Pub. Date : 2015 Mar 18
PMID : 25794283
8 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Molecular dynamics simulations of acylpeptide hydrolase bound to chlorpyrifosmethyl oxon and dichlorvos. | fospirate | acylaminoacyl-peptide hydrolase | Homo sapiens |
| 2 | We report a computational study of APH bound to chlorpyrifosmethyl oxon and dichlorvos. | fospirate | acylaminoacyl-peptide hydrolase | Homo sapiens |
| 3 | 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 | acylaminoacyl-peptide hydrolase | Homo sapiens |
| 4 | 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 | acylaminoacyl-peptide hydrolase | Homo sapiens |
| 5 | 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 | acylaminoacyl-peptide hydrolase | Homo sapiens |
| 6 | 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 | acylaminoacyl-peptide hydrolase | Homo sapiens |
| 7 | 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 | acylaminoacyl-peptide hydrolase | Homo sapiens |
| 8 | 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 | acylaminoacyl-peptide hydrolase | Homo sapiens |