydroxylase (specific for the pro-R hydrogen at C-2) and pea seedling amine oxidase (specific for the pro-S hydrogen at C-1).	Tritium	30-37	complement C2	Bos taurus	216-219
435461-4	1979	The configurational purity of tritium at C-2 of dopamine and C-1 of the dopamine precursor 3-methoxy-4-hydroxyphenethylamine has been confirmed employing dopamine-beta-hydroxylase (specific for the pro-R hydrogen at C-2) and pea seedling amine oxidase (specific for the pro-S hydrogen at C-1).	Dopamine	48-56	complement C2	Bos taurus	41-44
435461-4	1979	The configurational purity of tritium at C-2 of dopamine and C-1 of the dopamine precursor 3-methoxy-4-hydroxyphenethylamine has been confirmed employing dopamine-beta-hydroxylase (specific for the pro-R hydrogen at C-2) and pea seedling amine oxidase (specific for the pro-S hydrogen at C-1).	3-methoxytyramine	91-124	complement C2	Bos taurus	41-44
435461-4	1979	The configurational purity of tritium at C-2 of dopamine and C-1 of the dopamine precursor 3-methoxy-4-hydroxyphenethylamine has been confirmed employing dopamine-beta-hydroxylase (specific for the pro-R hydrogen at C-2) and pea seedling amine oxidase (specific for the pro-S hydrogen at C-1).	3-methoxytyramine	91-124	complement C2	Bos taurus	216-219
435461-4	1979	The configurational purity of tritium at C-2 of dopamine and C-1 of the dopamine precursor 3-methoxy-4-hydroxyphenethylamine has been confirmed employing dopamine-beta-hydroxylase (specific for the pro-R hydrogen at C-2) and pea seedling amine oxidase (specific for the pro-S hydrogen at C-1).	Hydrogen	204-212	complement C2	Bos taurus	41-44
435461-4	1979	The configurational purity of tritium at C-2 of dopamine and C-1 of the dopamine precursor 3-methoxy-4-hydroxyphenethylamine has been confirmed employing dopamine-beta-hydroxylase (specific for the pro-R hydrogen at C-2) and pea seedling amine oxidase (specific for the pro-S hydrogen at C-1).	Hydrogen	276-284	complement C2	Bos taurus	41-44
921767-1	1977	The C-2 proton of one histidine residue in bovine erythrocyte superoxide dismutase is shown to be particularly labile.	Histidine	22-31	complement C2	Bos taurus	4-7
4386407-10	1968	However, C-2 of glutamate is not incorporated into fatty acids or non-saponifiable lipid by bovine liver slices.	Glutamic Acid	16-25	complement C2	Bos taurus	9-12
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 C2	Bos taurus	69-72
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 C2	Bos taurus	69-72
1004498-2	1976	It is found that short times of exposure to d-TFA allow selective deuteration at the C-2 position with only a small amount of deuteration at the C-5 position, as expected from studies on model peptides described in the previous paper.	d-tfa	44-49	complement C2	Bos taurus	85-88
1004498-4	1976	Selective deuteration at the tryptophan C-2 position was readily observed by difference spectroscopy of the denatured protein, but PMR difference spectra of the same proteins in benign solvents did not contain resonances from all of the exchanged protons.	Tryptophan	29-39	complement C2	Bos taurus	40-43
8090-0	1976	pH dependence of tritium exchange with the C-2 protons of the histidines in bovine trypsin.	Histidine	62-72	complement C2	Bos taurus	43-46
8090-1	1976	At pH 8.9 and 37 degrees C the half-times for tritium exchange with the C-2 protons of the histidines of trypsin are 73 days for His-57, and greater than 1000 days for His-40 and His-91.	Tritium	46-53	complement C2	Bos taurus	72-75
8090-1	1976	At pH 8.9 and 37 degrees C the half-times for tritium exchange with the C-2 protons of the histidines of trypsin are 73 days for His-57, and greater than 1000 days for His-40 and His-91.	Histidine	91-101	complement C2	Bos taurus	72-75
8090-1	1976	At pH 8.9 and 37 degrees C the half-times for tritium exchange with the C-2 protons of the histidines of trypsin are 73 days for His-57, and greater than 1000 days for His-40 and His-91.	Histidine	129-132	complement C2	Bos taurus	72-75
8090-1	1976	At pH 8.9 and 37 degrees C the half-times for tritium exchange with the C-2 protons of the histidines of trypsin are 73 days for His-57, and greater than 1000 days for His-40 and His-91.	Histidine	168-171	complement C2	Bos taurus	72-75
8090-1	1976	At pH 8.9 and 37 degrees C the half-times for tritium exchange with the C-2 protons of the histidines of trypsin are 73 days for His-57, and greater than 1000 days for His-40 and His-91.	Histidine	168-171	complement C2	Bos taurus	72-75
8090-2	1976	These half-times are much longer than the half-life of exchange for the C-2 proton of free histidine (2.8 days at pD 8.2), and longer than any previously reported half-time of exchange at pH greater than 8.	Histidine	91-100	complement C2	Bos taurus	72-75
4454-2	1976	One of the four titrating histidine ring C-2 proton resonances of bovine pancreatic ribonuclease has been assigned to histidine residue 12.	Histidine	26-35	complement C2	Bos taurus	41-44
4454-2	1976	One of the four titrating histidine ring C-2 proton resonances of bovine pancreatic ribonuclease has been assigned to histidine residue 12.	Histidine	118-127	complement C2	Bos taurus	41-44
4454-3	1976	This was accomplished by a direct comparison of the rate of tritium incorporation into position C-2 of histidine 12 of S-peptide (residues 1 to 20) derived from ribonuclease S, with the rates of deuterium exchange of the four histidine C-2 proton resonances of ribonuclease S under the same experimental conditions.	Tritium	60-67	complement C2	Bos taurus	96-99
4454-3	1976	This was accomplished by a direct comparison of the rate of tritium incorporation into position C-2 of histidine 12 of S-peptide (residues 1 to 20) derived from ribonuclease S, with the rates of deuterium exchange of the four histidine C-2 proton resonances of ribonuclease S under the same experimental conditions.	Histidine	103-112	complement C2	Bos taurus	96-99
239193-2	1975	For neurophysin I alone, a normal titration curve for the C-2 proton resonance of the lone histidine residue was obtained with an apparent ionization constant of 6.9 addition of oxytocin to a solution of neurophysin I at pH 6.5 resulted in several changes in the spectrum.	Histidine	91-100	complement C2	Bos taurus	58-61
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 C2	Bos taurus	83-87
30398084-1	2018	AIM: To study of the interactions of two new ruthenium(II) complexes (C1 and C2) with calf thymus (CT)-DNA; production of RuO2 nanoparticles using the complexes precursor.	Ruthenium(II)	45-58	complement C2	Bos taurus	70-79
30398084-1	2018	AIM: To study of the interactions of two new ruthenium(II) complexes (C1 and C2) with calf thymus (CT)-DNA; production of RuO2 nanoparticles using the complexes precursor.	ruthenium dioxide	122-126	complement C2	Bos taurus	70-79
9237422-8	1997	Thus it seems that by replacing C-2 by an oxygen atom we can reduce the biological damage caused by relatively high concentrations of steroid treatment.	Oxygen	42-48	complement C2	Bos taurus	32-35
22558973-4	2012	The C1-2 dehydrogenation of naturally present cortisol and cortisone was checked by incubating urine, both contaminated and uncontaminated with faeces, at 37 C and by collecting samples at 0, 1, 2, 4, 6 and 24 h. The influence of Helix pomatia juice was also investigated in order to determine whether deconjugation could influence the reliability of the results.	Hydrocortisone	46-54	complement C2	Bos taurus	4-8
22558973-4	2012	The C1-2 dehydrogenation of naturally present cortisol and cortisone was checked by incubating urine, both contaminated and uncontaminated with faeces, at 37 C and by collecting samples at 0, 1, 2, 4, 6 and 24 h. The influence of Helix pomatia juice was also investigated in order to determine whether deconjugation could influence the reliability of the results.	Cortisone	59-68	complement C2	Bos taurus	4-8
20615869-3	2010	One orientation is such that it is expected to yield hydroxylation at C-2 of substrate, yielding xanthine.	Xanthine	97-105	complement C2	Bos taurus	70-73
20615869-5	2010	Kinetic experiments demonstrate that >98% of hypoxanthine is hydroxylated at C-2 rather than C-8, indicating that the second crystallographically observed orientation is significantly less catalytically effective than the former.	Hypoxanthine	48-60	complement C2	Bos taurus	80-83
20615869-6	2010	Theoretical calculations suggest that enzyme selectivity for the C-2 over C-8 of hypoxanthine is largely due to differences in the intrinsic reactivity of the two sites.	Hypoxanthine	81-93	complement C2	Bos taurus	65-68
20615869-7	2010	For the orientation of hypoxanthine with C-2 proximal to the molybdenum center, the disposition of substrate in the active site is such that Arg(880) and Glu(802), previous shown to be catalytically important for the conversion of xanthine to uric acid, play similar roles in hydroxylation at C-2 as at C-8.	Hypoxanthine	23-35	complement C2	Bos taurus	41-44
20615869-7	2010	For the orientation of hypoxanthine with C-2 proximal to the molybdenum center, the disposition of substrate in the active site is such that Arg(880) and Glu(802), previous shown to be catalytically important for the conversion of xanthine to uric acid, play similar roles in hydroxylation at C-2 as at C-8.	Hypoxanthine	23-35	complement C2	Bos taurus	293-296
20615869-7	2010	For the orientation of hypoxanthine with C-2 proximal to the molybdenum center, the disposition of substrate in the active site is such that Arg(880) and Glu(802), previous shown to be catalytically important for the conversion of xanthine to uric acid, play similar roles in hydroxylation at C-2 as at C-8.	Arginine	141-144	complement C2	Bos taurus	41-44
20615869-7	2010	For the orientation of hypoxanthine with C-2 proximal to the molybdenum center, the disposition of substrate in the active site is such that Arg(880) and Glu(802), previous shown to be catalytically important for the conversion of xanthine to uric acid, play similar roles in hydroxylation at C-2 as at C-8.	Arginine	141-144	complement C2	Bos taurus	293-296
20615869-7	2010	For the orientation of hypoxanthine with C-2 proximal to the molybdenum center, the disposition of substrate in the active site is such that Arg(880) and Glu(802), previous shown to be catalytically important for the conversion of xanthine to uric acid, play similar roles in hydroxylation at C-2 as at C-8.	Glutamic Acid	154-157	complement C2	Bos taurus	41-44
20615869-7	2010	For the orientation of hypoxanthine with C-2 proximal to the molybdenum center, the disposition of substrate in the active site is such that Arg(880) and Glu(802), previous shown to be catalytically important for the conversion of xanthine to uric acid, play similar roles in hydroxylation at C-2 as at C-8.	Glutamic Acid	154-157	complement C2	Bos taurus	293-296
20615869-7	2010	For the orientation of hypoxanthine with C-2 proximal to the molybdenum center, the disposition of substrate in the active site is such that Arg(880) and Glu(802), previous shown to be catalytically important for the conversion of xanthine to uric acid, play similar roles in hydroxylation at C-2 as at C-8.	Xanthine	27-35	complement C2	Bos taurus	41-44
20615869-7	2010	For the orientation of hypoxanthine with C-2 proximal to the molybdenum center, the disposition of substrate in the active site is such that Arg(880) and Glu(802), previous shown to be catalytically important for the conversion of xanthine to uric acid, play similar roles in hydroxylation at C-2 as at C-8.	Xanthine	27-35	complement C2	Bos taurus	293-296
20615869-7	2010	For the orientation of hypoxanthine with C-2 proximal to the molybdenum center, the disposition of substrate in the active site is such that Arg(880) and Glu(802), previous shown to be catalytically important for the conversion of xanthine to uric acid, play similar roles in hydroxylation at C-2 as at C-8.	Uric Acid	243-252	complement C2	Bos taurus	41-44
17400261-9	2007	Benzyl benzoates 14a and 15a have methoxyl groups at C-2/C-4 and C-3/C-4 in ring A, respectively; while 30a, in addition to the methoxyl groups at C-2/C-6 of ring A, hold a benzoyloxy moiety at C-3" of ring B.	Benzoates	7-16	complement C2	Bos taurus	53-56
17400261-9	2007	Benzyl benzoates 14a and 15a have methoxyl groups at C-2/C-4 and C-3/C-4 in ring A, respectively; while 30a, in addition to the methoxyl groups at C-2/C-6 of ring A, hold a benzoyloxy moiety at C-3" of ring B.	Benzoates	7-16	complement C2	Bos taurus	147-150
17400261-9	2007	Benzyl benzoates 14a and 15a have methoxyl groups at C-2/C-4 and C-3/C-4 in ring A, respectively; while 30a, in addition to the methoxyl groups at C-2/C-6 of ring A, hold a benzoyloxy moiety at C-3" of ring B.	7-methoxy-6-(2'-methoxy-3'-hydroxy-3'-methyl butyl)	34-42	complement C2	Bos taurus	53-56
9860488-3	1998	The coupling with the dG moiety occurred exclusively at C-2 of benzanthrone (BA), suggesting a significant contribution of a resonance-stabilized arenium ion intermediate derived from BA to the production of this new type of adduct.	benzanthrone	63-75	complement C2	Bos taurus	56-59
9860488-3	1998	The coupling with the dG moiety occurred exclusively at C-2 of benzanthrone (BA), suggesting a significant contribution of a resonance-stabilized arenium ion intermediate derived from BA to the production of this new type of adduct.	benzanthrone	77-79	complement C2	Bos taurus	56-59
15620101-1	2004	Five N10-substituted phenoxazines having different R groups and -Cl substitution at C-2 were found to bind to calf -thymus DNA and plasmid DNA with high affinity as seen from by UV and CD spectroscopy.	phenoxazine	21-33	complement C2	Bos taurus	84-87
9237422-8	1997	Thus it seems that by replacing C-2 by an oxygen atom we can reduce the biological damage caused by relatively high concentrations of steroid treatment.	Steroids	134-141	complement C2	Bos taurus	32-35
7881183-3	1994	A minor proportion of the L-iduronate may be O-sulphated at C-2.	Iduronic Acid	26-37	complement C2	Bos taurus	60-63
34318701-6	2021	Short-chain acylcarnitines (carbon chain length C2, C3, C4, and C5) and long-chain acylcarnitines (C14, C16, and C18) had the highest performance to indicate LPS response when testing the predictive power of single metabolites using receiver-operator characteristics (ROC) analysis.	acylcarnitine	12-26	complement C2	Bos taurus	48-66
8033884-7	1994	The results also suggest that the N-acetyl NH group in N-acetyllactosamine, as well as the hydroxyl group at position C-2 in methyl beta-lactoside, are involved in a polar interaction with neutral groups of the combining site.	Nitrogen	34-35	complement C2	Bos taurus	118-121
8033884-7	1994	The results also suggest that the N-acetyl NH group in N-acetyllactosamine, as well as the hydroxyl group at position C-2 in methyl beta-lactoside, are involved in a polar interaction with neutral groups of the combining site.	methyl radical	125-131	complement C2	Bos taurus	118-121
8033884-7	1994	The results also suggest that the N-acetyl NH group in N-acetyllactosamine, as well as the hydroxyl group at position C-2 in methyl beta-lactoside, are involved in a polar interaction with neutral groups of the combining site.	beta-lactoside	132-146	complement C2	Bos taurus	118-121
1637818-4	1992	The stereochemical course of the bovine and porcine aortic semicarbazide-sensitive amine oxidase reaction was investigated using chiral tyramines, deuterated at C-1 and C-2, and 1H-NMR spectroscopy to establish the loss or retention of deuterium in product p-hydroxyphenethyl alcohols.	carbamylhydrazine	59-72	complement C2	Bos taurus	161-172
1637818-5	1992	The preferred mode of tyramine oxidation was found to occur with the loss of pro-S proton at C-1, coupled with solvent exchange into C-2, a pattern which has not been observed for any copper amine oxidase examined to date.	Tyramine	22-30	complement C2	Bos taurus	133-136
8086426-2	1994	Several tropolones containing a free C-2 hydroxy group were found to be potent inhibitors of glyoxalase I, whereas the glutathione conjugates were found to be modest to poor inhibitors of this enzyme.	Tropolone	8-18	complement C2	Bos taurus	37-40
34318701-6	2021	Short-chain acylcarnitines (carbon chain length C2, C3, C4, and C5) and long-chain acylcarnitines (C14, C16, and C18) had the highest performance to indicate LPS response when testing the predictive power of single metabolites using receiver-operator characteristics (ROC) analysis.	Carbon	28-34	complement C2	Bos taurus	48-66