GENE - CHEMICAL INTERACTIONS REPORT
Note: Use of the qualifier "multiple interactions" designates that the annotated interaction
is comprised of a complex set of reactions and/or regulatory events, possibly involving
additional chemicals and/or gene products.
Object Symbol | Qualifier | Evidence | With | Reference | Source | Notes | Original Reference(s) | Abcb1a | multiple interactions | EXP | | 6480464 | CTD | [Rifampin metabolite results in decreased activity of ABCB1A protein] which results in decreased abundance of Adenosine Triphosphate | PMID:23685082 | Abcb1a | affects binding | ISO | ABCB1 (Homo sapiens) | 6480464 | CTD | Adenosine Triphosphate binds to ABCB1 protein | PMID:32497533 | Abcb1a | increases hydrolysis | ISO | ABCB1 (Homo sapiens) | 6480464 | CTD | ABCB1 protein results in increased hydrolysis of Adenosine Triphosphate | PMID:18829547 PMID:18955043 PMID:22233293 PMID:2900677 | Abcb1a | multiple interactions | ISO | ABCB1 (Homo sapiens) | 6480464 | CTD | [Cobalt results in increased activity of ABCB1 protein] which results in increased hydrolysis of Adenosine Triphosphate; [Magnesium results in increased activity of ABCB1 protein] which results in increased hydrolysis of Adenosine Triphosphate; [Manganese results in increased activity of ABCB1 protein] which results in increased hydrolysis of Adenosine Triphosphate; ABCB1 protein binds to and results in increased hydrolysis of Adenosine Triphosphate; aurapten promotes the reaction [ABCB1 protein results in increased hydrolysis of Adenosine Triphosphate]; crizotinib promotes the reaction [ABCB1 protein results in increased hydrolysis of Adenosine Triphosphate]; Disulfiram affects the reaction [ABCB1 protein results in increased hydrolysis of Adenosine Triphosphate]; lapatinib promotes the reaction [ABCB1 protein results in increased hydrolysis of Adenosine Triphosphate]; nobiletin promotes the reaction [ABCB1 protein results in increased hydrolysis of Adenosine Triphosphate] | PMID:14978246 PMID:18829547 PMID:18955043 PMID:22233293 PMID:2900677 | | ||||||||||||||||||||||
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