PMC:6194691 / 58251-58944 JSONTXT

{"project":"MyTest","denotations":[{"id":"30340614-1968065-30706119","span":{"begin":192,"end":195},"obj":"1968065"},{"id":"30340614-7910961-30706119","span":{"begin":192,"end":195},"obj":"7910961"},{"id":"30340614-24624364-30706119","span":{"begin":192,"end":195},"obj":"24624364"},{"id":"30340614-19325113-30706119","span":{"begin":192,"end":195},"obj":"19325113"},{"id":"30340614-19325113-30706120","span":{"begin":296,"end":299},"obj":"19325113"}],"namespaces":[{"prefix":"_base","uri":"https://www.uniprot.org/uniprot/testbase"},{"prefix":"UniProtKB","uri":"https://www.uniprot.org/uniprot/"},{"prefix":"uniprot","uri":"https://www.uniprot.org/uniprotkb/"}],"text":"It is believed by many that P-glycoprotein, a transmembrane protein, acts by removing its lipophilic substrates from the lipid layer of the cell membrane, depositing them back into the blood [210–213]. Its structure has been investigated in both substrate-free and inhibitor bound conformations [213] and binding sites for various of its many substrates identified within the large cavity seen in the substrate-free conformation. It is the binding and hydrolysis of ATP that provides the motive force leading to a large conformational change in the P-glycoprotein and the transfer and expulsion of its substrates. There are two ATP binding sites located on the cytoplasmic side of the protein."}

{"project":"2_test","denotations":[{"id":"30340614-1968065-30706119","span":{"begin":192,"end":195},"obj":"1968065"},{"id":"30340614-7910961-30706119","span":{"begin":192,"end":195},"obj":"7910961"},{"id":"30340614-24624364-30706119","span":{"begin":192,"end":195},"obj":"24624364"},{"id":"30340614-19325113-30706119","span":{"begin":192,"end":195},"obj":"19325113"},{"id":"30340614-19325113-30706120","span":{"begin":296,"end":299},"obj":"19325113"}],"text":"It is believed by many that P-glycoprotein, a transmembrane protein, acts by removing its lipophilic substrates from the lipid layer of the cell membrane, depositing them back into the blood [210–213]. Its structure has been investigated in both substrate-free and inhibitor bound conformations [213] and binding sites for various of its many substrates identified within the large cavity seen in the substrate-free conformation. It is the binding and hydrolysis of ATP that provides the motive force leading to a large conformational change in the P-glycoprotein and the transfer and expulsion of its substrates. There are two ATP binding sites located on the cytoplasmic side of the protein."}