Cysteines introduced into extracellular loops 1 and 4 of human P-glycoprotein that are close only in the open conformation spontaneously form a disulfide bond that inhibits drug efflux and ATPase activity. [electronic resource]
Producer: 20150128Description: 24749-58 p. digitalISSN:- 1083-351X
- ATP Binding Cassette Transporter, Subfamily B -- chemistry
- Adenosine Triphosphatases -- metabolism
- Adenosine Triphosphate -- metabolism
- Animals
- Binding Sites -- genetics
- Cell Line
- Cysteine -- chemistry
- Disulfides -- chemistry
- Dithiothreitol -- pharmacology
- Drug Resistance, Multiple -- drug effects
- Glycoside Hydrolases -- metabolism
- HEK293 Cells
- Humans
- Hydrolysis
- Immunoblotting
- Models, Molecular
- Mutation
- Pharmaceutical Preparations -- metabolism
- Protein Conformation
- Protein Structure, Secondary
- Protein Structure, Tertiary
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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