PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22747514-2	2012	At the neuromuscular junction, AChE is mainly anchored in the extracellular matrix by the collagen Q, whereas in the brain, AChE is tethered by the proline-rich membrane anchor (PRiMA).	Proline	148-155	acetylcholinesterase	Mus musculus	124-128	
23897820-6	2013	Although similar decreases in mRNA levels were observed of the proline-rich anchor of AChE, PRiMA, no changes were seen in mRNA levels of the related enzyme, butyryl-cholinesterase, nor of the high-affinity choline transporter.	Proline	63-70	acetylcholinesterase	Mus musculus	86-90	
26036470-6	2015	In the analysis of the expression of anchoring subunits of AChE in P2Y1R (-/-) mice, the proline-rich membrane anchor (PRiMA) subunit was reduced by 60 %; while the collagen tail (ColQ) subunit was reduced by 50 %.	Proline	89-96	acetylcholinesterase	Mus musculus	59-63	
24612677-3	2014	The major AChE variant expressed in the brain is a tetramer (G(4)) bound to a proline-rich membrane anchor (PRiMA).	Proline	78-85	acetylcholinesterase	Mus musculus	10-14	
19357277-0	2009	Targeting of acetylcholinesterase in neurons in vivo: a dual processing function for the proline-rich membrane anchor subunit and the attachment domain on the catalytic subunit.	Proline	89-96	acetylcholinesterase	Mus musculus	13-33	
22750213-1	2012	Acetylcholinesterase (AChE) is organized into globular tetramers (G(4)) by a structural protein called proline-rich membrane anchor (PRiMA), anchoring it into the cell membrane of neurons in the brain.	Proline	103-110	acetylcholinesterase	Mus musculus	0-20	
22750213-1	2012	Acetylcholinesterase (AChE) is organized into globular tetramers (G(4)) by a structural protein called proline-rich membrane anchor (PRiMA), anchoring it into the cell membrane of neurons in the brain.	Proline	103-110	acetylcholinesterase	Mus musculus	22-26	
20176004-2	2010	In neurons, the catalytic subunit of acetylcholinesterase (AChE(T)) interacts with proline-rich membrane anchor (PRiMA) to form a globular tetrameric form (G(4) form).	Proline	83-90	acetylcholinesterase	Mus musculus	37-57	
20176004-2	2010	In neurons, the catalytic subunit of acetylcholinesterase (AChE(T)) interacts with proline-rich membrane anchor (PRiMA) to form a globular tetrameric form (G(4) form).	Proline	83-90	acetylcholinesterase	Mus musculus	59-66	
19357277-1	2009	Acetylcholinesterase (AChE) accumulates on axonal varicosities and is primarily found as tetramers associated with a proline-rich membrane anchor (PRiMA).	Proline	117-124	acetylcholinesterase	Mus musculus	0-20	
19357277-1	2009	Acetylcholinesterase (AChE) accumulates on axonal varicosities and is primarily found as tetramers associated with a proline-rich membrane anchor (PRiMA).	Proline	117-124	acetylcholinesterase	Mus musculus	22-26	
16299589-2	2005	In physiological conditions, AChE exists as tetramers associated with the proline-rich attachment domain (PRAD) of either collagen-like Q subunit (ColQ) or proline-rich membrane-anchoring protein.	Proline	74-81	acetylcholinesterase	Mus musculus	29-33	
18215127-8	2008	Docking showed the major component of the interaction site on AChE to be the acidic sequence Arg(90)-Glu-Leu-Ser-Glu-Asp(95) on the omega loop, and also the involvement of Pro(40)-Pro-Val(42), Arg(46) (linked to Glu(94) by a salt bridge) and the hexapeptide Asp(61)-Ala-Thr-Thr-Phe-Gln(66).	Proline	172-175	acetylcholinesterase	Mus musculus	62-66	
17324938-2	2007	The transcriptional regulation of proline-rich membrane anchor (PRiMA), an anchoring protein of tetrameric globular form acetylcholinesterase (G(4) AChE), was revealed in muscle during myogenic differentiation under the influence of innervation.	Proline	34-41	acetylcholinesterase	Mus musculus	148-152	
16299589-2	2005	In physiological conditions, AChE exists as tetramers associated with the proline-rich attachment domain (PRAD) of either collagen-like Q subunit (ColQ) or proline-rich membrane-anchoring protein.	Proline	156-163	acetylcholinesterase	Mus musculus	29-33