PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 28607150-3 2017 For instance, in bone, AChE exists as a proline-rich membrane anchor (PRiMA)-linked globular form in osteoblasts, in which it is proposed to play a noncholinergic role in differentiation. Proline 40-47 acetylcholinesterase (Cartwright blood group) Homo sapiens 23-27 26521443-0 2015 [Design, synthesis and evaluation of new L-proline derivatives as acetylcholinesterase inhibitors]. Proline 41-50 acetylcholinesterase (Cartwright blood group) Homo sapiens 66-86 26521443-5 2015 So the acetylcholinesterase inhibitory activities of new L-proline derivatives were worth to be further studied. Proline 57-66 acetylcholinesterase (Cartwright blood group) Homo sapiens 7-27 25186736-5 2014 We found that BChE is anchored at the TSC by a proline-rich membrane anchor, the small transmembrane protein anchor of brain AChE. Proline 47-54 acetylcholinesterase (Cartwright blood group) Homo sapiens 125-129 24699279-5 2014 The AChE species capable of triggering the biggest increase in PS1 levels is a complex of AChE with the membrane anchoring subunit proline-rich membrane anchor (PRiMA), which restricts the localization of the resulting AChE tetramer to the outer plasma membrane. Proline 131-138 acetylcholinesterase (Cartwright blood group) Homo sapiens 4-8 24699279-5 2014 The AChE species capable of triggering the biggest increase in PS1 levels is a complex of AChE with the membrane anchoring subunit proline-rich membrane anchor (PRiMA), which restricts the localization of the resulting AChE tetramer to the outer plasma membrane. Proline 131-138 acetylcholinesterase (Cartwright blood group) Homo sapiens 90-94 24699279-5 2014 The AChE species capable of triggering the biggest increase in PS1 levels is a complex of AChE with the membrane anchoring subunit proline-rich membrane anchor (PRiMA), which restricts the localization of the resulting AChE tetramer to the outer plasma membrane. Proline 131-138 acetylcholinesterase (Cartwright blood group) Homo sapiens 90-94 23047022-3 2013 Since AChE does not possess a transmembrane domain, its anchorage in the membrane is established via the Proline Rich Membrane Anchor (PRiMA), a transmembrane protein. Proline 105-112 acetylcholinesterase (Cartwright blood group) Homo sapiens 6-10 20178777-2 2010 The AChE(T) variant is expressed in the brain and muscle: this subunit forms non-amphiphilic tetramers with a collagen tail (ColQ) as asymmetric AChE (A(12) AChE) in muscle, and amphiphilic tetramers with a proline-rich membrane anchor (PRiMA) as globular AChE (G(4) AChE) in the brain and muscle. Proline 207-214 acetylcholinesterase (Cartwright blood group) Homo sapiens 4-8 19680821-2 2010 Proline-rich membrane anchor (PRiMA)-linked tetrameric globular AChE (G4 AChE) is mainly found in the vertebrate brain; however, recent studies from our laboratory have suggested its existence at neuromuscular junctions (nmjs). Proline 0-7 acetylcholinesterase (Cartwright blood group) Homo sapiens 64-68 19680821-2 2010 Proline-rich membrane anchor (PRiMA)-linked tetrameric globular AChE (G4 AChE) is mainly found in the vertebrate brain; however, recent studies from our laboratory have suggested its existence at neuromuscular junctions (nmjs). Proline 0-7 acetylcholinesterase (Cartwright blood group) Homo sapiens 73-77 19368807-0 2009 Transcriptional regulation of proline-rich membrane anchor (PRiMA) of globular form acetylcholinesterase in neuron: an inductive effect of neuron differentiation. Proline 30-37 acetylcholinesterase (Cartwright blood group) Homo sapiens 84-104 19368807-1 2009 The transcriptional regulation of proline-rich membrane anchor (PRiMA), an anchoring protein of tetrameric globular form of acetylcholinesterase (G(4) AChE), was revealed in cultured cortical neurons during differentiation. Proline 34-41 acetylcholinesterase (Cartwright blood group) Homo sapiens 124-144 19368807-1 2009 The transcriptional regulation of proline-rich membrane anchor (PRiMA), an anchoring protein of tetrameric globular form of acetylcholinesterase (G(4) AChE), was revealed in cultured cortical neurons during differentiation. Proline 34-41 acetylcholinesterase (Cartwright blood group) Homo sapiens 151-155 18514177-5 2008 AChE(T) subunits associate with a collagen tail subunit (ColQ) forming asymmetric AChE species (A(4), A(8), and A(12) AChE) in muscle, and also form amphiphilic tetramers associated with a proline-rich membrane anchor (PRiMA) as globular AChE (G(4) AChE) in brain and muscle. Proline 189-196 acetylcholinesterase (Cartwright blood group) Homo sapiens 0-4 18511416-1 2008 Acetylcholinesterase tetramers are inserted in the basal lamina of neuromuscular junctions or anchored in cell membranes through the interaction of four C-terminal t peptides with proline-rich attachment domains (PRADs) of cholinesterase-associated collagen Q (ColQ) or of the transmembrane protein PRiMA (proline-rich membrane anchor). Proline 180-187 acetylcholinesterase (Cartwright blood group) Homo sapiens 0-20 17158452-0 2007 Assembly of acetylcholinesterase tetramers by peptidic motifs from the proline-rich membrane anchor, PRiMA: competition between degradation and secretion pathways of heteromeric complexes. Proline 71-78 acetylcholinesterase (Cartwright blood group) Homo sapiens 12-32 17158452-8 2007 Interestingly, short PRiMA mutants, truncated within the proline-rich motif, reduced both cellular and secreted AChE activity, suggesting that their interaction with AChE(T) subunits induces their intracellular degradation. Proline 57-64 acetylcholinesterase (Cartwright blood group) Homo sapiens 112-116 17158452-8 2007 Interestingly, short PRiMA mutants, truncated within the proline-rich motif, reduced both cellular and secreted AChE activity, suggesting that their interaction with AChE(T) subunits induces their intracellular degradation. Proline 57-64 acetylcholinesterase (Cartwright blood group) Homo sapiens 166-170 17192673-7 2006 PRiMAcDNA encodes a single-pass approximately 20-kDa type-I transmembrane protein and, similar to that of ColQ, contains a short PRAD (proline-rich attachment domain) that is able to organize AChE catalytic subunits into tetramers and anchor the enzyme at the surface of neuron and muscle (Massoulie, 2002). Proline 135-142 acetylcholinesterase (Cartwright blood group) Homo sapiens 192-196 16114264-2 2005 A short proline rich sequence in the N-terminal domain of ColQ or PRiMA associates four C-terminal extension of AChE or BChE. Proline 8-15 acetylcholinesterase (Cartwright blood group) Homo sapiens 112-116 15526038-1 2004 Functional localization of acetylcholinesterase (AChE) in vertebrate muscle and brain depends on interaction of the tryptophan amphiphilic tetramerization (WAT) sequence, at the C-terminus of its major splice variant (T), with a proline-rich attachment domain (PRAD), of the anchoring proteins, collagenous (ColQ) and proline-rich membrane anchor. Proline 229-236 acetylcholinesterase (Cartwright blood group) Homo sapiens 27-47 15526038-1 2004 Functional localization of acetylcholinesterase (AChE) in vertebrate muscle and brain depends on interaction of the tryptophan amphiphilic tetramerization (WAT) sequence, at the C-terminus of its major splice variant (T), with a proline-rich attachment domain (PRAD), of the anchoring proteins, collagenous (ColQ) and proline-rich membrane anchor. Proline 229-236 acetylcholinesterase (Cartwright blood group) Homo sapiens 49-53 15526038-1 2004 Functional localization of acetylcholinesterase (AChE) in vertebrate muscle and brain depends on interaction of the tryptophan amphiphilic tetramerization (WAT) sequence, at the C-terminus of its major splice variant (T), with a proline-rich attachment domain (PRAD), of the anchoring proteins, collagenous (ColQ) and proline-rich membrane anchor. Proline 318-325 acetylcholinesterase (Cartwright blood group) Homo sapiens 27-47 15526038-1 2004 Functional localization of acetylcholinesterase (AChE) in vertebrate muscle and brain depends on interaction of the tryptophan amphiphilic tetramerization (WAT) sequence, at the C-terminus of its major splice variant (T), with a proline-rich attachment domain (PRAD), of the anchoring proteins, collagenous (ColQ) and proline-rich membrane anchor. Proline 318-325 acetylcholinesterase (Cartwright blood group) Homo sapiens 49-53 15066173-1 2004 The C-terminal t peptide (40 residues) of vertebrate acetylcholinesterase (AChE) T subunits possesses a series of seven conserved aromatic residues and forms an amphiphilic alpha-helix; it allows the formation of homo-oligomers (monomers, dimers and tetramers) and heteromeric associations with the anchoring proteins, ColQ and PRiMA, which contain a proline-rich motif (PRAD). Proline 351-358 acetylcholinesterase (Cartwright blood group) Homo sapiens 53-73 15066173-1 2004 The C-terminal t peptide (40 residues) of vertebrate acetylcholinesterase (AChE) T subunits possesses a series of seven conserved aromatic residues and forms an amphiphilic alpha-helix; it allows the formation of homo-oligomers (monomers, dimers and tetramers) and heteromeric associations with the anchoring proteins, ColQ and PRiMA, which contain a proline-rich motif (PRAD). Proline 351-358 acetylcholinesterase (Cartwright blood group) Homo sapiens 75-79 14686917-1 2004 Acetylcholinesterase subunits of type T (AChET) possess an alternatively spliced C-terminal peptide (t peptide) which endows them with amphiphilic properties, the capacity to form various homo-oligomers and to associate, as a tetramer, with anchoring proteins containing a proline rich attachment domain (PRAD). Proline 273-280 acetylcholinesterase (Cartwright blood group) Homo sapiens 0-20 12853469-1 2003 The catalytic domain of acetylcholinesterase AChE(T) subunits is followed by a C-terminal T peptide which mediates their association with the proline-rich attachment domain (PRAD) of anchoring proteins. Proline 142-149 acetylcholinesterase (Cartwright blood group) Homo sapiens 24-44 12853469-1 2003 The catalytic domain of acetylcholinesterase AChE(T) subunits is followed by a C-terminal T peptide which mediates their association with the proline-rich attachment domain (PRAD) of anchoring proteins. Proline 142-149 acetylcholinesterase (Cartwright blood group) Homo sapiens 45-49 12609505-8 2003 Both patients presented a novel splicing mutation (IVS1-1G-->A) affecting the exon encoding the proline-rich attachment domain (PRAD), which interacts with acetylcholinesterase. Proline 99-106 acetylcholinesterase (Cartwright blood group) Homo sapiens 159-179 10665486-1 2000 The end-plate species of acetylcholinesterase (AChE) is an asymmetric enzyme consisting of a collagenic tail subunit composed of three collagenic strands (ColQ), each attached to a tetramer of the T isoform of the catalytic subunit (AChE(T)) via a proline-rich attachment domain. Proline 248-255 acetylcholinesterase (Cartwright blood group) Homo sapiens 25-45 10665486-1 2000 The end-plate species of acetylcholinesterase (AChE) is an asymmetric enzyme consisting of a collagenic tail subunit composed of three collagenic strands (ColQ), each attached to a tetramer of the T isoform of the catalytic subunit (AChE(T)) via a proline-rich attachment domain. Proline 248-255 acetylcholinesterase (Cartwright blood group) Homo sapiens 47-51 10421436-8 1999 ColQ contains a short peptidic motif, the proline-rich attachment domain (PRAD), that triggers the formation of AChE(T) tetramers, from monomers and dimers. Proline 42-49 acetylcholinesterase (Cartwright blood group) Homo sapiens 112-116 9278446-7 1997 A splice variant from the COLQ gene encodes a proline- rich AChE attachment domain without the collagen domain but does not represent the membrane anchor of the brain tetramer. Proline 46-53 acetylcholinesterase (Cartwright blood group) Homo sapiens 60-64 34531295-4 2021 Here, we found tacrine could disrupt the proper trafficking of proline-rich membrane anchor-linked tetrameric AChE in the endoplasmic reticulum (ER). Proline 63-70 acetylcholinesterase (Cartwright blood group) Homo sapiens 110-114 33196952-5 2021 Acetylcholinesterase activity was inhibited by proline at 1, 3, and 5 mM. Proline 47-54 acetylcholinesterase (Cartwright blood group) Homo sapiens 0-20 33196952-7 2021 Results from Western blot analyses showed that proline at 1 mM after 72 h increased p-NF-kB and decreased acetylcholinesterase immunocontent but did not altered AKT, p-AKT, GSK3beta, and p-GSK3beta. Proline 47-54 acetylcholinesterase (Cartwright blood group) Homo sapiens 106-126 33196952-8 2021 Taken together, the data suggest that high proline levels seems to favor the signaling pathways towards cell proliferation, since acetylcholinesterase, which may act as tumor suppressor, is inhibited by proline. Proline 43-50 acetylcholinesterase (Cartwright blood group) Homo sapiens 130-150 33196952-8 2021 Taken together, the data suggest that high proline levels seems to favor the signaling pathways towards cell proliferation, since acetylcholinesterase, which may act as tumor suppressor, is inhibited by proline. Proline 203-210 acetylcholinesterase (Cartwright blood group) Homo sapiens 130-150