PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
20565071-2	2010	Preference for the North (N) ring conformation of the ribose moiety of adenine nucleotide 3",5"-bisphosphate antagonists of the P2Y(1) receptor was established by using a ring-constrained methanocarba (a bicyclo[3.1.0]hexane) ring as a ribose substitute.	Ribose	54-60	purinergic receptor P2Y1	Homo sapiens	128-143	
20565071-2	2010	Preference for the North (N) ring conformation of the ribose moiety of adenine nucleotide 3",5"-bisphosphate antagonists of the P2Y(1) receptor was established by using a ring-constrained methanocarba (a bicyclo[3.1.0]hexane) ring as a ribose substitute.	Ribose	236-242	purinergic receptor P2Y1	Homo sapiens	128-143	
18673269-6	2008	Finally, replacement of the ribose ring with a five member methanocarba ring constrained in the Northern conformation conferred dramatic increases in affinity to both P2Y(1) receptor antagonists as well as agonists.	Ribose	28-34	purinergic receptor P2Y1	Homo sapiens	167-182	
11563046-4	2001	Conformational constraints were built into the ribose rings of nucleoside and nucleotide ligands using the methanocarba approach, i.e. fused cyclopropane and cyclopentane rings in place of ribose, suggesting a preference for the Northern (N) conformation among ligands for P2Y1 and A1 and A3ARs.	Ribose	47-53	purinergic receptor P2Y1	Homo sapiens	273-294	
11959804-2	2002	We reported previously that bisphosphate derivatives of adenosine are antagonists of the P2Y(1) receptor and that modification of the ribose in these analogues is tolerated in the P2Y(1) receptor binding pharmacophore.	Ribose	134-140	purinergic receptor P2Y1	Homo sapiens	89-104	
11959804-2	2002	We reported previously that bisphosphate derivatives of adenosine are antagonists of the P2Y(1) receptor and that modification of the ribose in these analogues is tolerated in the P2Y(1) receptor binding pharmacophore.	Ribose	134-140	purinergic receptor P2Y1	Homo sapiens	180-195	
15465340-1	2004	The ribose moiety of adenine nucleotide 3",5"-bisphosphate antagonists of the P2Y(1) receptor has been successfully substituted with a rigid methanocarba ring system, leading to the conclusion that the North (N) ring conformation is preferred in receptor binding.	Ribose	4-10	purinergic receptor P2Y1	Homo sapiens	78-93	
14584948-1	2003	Preference for the northern (N) ring conformation of the ribose moiety of adenine nucleotide 3",5"-bisphosphate antagonists of P2Y(1) receptors was established by using a ring-constrained methanocarba (a bicyclo[3.1.0]hexane) ring as a ribose substitute (Nandanan et al.	Ribose	57-63	purinergic receptor P2Y1	Homo sapiens	127-133	
14584948-1	2003	Preference for the northern (N) ring conformation of the ribose moiety of adenine nucleotide 3",5"-bisphosphate antagonists of P2Y(1) receptors was established by using a ring-constrained methanocarba (a bicyclo[3.1.0]hexane) ring as a ribose substitute (Nandanan et al.	Ribose	236-242	purinergic receptor P2Y1	Homo sapiens	127-133	
11754592-1	2002	The potency of nucleotide antagonists at P2Y1 receptors was enhanced by replacing the ribose moiety with a constrained carbocyclic ring (Nandanan, et al.	Ribose	86-92	purinergic receptor P2Y1	Homo sapiens	41-45