PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 21414769-9 2012 Kuguacin J also inhibited the incorporation of [125I]-iodoarylazidoprazosin into P-gp in a concentration-dependent manner, indicating that kuguacin J directly interacts with the drug-substrate-binding site on P-gp. azidoprazosin 47-75 phosphoglycolate phosphatase Homo sapiens 81-85 26820614-7 2016 P-gp ATPase assays and photo-cross-linking with [(125)I]iodoarylazidoprazosin confirmed that transport and biochemical properties of P-gp chimeras were similar to those of wild-type P-gp, although differences in drug binding were detected when human and mouse transmembrane domains were combined. azidoprazosin 56-77 phosphoglycolate phosphatase Homo sapiens 133-137 26820614-7 2016 P-gp ATPase assays and photo-cross-linking with [(125)I]iodoarylazidoprazosin confirmed that transport and biochemical properties of P-gp chimeras were similar to those of wild-type P-gp, although differences in drug binding were detected when human and mouse transmembrane domains were combined. azidoprazosin 56-77 phosphoglycolate phosphatase Homo sapiens 133-137 24865254-6 2014 A set of in vitro experiments including kinase activity and cell-based transport assays and photolabeling of P-gp and ABCG2 with a transport substrate, [(125)I]-iodoarylazido-prazosin (IAAP), were carried out in isolated membranes to evaluate the potency of the derivatives to inhibit the function of ABC drug transporters and BCR-ABL kinase. azidoprazosin 161-183 phosphoglycolate phosphatase Homo sapiens 109-113 21414769-9 2012 Kuguacin J also inhibited the incorporation of [125I]-iodoarylazidoprazosin into P-gp in a concentration-dependent manner, indicating that kuguacin J directly interacts with the drug-substrate-binding site on P-gp. azidoprazosin 47-75 phosphoglycolate phosphatase Homo sapiens 209-213 16729976-3 2006 Unlike most other Pgp modulators, the cis isomer of flupentixol [cis-(Z)-flupentixol] facilitates interaction of Pgp with its transport-substrate [125I]iodoarylazidoprazosin (or [125I]IAAP), yet inhibits transport. azidoprazosin 152-173 phosphoglycolate phosphatase Homo sapiens 113-116 16960658-12 2007 THC stimulated P-gp ATPase activity and inhibited the incorporation of [(125)I]-iodoarylazidoprazosin (IAAP) into P-gp in a concentration-dependent manner. azidoprazosin 71-101 phosphoglycolate phosphatase Homo sapiens 114-118 7682843-5 1993 Labeling experiments with the photoactivatable P-gp ligands iodoarylazidoprazosin and azidopine indicate a strong reduction in binding of these photoactivatable probes to the mutant P-gps (1F, 3F) as compared to their wild-type counterparts (1S,3S). azidoprazosin 60-81 phosphoglycolate phosphatase Homo sapiens 47-51 10350482-2 1999 The rate of ATP hydrolysis by Pgp and photoaffinity labeling of Pgp with the substrate analogue [125I]iodoarylazidoprazosin ([125I]IAAP) are modulated by each isomer in an opposite manner, suggesting different mechanisms for the inhibitory effect on drug transport. azidoprazosin 96-123 phosphoglycolate phosphatase Homo sapiens 30-33 10350482-2 1999 The rate of ATP hydrolysis by Pgp and photoaffinity labeling of Pgp with the substrate analogue [125I]iodoarylazidoprazosin ([125I]IAAP) are modulated by each isomer in an opposite manner, suggesting different mechanisms for the inhibitory effect on drug transport. azidoprazosin 96-123 phosphoglycolate phosphatase Homo sapiens 64-67 9530286-4 1998 Furthermore, photoaffinity labeling of P-gp with the substrate analogue [125I]iodoarylazidoprazosin (IAAP) was inhibited by all three inhibitors. azidoprazosin 72-99 phosphoglycolate phosphatase Homo sapiens 39-43 9530286-4 1998 Furthermore, photoaffinity labeling of P-gp with the substrate analogue [125I]iodoarylazidoprazosin (IAAP) was inhibited by all three inhibitors. azidoprazosin 101-105 phosphoglycolate phosphatase Homo sapiens 39-43