PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 29451128-2 2018 The biosensor was fabricated with poly(ethylene glycol) (PEG) hydrogel microarrays that entrapped acetylcholinesterase (AChE) and quantum dots (QDs) as fluorescence reporters. Polyethylene Glycols 34-55 acetylcholinesterase (Cartwright blood group) Homo sapiens 98-118 15000836-1 2003 To determine whether the efficacy of entry and action of antisense oligonucleotides (AS-ODN) on hematopoietic stem cells in vitro could be improved by the addition of polyethylene glycol (PEG), a molecule of PEG was bound to AS- or sense-acetylcholinesterase (AS-ACHE or S-ACHE). Polyethylene Glycols 167-186 acetylcholinesterase (Cartwright blood group) Homo sapiens 263-267 15000836-1 2003 To determine whether the efficacy of entry and action of antisense oligonucleotides (AS-ODN) on hematopoietic stem cells in vitro could be improved by the addition of polyethylene glycol (PEG), a molecule of PEG was bound to AS- or sense-acetylcholinesterase (AS-ACHE or S-ACHE). Polyethylene Glycols 167-186 acetylcholinesterase (Cartwright blood group) Homo sapiens 273-277 15000836-4 2003 PEG-AS-ACHE induced higher colony numbers and greatly increased megakaryocyte (MK) formation when compared with PEG and AS-ACHE added separately to the culture. Polyethylene Glycols 0-3 acetylcholinesterase (Cartwright blood group) Homo sapiens 7-11 15000836-5 2003 In addition, differentials of the CFU-GEMMs indicated there was a direct relationship between MK number and PEG-AS-ACHE concentration. Polyethylene Glycols 108-111 acetylcholinesterase (Cartwright blood group) Homo sapiens 115-119 2546574-0 1989 The inhibitory effects of polyoxyethylene detergents on human erythrocyte acetylcholinesterase and Ca2+ + Mg2+ ATPase. Polyethylene Glycols 26-41 acetylcholinesterase (Cartwright blood group) Homo sapiens 74-94 11463350-0 2001 Effect of chemical modification of recombinant human acetylcholinesterase by polyethylene glycol on its circulatory longevity. Polyethylene Glycols 77-96 acetylcholinesterase (Cartwright blood group) Homo sapiens 53-73 29451128-2 2018 The biosensor was fabricated with poly(ethylene glycol) (PEG) hydrogel microarrays that entrapped acetylcholinesterase (AChE) and quantum dots (QDs) as fluorescence reporters. Polyethylene Glycols 57-60 acetylcholinesterase (Cartwright blood group) Homo sapiens 98-118 29451128-2 2018 The biosensor was fabricated with poly(ethylene glycol) (PEG) hydrogel microarrays that entrapped acetylcholinesterase (AChE) and quantum dots (QDs) as fluorescence reporters. Polyethylene Glycols 57-60 acetylcholinesterase (Cartwright blood group) Homo sapiens 120-124 29451128-5 2018 PEG hydrogel microarray entrapping QD-decorated Ag@Silica and AChE was prepared via photopatterning process. Polyethylene Glycols 0-3 acetylcholinesterase (Cartwright blood group) Homo sapiens 62-66 17045722-0 2007 Polyethylene-glycol conjugated recombinant human acetylcholinesterase serves as an efficacious bioscavenger against soman intoxication. Polyethylene Glycols 0-19 acetylcholinesterase (Cartwright blood group) Homo sapiens 49-69 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 17932038-0 2007 Controlled concealment of exposed clearance and immunogenic domains by site-specific polyethylene glycol attachment to acetylcholinesterase hypolysine mutants. Polyethylene Glycols 85-104 acetylcholinesterase (Cartwright blood group) Homo sapiens 119-139 17932038-3 2007 Series of multiple Lys-Ala mutants of human acetylcholinesterase were prepared allowing the generation of homogenous and well defined polyethylene-glycol conjugated AChEs with either one, two, three, four, or five appended polyethylene glycol (PEG) moieties/molecule. Polyethylene Glycols 134-153 acetylcholinesterase (Cartwright blood group) Homo sapiens 44-64 17932038-3 2007 Series of multiple Lys-Ala mutants of human acetylcholinesterase were prepared allowing the generation of homogenous and well defined polyethylene-glycol conjugated AChEs with either one, two, three, four, or five appended polyethylene glycol (PEG) moieties/molecule. Polyethylene Glycols 223-242 acetylcholinesterase (Cartwright blood group) Homo sapiens 44-64 17932038-3 2007 Series of multiple Lys-Ala mutants of human acetylcholinesterase were prepared allowing the generation of homogenous and well defined polyethylene-glycol conjugated AChEs with either one, two, three, four, or five appended polyethylene glycol (PEG) moieties/molecule. Polyethylene Glycols 244-247 acetylcholinesterase (Cartwright blood group) Homo sapiens 44-64 17932038-5 2007 Hypolysine acetylcholinesterases (AChEs) carrying the same number of PEGs, and therefore with identical masses, allowed us to demonstrate that circulatory longevity correlates with the predicted extent of concealment of the AChE surface. Polyethylene Glycols 69-73 acetylcholinesterase (Cartwright blood group) Homo sapiens 34-38 17932038-6 2007 Furthermore, circulatory profiles of high number and low number PEG-AChEs differing in their sialic acid contents demonstrate a direct relationship between PEG loading and the effective seclusion of AChE from the hepatic asialoglycoprotein receptor clearance system. Polyethylene Glycols 64-67 acetylcholinesterase (Cartwright blood group) Homo sapiens 68-72 17932038-6 2007 Furthermore, circulatory profiles of high number and low number PEG-AChEs differing in their sialic acid contents demonstrate a direct relationship between PEG loading and the effective seclusion of AChE from the hepatic asialoglycoprotein receptor clearance system. Polyethylene Glycols 156-159 acetylcholinesterase (Cartwright blood group) Homo sapiens 68-72 17932038-7 2007 Finally, an inverse relationship is found between the extent of PEG loading and the ability of the human acetylcholinesterase to elicit specific anti-HuAChE antibodies. Polyethylene Glycols 64-67 acetylcholinesterase (Cartwright blood group) Homo sapiens 105-125 16801396-0 2006 Comparison of polyethylene glycol-conjugated recombinant human acetylcholinesterase and serum human butyrylcholinesterase as bioscavengers of organophosphate compounds. Polyethylene Glycols 14-33 acetylcholinesterase (Cartwright blood group) Homo sapiens 63-83