PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
6182778-4	1982	The inhibitory effect of flavonoids on human platelet function was diminished by saturation of the C-2, C-3 double bond, lack of the C-4 carbonyl, glycosylation at C-3 and a high number of hydroxyl substituents.	Flavonoids	25-35	complement C3	Homo sapiens	104-107	
6182778-4	1982	The inhibitory effect of flavonoids on human platelet function was diminished by saturation of the C-2, C-3 double bond, lack of the C-4 carbonyl, glycosylation at C-3 and a high number of hydroxyl substituents.	Flavonoids	25-35	complement C3	Homo sapiens	164-167	
31621310-7	2019	These results coupled with simulation studies modeling flavonoid interaction within the AhR binding pocket demonstrate that the orientation of the substituted phenyl ring at C-2 (flavones) or C-3 (isoflavones) on the common 4-H-chromen-4-one ring strongly influences the activities of isoflavones and flavones as AhR agonists.	Flavonoids	55-64	complement C3	Homo sapiens	192-195	
23330926-2	2013	The metabolites of flavonoids in liver can be summarized as follows: 1) For flavones, the hydroxylation appears to occur at the C-4"-, C-3", C-6 and C-8- position when there is a single or no hydroxy group on the B-ring.	Flavonoids	19-29	complement C3	Homo sapiens	135-138	
22542668-7	2012	Analysis of structure-activity data revealed that flavonoids containing two hydroxyl groups in ring B and a carbonyl group at C-4 in combination with a double bond between C-2 and C-3 produced a much stronger inhibition, whereas substitution of a hydroxyl group at C-3 was associated with a less inhibitory effect.	Flavonoids	50-60	complement C3	Homo sapiens	180-183	
22292767-4	2012	The hydroxylation on A-ring of flavones and isoflavones, especially at C-5 and C-7, significantly enhanced the inhibitory activities against digestive enzymes and the hydroxylation on positions C-3" and C-4" of B-ring of flavonoids remarkably improved the inhibition.	Flavonoids	221-231	complement C3	Homo sapiens	194-197	
22292767-10	2012	The methylation and methoxylation of the hydroxyl group at C-3, C-3" and C-4" of flavonoids decreased or little affected the inhibitory potency against aldose reductases.	Flavonoids	81-91	complement C3	Homo sapiens	59-62	
22292767-10	2012	The methylation and methoxylation of the hydroxyl group at C-3, C-3" and C-4" of flavonoids decreased or little affected the inhibitory potency against aldose reductases.	Flavonoids	81-91	complement C3	Homo sapiens	64-67	
14570878-7	2004	In the case of products formed by oxidation of flavonoid substrates with a C-3 hydroxyl group (e.g. (2R,3R)-trans-dihydroquercetin), the results imply that oxygen exchange can occur at a stage subsequent to initial oxidation of the C-ring, probably via an enzyme-bound C-3 ketone/3,3-gem-diol intermediate.	Flavonoids	47-56	complement C3	Homo sapiens	75-78	
21413806-2	2011	We systematically studied the glucuronidation of 13 flavonoids (7 flavones and 6 flavonols, with hydroxyl groups at C-3, C-4", C-5, and/or C-7 positions in flavonoid structure) at a substrate concentration of 10 muM by 8 recombinant human UGT isoforms mainly responsible for the metabolism of flavonoids, UGTs 1A1, 1A3, 1A6, 1A7, 1A8, 1A9, 1A10, and 2B7.	Flavonoids	52-62	complement C3	Homo sapiens	116-119	
16106293-11	2005	Thus, by utilising flavonoid substrates with different C-2 stereochemistries, the balance between C-3 hydroxylation or C-2, C-3 desaturation mechanisms can be altered.	Flavonoids	19-28	complement C3	Homo sapiens	98-101	
16106293-11	2005	Thus, by utilising flavonoid substrates with different C-2 stereochemistries, the balance between C-3 hydroxylation or C-2, C-3 desaturation mechanisms can be altered.	Flavonoids	19-28	complement C3	Homo sapiens	124-127	
14570878-7	2004	In the case of products formed by oxidation of flavonoid substrates with a C-3 hydroxyl group (e.g. (2R,3R)-trans-dihydroquercetin), the results imply that oxygen exchange can occur at a stage subsequent to initial oxidation of the C-ring, probably via an enzyme-bound C-3 ketone/3,3-gem-diol intermediate.	Flavonoids	47-56	complement C3	Homo sapiens	269-272	
12240335-0	2001	Evidence for oxidation at C-3 of the flavonoid C-ring during anthocyanin biosynthesis.	Flavonoids	37-46	complement C3	Homo sapiens	26-29	
12240335-1	2001	Evidence is presented for initial oxidation at the C-3 position of the flavonoid C-ring and for two bifurcating steps during catalysis by anthocyanidin synthase.	Flavonoids	71-80	complement C3	Homo sapiens	51-54	
11409965-2	2001	From seven structurally divergent groups of flavonoids, only flavonols with a free hydroxyl group at the C-3 position of the flavonoid skeleton showed high inhibitory activity to beta-carotene oxidation.	Flavonoids	44-54	complement C3	Homo sapiens	105-108	
11409965-2	2001	From seven structurally divergent groups of flavonoids, only flavonols with a free hydroxyl group at the C-3 position of the flavonoid skeleton showed high inhibitory activity to beta-carotene oxidation.	Flavonoids	44-53	complement C3	Homo sapiens	105-108	
10861967-6	2000	This result indicates that the stereoscopic structure between the C-3 group and the B ring of flavonoids as well as substituents at the C-3 position make a contribution to radical scavenging activity.	Flavonoids	94-104	complement C3	Homo sapiens	66-69	
7673925-4	1995	Inhibition of leucine aminopeptidase by flavonoids does not require 5,7-hydroxylation, but dihydroxylation at C-3" and C-4" and a double bond at positions C-2, C-3 are essential for this activity.	Flavonoids	40-50	complement C3	Homo sapiens	160-163	
7769390-3	1995	Flavonoids demonstrating potent topo I and II inhibition required hydroxyl group substitution at the C-3, C-7, C-3", and C-4" positions and also required a keto group at C-4.	Flavonoids	0-10	complement C3	Homo sapiens	101-104	
7769390-3	1995	Flavonoids demonstrating potent topo I and II inhibition required hydroxyl group substitution at the C-3, C-7, C-3", and C-4" positions and also required a keto group at C-4.	Flavonoids	0-10	complement C3	Homo sapiens	111-114