PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24292832-6	2014	Arrestin-2 apparently self-associates into "infinite" chains, very similar to those observed in IP6-soaked crystals, where IP6 connects the concave sides of the N- and C-domains of adjacent protomers.	Phytic Acid	96-99	arrestin beta 1	Homo sapiens	0-10	
24292832-6	2014	Arrestin-2 apparently self-associates into "infinite" chains, very similar to those observed in IP6-soaked crystals, where IP6 connects the concave sides of the N- and C-domains of adjacent protomers.	Phytic Acid	123-126	arrestin beta 1	Homo sapiens	0-10	
18161994-0	2008	Opposing effects of inositol hexakisphosphate on rod arrestin and arrestin2 self-association.	Phytic Acid	20-45	arrestin beta 1	Homo sapiens	66-75	
18161994-4	2008	However, inositol hexakisphosphate (IP6), a fairly abundant form of inositol in the cytoplasm, greatly facilitates self-association of arrestin2.	Phytic Acid	9-34	arrestin beta 1	Homo sapiens	135-144	
18161994-4	2008	However, inositol hexakisphosphate (IP6), a fairly abundant form of inositol in the cytoplasm, greatly facilitates self-association of arrestin2.	Phytic Acid	36-39	arrestin beta 1	Homo sapiens	135-144	
18161994-5	2008	Arrestin2 self-association equilibrium constants in the presence of 100 microM IP6 suggest that an appreciable proportion could exist in an oligomeric state but only in intracellular compartments where its concentration is 5-10-fold higher than average.	Phytic Acid	79-82	arrestin beta 1	Homo sapiens	0-9	
16439357-3	2006	Here we characterize the structural, molecular, and cellular interactions between arrestin-2 and inositol hexakisphosphate (inositol 1,2,3,4,5,6-hexakisphosphate (IP(6))).	Phytic Acid	97-122	arrestin beta 1	Homo sapiens	82-92	
16439357-3	2006	Here we characterize the structural, molecular, and cellular interactions between arrestin-2 and inositol hexakisphosphate (inositol 1,2,3,4,5,6-hexakisphosphate (IP(6))).	Phytic Acid	124-161	arrestin beta 1	Homo sapiens	82-92