Allosteric modulation bypasses the requirement for ATP hydrolysis in regenerating low affinity transition state conformation of human P-glycoprotein

Journal of Biological Chemistry

Volumn 281, Issue 16, 2006, Pages 10769-10777

  Maki, Nazli ^a   Moitra, Karobi ^a   Ghosh, Pratiti ^a   Dey, Saibal ^a  

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

Author keywords

[No Author keywords available]

Indexed keywords

DISSOCIATION; DRUG PRODUCTS; HYDROLYSIS; NITROGEN COMPOUNDS; SUBSTRATES;

AFFINITY TRANSITION; ATP HYDROLYSIS; SUBSTRATE TRANSLOCATION;

PROTEINS;

ADENOSINE TRIPHOSPHATE; FLUOROALUMINATE; FLUPENTIXOL; GLYCOPROTEIN P; NUCLEOTIDE; THIOXANTHENE; VANADIC ACID;

ALLOSTERISM; ANIMAL CELL; ARTICLE; BINDING AFFINITY; CATALYSIS; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ALLOSTERIC SITE; ANIMALS; AZIDES; BINDING SITES; CATALYTIC DOMAIN; CELL LINE; CELL MEMBRANE; FLUPENTHIXOL; HUMANS; HYDROLYSIS; INSECTS; LIGANDS; MOLECULAR CONFORMATION; P-GLYCOPROTEIN; P-GLYCOPROTEINS; PRAZOSIN; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; THIOXANTHENES; TIME FACTORS; TRYPSIN; VANADATES;

EID: 33744964346     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M512579200     Document Type: Article

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