A single WW domain is the predominant mediator of the interaction between the human ubiquitin-protein ligase Nedd4 and the human epithelial sodium channel

Biochemical Journal

Volumn 361, Issue 3, 2002, Pages 481-488

  Lott, J Shaun ^a   Coddington Lawson, Sarah J ^a   Teesdale Spittle, Paul H ^a   McDonald, Fiona J ^a  

^a UNIVERSITY OF OTAGO   (New Zealand)

Author keywords

BIAcore; ENaC; Surface plasmon resonance

Indexed keywords

AMINO ACIDS; CELLS; GENES; MUTAGENESIS; SALTS; WATER;

WATER BALANCE;

PROTEINS;

ARGININE; SODIUM CHANNEL; SODIUM ION; THREONINE; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE NEDD4; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; COMPLEX FORMATION; CONTROLLED STUDY; ELECTROLYTE BALANCE; ENZYME ACTIVITY; HUMAN; HUMAN TISSUE; HYPERTENSION; LIDDLE SYNDROME; MOLECULAR CLONING; PATHOGENESIS; PREDICTION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION;

AMINO ACID SEQUENCE; AMINO ACIDS; ANIMALS; CALCIUM-BINDING PROTEINS; CLONING, MOLECULAR; DOWN-REGULATION; EPITHELIAL CELLS; HUMANS; LIGASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SODIUM CHANNELS; SURFACE PLASMON RESONANCE; TIME FACTORS; UBIQUITIN-PROTEIN LIGASES;

EID: 0036471394     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3610481     Document Type: Article

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