Functional importance of three basic residues clustered at the cytosolic interface of transmembrane helix 15 in the multidrug and organic anion transporter MRP1 (ABCC1)

Journal of Biological Chemistry

Volumn 281, Issue 1, 2006, Pages 43-50

  Conseil, Gwenaëlle ^a   Deeley, Roger G ^a   Cole, Susan P C ^a,b  

^a QUEEN S UNIVERSITY   (Canada)

^b Department of Cancer Biology ^*  (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOLOGICAL MEMBRANES; CELLS; DRUG PRODUCTS; NEGATIVE IONS; PLASMAS;

CYTOSOLIC INTERFACE; GLUTATHIONE; MULTIDRUG RESISTANCE; MUTATION; ORGANIC ANION;

PROTEINS;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ARGININE; GLUTAMIC ACID; GLUTATHIONE; LEUKOTRIENE C4; LYSINE; MULTIDRUG RESISTANCE PROTEIN 1; ORGANIC ANION TRANSPORTER; VANADIC ACID; 8 AZIDOADENOSINE DIPHOSPHATE; 8-AZIDOADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; AZIDE; DIAGNOSTIC AGENT; DRUG DERIVATIVE; ESTRADIOL; MULTIDRUG RESISTANCE PROTEIN; MULTIDRUG RESISTANCE-ASSOCIATED PROTEIN 1; PHOSPHORUS; TRITIUM;

ANION TRANSPORT; ARTICLE; CELL MEMBRANE; CONFOCAL LASER MICROSCOPY; CONTROLLED STUDY; ENZYME ACTIVITY; HUMAN; HUMAN CELL; IMMUNOBLOTTING; KIDNEY CELL; KINETICS; MEMBRANE POTENTIAL; PHOTOAFFINITY LABELING; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN TRANSPORT; RESIDUE ANALYSIS; SEQUENCE ALIGNMENT; AMINO ACID SEQUENCE; CELL LINE; CHEMISTRY; CYTOLOGY; CYTOSOL; ENZYME ACTIVE SITE; GENETICS; KIDNEY; METABOLISM; MOLECULAR GENETICS; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ARGININE; AZIDES; CATALYTIC DOMAIN; CELL LINE; CYTOSOL; ESTRADIOL; HUMANS; KIDNEY; LEUKOTRIENE C4; LYSINE; MOLECULAR SEQUENCE DATA; MULTIDRUG RESISTANCE-ASSOCIATED PROTEINS; MUTAGENESIS, SITE-DIRECTED; PHOSPHORUS RADIOISOTOPES; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP; TRITIUM; VANADATES;

EID: 31844446751     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M510143200     Document Type: Article

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