Acute regulation of mouse AE2 anion exchanger requires isoform-specific amino acid residues from most of the transmembrane domain

Journal of Physiology

Volumn 584, Issue 1, 2007, Pages 59-73

  Stewart, A K ^a,b   Kurschat, C E ^a,b   Vaughan jones, R D ^c   Shmukler, B E ^a,b   Alper, S L ^a,b  

^a HARVARD MEDICAL SCHOOL   (United States)

^b BETH ISRAEL DEACONESS MEDICAL CENTER   (United States)

^c UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; AMMONIA; ANION EXCHANGE PROTEIN AE2; ANION EXCHANGE PROTEIN SLC4A2; ANTIPORTER; MEMBRANE PROTEIN; POLYPEPTIDE; UNCLASSIFIED DRUG; AE1 POLYPEPTIDE; AE2 POLYPEPTIDE; AMIDE; CALMIDAZOLIUM;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CHIMERA; CONTROLLED STUDY; FEMALE; GENE EXPRESSION REGULATION; NONHUMAN; NUCLEOTIDE SEQUENCE; OOCYTE; PH; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; REGULATORY MECHANISM; SENSITIVITY ANALYSIS; XENOPUS; AMINO ACID SUBSTITUTION; ANION EXCHANGE; CARBOXY TERMINAL SEQUENCE; CELL PH; CELLULAR PARAMETERS; CHLORIDE TRANSPORT; EXTRACELLULAR LOOP; TRANSMEMBRANE DOMAIN; XENOPUS LAEVIS;

AMINO ACID SEQUENCE; ANIMALS; ANION EXCHANGE PROTEIN 1, ERYTHROCYTE; ANION TRANSPORT PROTEINS; ANTIPORTERS; CELL MEMBRANE; CODON, NONSENSE; FEMALE; HYDROGEN-ION CONCENTRATION; IMIDAZOLES; MICE; OOCYTES; PEPTIDES; PROTEIN ISOFORMS; PROTEIN STRUCTURE, TERTIARY; QUATERNARY AMMONIUM COMPOUNDS; RECOMBINANT FUSION PROTEINS; XENOPUS LAEVIS;

EID: 34848927532     PISSN: 00223751     EISSN: 14697793     Source Type: Journal    
DOI: 10.1113/jphysiol.2007.136119     Document Type: Article

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