Specific aspartate residues in FET3 control high-affinity iron transport in Saccharomyces cerevisiae

Yeast

Volumn 22, Issue 9, 2005, Pages 677-687

  Bonaccorsi di Patti, Maria Carmela ^a   Felice, Maria Rosa ^b   De Domenico, Ivana ^b   Lania, Amalia ^b   Alaleona, Flaminia ^a   Musci, Giovanni ^b  

^a SAPIENZA UNIVERSITY OF ROME   (Italy)

^b UNIVERSITY OF MESSINA   (Italy)

Author keywords

Copper; Fet3; Iron; Site directed mutagenesis

Indexed keywords

AMINO ACID DERIVATIVE; ASPARAGINE; ASPARTIC ACID; CERULOPLASMIN; COPPER; IRON; ISOLEUCINE; MUTANT PROTEIN; PERMEASE; PROTEIN FET3; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; BINDING SITE; CELL MEMBRANE; CONTROLLED STUDY; ELECTRON SPIN RESONANCE; FUNGUS GROWTH; GENE MUTATION; IN VIVO STUDY; IRON TRANSPORT; MEMBRANE BINDING; MOLECULAR MODEL; NONHUMAN; PREDICTION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN MODIFICATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SACCHAROMYCES CEREVISIAE; SENSITIVITY ANALYSIS; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; SURFACE PROPERTY; WILD TYPE;

AMINO ACID SEQUENCE; ASPARTIC ACID; BINDING SITES; CERULOPLASMIN; ELECTRON SPIN RESONANCE SPECTROSCOPY; ION TRANSPORT; IRON; KINETICS; MEMBRANE TRANSPORT PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE ALIGNMENT; STRUCTURE-ACTIVITY RELATIONSHIP; TRANSFORMATION, GENETIC;

SACCHAROMYCES CEREVISIAE;

EID: 23844494399     PISSN: 0749503X     EISSN: None     Source Type: Journal    
DOI: 10.1002/yea.1237     Document Type: Article

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