Allosteric modulation of human P-glycoprotein. Inhibition of transport by preventing substrate translocation and dissociation

Journal of Biological Chemistry

Volumn 278, Issue 20, 2003, Pages 18132-18139

  Maki, Nazli ^a   Hafkemeyer, Peter ^b   Dey, Saibal ^a  

^a Uniformed Services University of the Health Sciences and the Walter Reed National Military Medical Center   (United States)

^b UNIVERSITY OF FREIBURG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELLS; CONFORMATIONS; DRUG PRODUCTS; SUBSTRATES; TUMORS;

DRUG TRANSPORT;

PROTEINS;

CYCLOSPORIN A; FLUPENTIXOL; GLYCOPROTEIN P; GLYCOPROTEIN P INHIBITOR; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY UIC2; PROTEIN INHIBITOR; RAPAMYCIN; SODIUM AZIDE; THIOXANTHENE DERIVATIVE; UNCLASSIFIED DRUG; VANADATE SODIUM; VANADIC ACID; VERAPAMIL; VINCRISTINE; CALCIUM CHANNEL BLOCKING AGENT; CYCLOSPORIN; DOPAMINE RECEPTOR BLOCKING AGENT; ENZYME INHIBITOR; EPITOPE;

ALLOSTERISM; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DRUG MECHANISM; DRUG STRUCTURE; DRUG TRANSPORT; ENZYME SUBSTRATE; FIBROBLAST; HUMAN; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; STRUCTURE ACTIVITY RELATION; TIME SERIES ANALYSIS; ANIMAL; BINDING COMPETITION; BINDING SITE; CELL CULTURE; CELL LINE; CELL MEMBRANE; CELL STRAIN 3T3; CHEMISTRY; DRUG RESISTANCE; ENZYME SPECIFICITY; IMMUNOBLOTTING; METABOLISM; MOUSE; PLASMID; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN TRANSPORT; SPECTROFLUOROMETRY; TIME;

ANIMALIA;

3T3 CELLS; ALLOSTERIC SITE; ANIMALS; BINDING SITES; BINDING, COMPETITIVE; CALCIUM CHANNEL BLOCKERS; CELL LINE; CELL MEMBRANE; CYCLOSPORINE; DOPAMINE ANTAGONISTS; DRUG RESISTANCE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME INHIBITORS; EPITOPES; FLUPENTHIXOL; HUMANS; IMMUNOBLOTTING; MICE; P-GLYCOPROTEIN; PLASMIDS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN TRANSPORT; SPECTROMETRY, FLUORESCENCE; SUBSTRATE SPECIFICITY; TIME FACTORS; TUMOR CELLS, CULTURED; VERAPAMIL;

EID: 0038043182     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M210413200     Document Type: Article

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