Tyrosine 112 Is essential for organic cation transport by the plasma membrane monoamine transporter

Biochemistry

Volumn 49, Issue 36, 2010, Pages 7839-7846

  Ho, Horace T B ^a   Wang, Joanne ^a  

^a UNIVERSITY OF WASHINGTON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; AMINO ACIDS; AROMATIC COMPOUNDS; BINDING ENERGY; BRAIN; CELL MEMBRANES; PHOSPHATASES; POSITIVE IONS; RESTORATION;

1-METHYL-4-PHENYLPYRIDINIUM; AROMATIC RESIDUES; AROMATIC SUBSTITUTIONS; BINDING AFFINITIES; CELL SURFACE EXPRESSION; DETAILED KINETICS; MEMBRANE LOCALIZATION; MOLECULAR DETERMINANTS; OPTIMAL INTERACTIONS; ORGANIC CATION TRANSPORTERS; ORGANIC CATION TRANSPORTS; ORGANIC CATIONS; PLASMA MEMBRANES; SOLUTE CARRIERS; SUBSTRATE RECOGNITION; SUBSTRATE RECOGNITION SITES; TRANS-MEMBRANE DOMAINS; TRANSMEMBRANE DOMAIN; TRANSPORT ACTIVITY; TRANSPORT VELOCITY; TRYPTOPHAN RESIDUES;

SUBSTRATES;

ALANINE; DOPAMINE; MUTANT PROTEIN; ORGANIC CATION TRANSPORTER; PHENYLALANINE; PROTEIN INTERACTING WITH PROTEIN KINASE C; SEROTONIN; TRYPTOPHAN; TYROSINE; VESICULAR MONOAMINE TRANSPORTER; EQUILIBRATIVE NUCLEOSIDE TRANSPORTER;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CATION TRANSPORT; CELL LINE; CELL MEMBRANE TRANSPORT; CELL SURFACE; CONFOCAL MICROSCOPY; CONTROLLED STUDY; MOLECULAR RECOGNITION; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN SECONDARY STRUCTURE; SEQUENCE ALIGNMENT; TRANSPORT KINETICS; ANIMAL; BINDING SITE; CELL CULTURE; CHEMISTRY; DOG; GENETICS; HUMAN; KINETICS; METABOLISM; MOLECULAR GENETICS; STRUCTURE ACTIVITY RELATION; TRANSPORT AT THE CELLULAR LEVEL;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; BIOLOGICAL TRANSPORT; CELLS, CULTURED; DOGS; EQUILIBRATIVE NUCLEOSIDE TRANSPORT PROTEINS; HUMANS; KINETICS; MICROSCOPY, CONFOCAL; MOLECULAR SEQUENCE DATA; ORGANIC CATION TRANSPORT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; TYROSINE;

EID: 77956416114     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100560q     Document Type: Article

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