Proline residues in transmembrane segment IV are critical for activity, expression and targeting of the Na+/H+ exchanger isoform 1

Biochemical Journal

Volumn 379, Issue 1, 2004, Pages 31-38

  Slepkov, Emily R ^a   Chow, Signy ^a   Lemieux, M Joanne ^a   Fliegel, Larry ^a  

^a UNIVERSITY OF ALBERTA   (Canada)

Author keywords

Cation transport; Membrane; Na+ H+ exchanger; Proline; Transmembrane segment IV

Indexed keywords

BIOLOGICAL MEMBRANES; CELLS; MUTAGENESIS; PH EFFECTS; PROTEINS;

MAMMALIAN CELLS; PROLINE RESIDUES; TRANSMEMBRANE SEGMENTS;

BIOCHEMISTRY;

ALANINE; CYSTEINE; GLYCINE; MEMBRANE PROTEIN; MUTANT PROTEIN; PROLINE; SODIUM PROTON EXCHANGE PROTEIN 1;

ANIMAL CELL; ARTICLE; CELL MEMBRANE; CONTROLLED STUDY; IMMUNOBLOTTING; IMMUNOCYTOCHEMISTRY; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; PROTEIN TARGETING; SITE DIRECTED MUTAGENESIS; WILD TYPE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; CELL LINE; CRICETINAE; CRICETULUS; DNA, COMPLEMENTARY; HUMANS; MEMBRANE PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION, MISSENSE; POINT MUTATION; PROLINE; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SODIUM-HYDROGEN ANTIPORTER; STRUCTURE-ACTIVITY RELATIONSHIP; TRANSFECTION;

ANIMALIA; MAMMALIA;

EID: 1842866228     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20030884     Document Type: Article

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