PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 15526038-0 2004 The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix. polyproline 62-73 acetylcholinesterase (Cartwright blood group) Homo sapiens 13-33 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