PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15526038-0	2004	The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix.	polyproline	62-73	acetylcholinesterase (Cartwright blood group)	Homo sapiens	13-33	
10421436-9	1999	The critical feature of this motif is the presence of a string of prolines, and in fact synthetic polyproline shows a similar capacity to organize AChE(T) tetramers.	polyproline	98-109	acetylcholinesterase (Cartwright blood group)	Homo sapiens	147-151	
23352838-0	2013	Polyproline tetramer organizing peptides in fetal bovine serum acetylcholinesterase.	polyproline	0-11	acetylcholinesterase (Cartwright blood group)	Homo sapiens	63-83	
23352838-10	2013	A search of the mammalian proteome database suggested that this assortment of polyproline peptides originated from at least 5 different precursor proteins, none of which were the ColQ or PRiMA of membrane-anchored AChE.	polyproline	78-89	acetylcholinesterase (Cartwright blood group)	Homo sapiens	214-218	
23352838-11	2013	To date, AChE and BChE are the only proteins known that include polyproline tetramer organizing peptides in their tetrameric structure.	polyproline	64-75	acetylcholinesterase (Cartwright blood group)	Homo sapiens	9-13	
17158452-6	2007	We confirmed the importance of the polyproline stretches and defined a peptidic motif (RP4LP10RL), which induces the assembly and secretion of a heteromeric complex with four AChE(T) subunits, nearly as efficiently as the entire extracellular domain of PRiMA.	polyproline	35-46	acetylcholinesterase (Cartwright blood group)	Homo sapiens	175-179