PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
28340590-8	2017	Results indicate that the mean angle was different between Dob-CSM and GD-CSM at C4-5, C5-6, and C6-7, and between GD-N and GD-CSM at C6-7.	2,5-dimethoxy-4-bromoamphetamine	59-62	complement C6	Canis lupus familiaris	97-101
6306109-1	1983	Isolated dog mastocytoma cells sensitized with dog anti-ragweed IgE and challenged with ragweed antigen generate the C-6 peptide leukotriene (LT) constituents of the slow-reacting substance of anaphylaxis (SRS-A), LTC4 and LTD4, and the potent leukocyte chemotactic factor, LTB4, as well as 15-hydroxyeicosatetraenoic acid (15-HETE), 12-HETE, and 5-HETE.	Leukotrienes	129-140	complement C6	Canis lupus familiaris	117-120
6306109-1	1983	Isolated dog mastocytoma cells sensitized with dog anti-ragweed IgE and challenged with ragweed antigen generate the C-6 peptide leukotriene (LT) constituents of the slow-reacting substance of anaphylaxis (SRS-A), LTC4 and LTD4, and the potent leukocyte chemotactic factor, LTB4, as well as 15-hydroxyeicosatetraenoic acid (15-HETE), 12-HETE, and 5-HETE.	Eicosatetraenoic acid, 15-hydroxy-	291-322	complement C6	Canis lupus familiaris	117-120
6306109-1	1983	Isolated dog mastocytoma cells sensitized with dog anti-ragweed IgE and challenged with ragweed antigen generate the C-6 peptide leukotriene (LT) constituents of the slow-reacting substance of anaphylaxis (SRS-A), LTC4 and LTD4, and the potent leukocyte chemotactic factor, LTB4, as well as 15-hydroxyeicosatetraenoic acid (15-HETE), 12-HETE, and 5-HETE.	15-Hete	324-331	complement C6	Canis lupus familiaris	117-120
3455050-1	1987	A number of progesterone derivatives, having a 17 alpha-acetoxy group and various functions at C-3 and C-6, interact at the cardiac glycoside (CG) binding site, using [3H]ouabain in a radioligand binding assay (RBA) with membranes from dog myocardium.	Glycosides	132-141	complement C6	Canis lupus familiaris	103-106
3455050-1	1987	A number of progesterone derivatives, having a 17 alpha-acetoxy group and various functions at C-3 and C-6, interact at the cardiac glycoside (CG) binding site, using [3H]ouabain in a radioligand binding assay (RBA) with membranes from dog myocardium.	Cardiac Glycosides	143-145	complement C6	Canis lupus familiaris	103-106
3455050-1	1987	A number of progesterone derivatives, having a 17 alpha-acetoxy group and various functions at C-3 and C-6, interact at the cardiac glycoside (CG) binding site, using [3H]ouabain in a radioligand binding assay (RBA) with membranes from dog myocardium.	Tritium	168-170	complement C6	Canis lupus familiaris	103-106
3455050-6	1987	In compounds with other substituents that promote activity, C-6 alpha substitution with -CH3, -Cl, or -Br strongly enhances activity; -F, -OCH3, carbonyl, or the unsubstituted compound promotes weak binding; and -OC2H5, -OAc, -OCOOCH3, or -OH eliminates binding activity.	SDZ 33-243	221-224	complement C6	Canis lupus familiaris	60-63
28340590-8	2017	Results indicate that the mean angle was different between Dob-CSM and GD-CSM at C4-5, C5-6, and C6-7, and between GD-N and GD-CSM at C6-7.	Gadolinium	71-73	complement C6	Canis lupus familiaris	97-101
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.	hydrazine	0-9	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.	hydrazine	0-9	complement C6	Canis lupus familiaris	258-261
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.	Nitrous Acid	10-22	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.	sodium borohydride	23-27	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.	Acetylglucosamine	140-159	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.	Acetylglucosamine	140-159	complement C6	Canis lupus familiaris	258-261
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
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.	Acetylglucosamine	275-294	complement C6	Canis lupus familiaris	129-132
1825861-12	1991	The uptake of DOG and the conversion of glucose C-1 and glucose C-6 to CO2, were significantly (P less than 0.05) higher in the adipocytes of trained animals indicating that they were more responsive to insulin than the sedentary controls, which corresponded to increases in the respiratory enzyme levels of the muscles.	Glucose	56-63	complement C6	Canis lupus familiaris	64-67
1825861-13	1991	During the first 7 days of detraining DOG uptake and both C-1 and C-6 glucose oxidation remained elevated.	Glucose	70-77	complement C6	Canis lupus familiaris	66-69