PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 29310276-3 2018 Apyrase and acetylcholinesterase (AChE), as selective elements, are used to recognize adenosine 5"-triphosphate (ATP) and acetylcholine (ACh), respectively. Adenosine Triphosphate 86-111 acetylcholinesterase (Cartwright blood group) Homo sapiens 12-32 29310276-3 2018 Apyrase and acetylcholinesterase (AChE), as selective elements, are used to recognize adenosine 5"-triphosphate (ATP) and acetylcholine (ACh), respectively. Adenosine Triphosphate 86-111 acetylcholinesterase (Cartwright blood group) Homo sapiens 34-38 29310276-3 2018 Apyrase and acetylcholinesterase (AChE), as selective elements, are used to recognize adenosine 5"-triphosphate (ATP) and acetylcholine (ACh), respectively. Adenosine Triphosphate 113-116 acetylcholinesterase (Cartwright blood group) Homo sapiens 12-32 29310276-3 2018 Apyrase and acetylcholinesterase (AChE), as selective elements, are used to recognize adenosine 5"-triphosphate (ATP) and acetylcholine (ACh), respectively. Adenosine Triphosphate 113-116 acetylcholinesterase (Cartwright blood group) Homo sapiens 34-38 16429571-0 2005 ATP induces the post-synaptic gene expression in neuron-neuron synapses: Transcriptional regulation of AChE catalytic subunit. Adenosine Triphosphate 0-3 acetylcholinesterase (Cartwright blood group) Homo sapiens 103-107 16518518-5 2006 In addition, during the course of these excitatory processes and inhibition of AChE, a high rate of ATP consumption, coupled with the inhibition of oxidative phosphorylation, compromise the cell"s ability to maintain its energy levels and excessive amounts of ROS and RNS may be generated. Adenosine Triphosphate 100-103 acetylcholinesterase (Cartwright blood group) Homo sapiens 79-83 16429571-2 2005 The synaptic ATP induces post-synaptic gene transcription during the formation and maintenance of vertebrate neuromuscular junction (nmj) via a mitogen-activaton protein (MAP) kinase signaling pathway and subsequently activates acetylcholinesterase (AChE) and acetylcholine receptor (AChR) genes. Adenosine Triphosphate 13-16 acetylcholinesterase (Cartwright blood group) Homo sapiens 228-248 16429571-2 2005 The synaptic ATP induces post-synaptic gene transcription during the formation and maintenance of vertebrate neuromuscular junction (nmj) via a mitogen-activaton protein (MAP) kinase signaling pathway and subsequently activates acetylcholinesterase (AChE) and acetylcholine receptor (AChR) genes. Adenosine Triphosphate 13-16 acetylcholinesterase (Cartwright blood group) Homo sapiens 250-254 16429571-6 2005 By using a human AChE promoter tagged with a luciferase-reporter gene, the transcriptional regulation of AChE gene by ATP could be monitored. Adenosine Triphosphate 118-121 acetylcholinesterase (Cartwright blood group) Homo sapiens 17-21 16429571-6 2005 By using a human AChE promoter tagged with a luciferase-reporter gene, the transcriptional regulation of AChE gene by ATP could be monitored. Adenosine Triphosphate 118-121 acetylcholinesterase (Cartwright blood group) Homo sapiens 105-109 8326133-1 1993 Vesicles released from human E by Ca(2+)-loading, ATP-depletion, or storage are enriched in several glycosylphosphatidylinositol-anchored proteins such as acetylcholinesterase (AchE) and decay-accelerating factor (DAF). Adenosine Triphosphate 50-53 acetylcholinesterase (Cartwright blood group) Homo sapiens 155-175 15143516-2 2003 The activity of acetylcholinesterase in suspension of cells compounds is 9.8 +/- 0.2 mumol of tiocholinbromide/mg protein/hour and is reduced under influence of exogenous ATP, NO2-, H2O2 and Triton X-100. Adenosine Triphosphate 171-174 acetylcholinesterase (Cartwright blood group) Homo sapiens 16-36 6885744-6 1983 The vesicles showed similar characteristics to those generated by ATP depletion; their diameter is 150-200 nm and they are enriched with acetylcholinesterase activity. Adenosine Triphosphate 66-69 acetylcholinesterase (Cartwright blood group) Homo sapiens 137-157 6266109-4 1981 The obtained results seem to suggest that the changes in the native conformation of membrane catalytic proteins resulted from cryodamage are responsible for the lowered aChE activity; the primary cause of increase Na+, K+-ATPase activity is due to the changes in the permeability and integrity of erythrocyte membrane, which are followed by the greater accessibility of the substrate (ATP) to the enzyme. Adenosine Triphosphate 222-225 acetylcholinesterase (Cartwright blood group) Homo sapiens 169-173 33145964-0 2020 Interaction of amyloid beta with humanin and acetylcholinesterase is modulated by ATP. Adenosine Triphosphate 82-85 acetylcholinesterase (Cartwright blood group) Homo sapiens 45-65 33145964-4 2020 We found that binding of either HN or AChE to Abeta is not affected by heparan sulfate, while ATP, thought to reduce misfolding of Abeta, weakened interactions between AChE and Abeta but strengthened those between Abeta and HN. Adenosine Triphosphate 94-97 acetylcholinesterase (Cartwright blood group) Homo sapiens 168-172 33145964-5 2020 Using media from either A549 or H1299 lung cancer cells, we observed that more HN was bound to Abeta upon addition of ATP, while levels of AChE in a complex with Abeta were decreased by ATP addition to A549 cell media. Adenosine Triphosphate 186-189 acetylcholinesterase (Cartwright blood group) Homo sapiens 139-143 33145964-6 2020 Exogenous addition of ATP to either A549 or H1299 cell media increased interactions of endogenous HN with Abeta to a comparable extent despite differences in AChE expression in the two cell lines, and this was correlated with decreased binding of exogenously added HN to Abeta. Adenosine Triphosphate 22-25 acetylcholinesterase (Cartwright blood group) Homo sapiens 158-162