PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
20005217-1	2010	We have shown previously that conjugation of polyethylene glycol (PEG) chains to recombinant human acetylcholinesterase (rHuAChE) results in the extension of its residence time in the circulation of mice and monkeys [1,2].	Polyethylene Glycols	45-64	acetylcholinesterase (Cartwright blood group)	Homo sapiens	99-119	
20005217-1	2010	We have shown previously that conjugation of polyethylene glycol (PEG) chains to recombinant human acetylcholinesterase (rHuAChE) results in the extension of its residence time in the circulation of mice and monkeys [1,2].	Polyethylene Glycols	66-69	acetylcholinesterase (Cartwright blood group)	Homo sapiens	99-119	
20005217-2	2010	By profiling the pharmacokinetic behavior of an array of well-defined hypolysine human mutant AChE molecules following PEGylation, we now determine that the duration of these enzyme forms in the circulation of rhesus macaques correlates with their number of appended PEG moieties, and is influenced by the actual location of the PEG chains at the molecule surface, as well.	Polyethylene Glycols	119-122	acetylcholinesterase (Cartwright blood group)	Homo sapiens	94-98	
20005217-2	2010	By profiling the pharmacokinetic behavior of an array of well-defined hypolysine human mutant AChE molecules following PEGylation, we now determine that the duration of these enzyme forms in the circulation of rhesus macaques correlates with their number of appended PEG moieties, and is influenced by the actual location of the PEG chains at the molecule surface, as well.	Polyethylene Glycols	267-270	acetylcholinesterase (Cartwright blood group)	Homo sapiens	94-98	
20005217-5	2010	Thus, an inverse relationship between anti-AChE antibody production and PEG loading was observed following repeated administration of the different PEGylated hypolysine human AChEs to mice.	Polyethylene Glycols	72-75	acetylcholinesterase (Cartwright blood group)	Homo sapiens	43-47