PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 25794283-0 2015 Molecular dynamics simulations of acylpeptide hydrolase bound to chlorpyrifosmethyl oxon and dichlorvos. fospirate 65-88 acylaminoacyl-peptide hydrolase Homo sapiens 34-55 25794283-4 2015 We report a computational study of APH bound to chlorpyrifosmethyl oxon and dichlorvos. fospirate 48-71 acylaminoacyl-peptide hydrolase Homo sapiens 35-38 25794283-6 2015 Molecular dynamics simulations were also performed to explore the conformational changes between the chlorpyrifosmethyl oxon and dichlorvos bound to APH, which indicated that the structural feature of chlorpyrifosmethyl oxon binding in APH permitted partial opening of the beta-propeller fold and allowed the chlorpyrifosmethyl oxon to easily enter the catalytic site. fospirate 101-124 acylaminoacyl-peptide hydrolase Homo sapiens 149-152 25794283-6 2015 Molecular dynamics simulations were also performed to explore the conformational changes between the chlorpyrifosmethyl oxon and dichlorvos bound to APH, which indicated that the structural feature of chlorpyrifosmethyl oxon binding in APH permitted partial opening of the beta-propeller fold and allowed the chlorpyrifosmethyl oxon to easily enter the catalytic site. fospirate 101-124 acylaminoacyl-peptide hydrolase Homo sapiens 236-239 25794283-6 2015 Molecular dynamics simulations were also performed to explore the conformational changes between the chlorpyrifosmethyl oxon and dichlorvos bound to APH, which indicated that the structural feature of chlorpyrifosmethyl oxon binding in APH permitted partial opening of the beta-propeller fold and allowed the chlorpyrifosmethyl oxon to easily enter the catalytic site. fospirate 201-224 acylaminoacyl-peptide hydrolase Homo sapiens 149-152 25794283-6 2015 Molecular dynamics simulations were also performed to explore the conformational changes between the chlorpyrifosmethyl oxon and dichlorvos bound to APH, which indicated that the structural feature of chlorpyrifosmethyl oxon binding in APH permitted partial opening of the beta-propeller fold and allowed the chlorpyrifosmethyl oxon to easily enter the catalytic site. fospirate 201-224 acylaminoacyl-peptide hydrolase Homo sapiens 236-239 25794283-6 2015 Molecular dynamics simulations were also performed to explore the conformational changes between the chlorpyrifosmethyl oxon and dichlorvos bound to APH, which indicated that the structural feature of chlorpyrifosmethyl oxon binding in APH permitted partial opening of the beta-propeller fold and allowed the chlorpyrifosmethyl oxon to easily enter the catalytic site. fospirate 201-224 acylaminoacyl-peptide hydrolase Homo sapiens 149-152 25794283-6 2015 Molecular dynamics simulations were also performed to explore the conformational changes between the chlorpyrifosmethyl oxon and dichlorvos bound to APH, which indicated that the structural feature of chlorpyrifosmethyl oxon binding in APH permitted partial opening of the beta-propeller fold and allowed the chlorpyrifosmethyl oxon to easily enter the catalytic site. fospirate 201-224 acylaminoacyl-peptide hydrolase Homo sapiens 236-239