The function of the endocytic scaffold protein Pan1p depends on multiple domains

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Volumn 5, Issue 12, 2004, Pages 963-978

  Miliaras, Nicholas B ^a   Park, Jin Hyouk ^a   Wendland, Beverly ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Actin; EH domain; End3p; Endocytosis; Pan1p; Prk1p; Proline rich domain; Scaffold; Yeast

Indexed keywords

ACTIN; DIMER; OLIGOMER; PROTEIN KINASE; RECEPTOR PROTEIN;

ACTIN FILAMENT; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL VIABILITY; CONTROLLED STUDY; ENDOCYTOSIS; IMMUNOPRECIPITATION; INTERNALIZATION; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; SACCHAROMYCES CEREVISIAE; TWO HYBRID SYSTEM; WILD TYPE; YEAST; YEAST CELL;

ACTINS; ENDOCYTOSIS; FUNGAL PROTEINS; GENES, REPORTER; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, TERTIARY; PROTEIN-SERINE-THREONINE KINASES; RECEPTOR PROTEIN-TYROSINE KINASES; RECEPTORS, G-PROTEIN-COUPLED; RECEPTORS, MATING FACTOR; RECEPTORS, PHEROMONE; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 8844231083     PISSN: 13989219     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2004.00238.x     Document Type: Article

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