Title : Ulixertinib (BVD-523) antagonizes ABCB1- and ABCG2-mediated chemotherapeutic drug resistance.

Pub. Date : 2018 Dec

PMID : 30431011






9 Functional Relationships(s)
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1 Ulixertinib (BVD-523) antagonizes ABCB1- and ABCG2-mediated chemotherapeutic drug resistance. ulixertinib ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens
2 The results showed that ulixertinib, at non-toxic concentrations, significantly reversed ATP-binding cassette subfamily B member 1 (ABCB1)- and ATP-binding cassette subfamily G member 2 (ABCG2)-mediated MDR. ulixertinib ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens
3 The results showed that ulixertinib, at non-toxic concentrations, significantly reversed ATP-binding cassette subfamily B member 1 (ABCB1)- and ATP-binding cassette subfamily G member 2 (ABCG2)-mediated MDR. ulixertinib ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens
4 Similarly, in ABCG2-overexpressing cells, ulixertinib inhibited the efflux activity of ABCG2 and reversed resistance to substrate anticancer drugs. ulixertinib ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens
5 Similarly, in ABCG2-overexpressing cells, ulixertinib inhibited the efflux activity of ABCG2 and reversed resistance to substrate anticancer drugs. ulixertinib ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens
6 Mechanistic investigations revealed that ulixertinib stimulated the ATPase activity of both ABCB1 and ABCG2 in a concentration-dependent manner, and the in silico docking study predicted that ulixertinib could interact with the substrate-binding sites of both ABCB1 and ABCG2. ulixertinib ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens
7 Mechanistic investigations revealed that ulixertinib stimulated the ATPase activity of both ABCB1 and ABCG2 in a concentration-dependent manner, and the in silico docking study predicted that ulixertinib could interact with the substrate-binding sites of both ABCB1 and ABCG2. ulixertinib ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens
8 Mechanistic investigations revealed that ulixertinib stimulated the ATPase activity of both ABCB1 and ABCG2 in a concentration-dependent manner, and the in silico docking study predicted that ulixertinib could interact with the substrate-binding sites of both ABCB1 and ABCG2. ulixertinib ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens
9 Our finding provides a clue into a novel treatment strategy: a combination of ulixertinib with anticancer drugs to attenuate MDR mediated by ABCB1 or ABCG2 in cancer cells overexpressing these transporters. ulixertinib ATP binding cassette subfamily G member 2 (Junior blood group) Homo sapiens