The Protein Kinase Gcn2p Mediates Sodium Toxicity in Yeast

Journal of Biological Chemistry

Volumn 276, Issue 33, 2001, Pages 30753-30760

  Goossens, Alain ^a,c   Dever, Thomas E ^b   Pascual Ahuir, Amparo ^a   Serrano, Ramon ^a  

^a Ciudad Politécnica de la Innovación   (Spain)

^b EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH AND HUMAN DEVELOPMENT   (United States)

^c DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOSYNTHESIS; CELLS; ENZYMES; MUTAGENESIS; TOXICITY;

PHOSPHORYLATION;

YEAST;

CPC2 PROTEIN; GCN1 PROTEIN; GCN2P PROTEIN; GCN3 PROTEIN; GCN4P PROTEIN; INITIATION FACTOR 2; INITIATION FACTOR 2ALPHA; PROTEIN; PROTEIN GCD[7-201]; PROTEIN KINASE; PROTEIN KINASE GCN2P; SODIUM CHLORIDE; SODIUM ION; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; AMINO ACID; BISPHOSPHOADENYLATE 3' NUCLEOTIDASE; BISPHOSPHOADENYLATE 3'-NUCLEOTIDASE; DNA BINDING PROTEIN; ELONGATION FACTOR; FUNGAL PROTEIN; GCN1 PROTEIN, S CEREVISIAE; GCN2 PROTEIN, S CEREVISIAE; GCN3 PROTEIN, S CEREVISIAE; GUANINE NUCLEOTIDE EXCHANGE FACTOR; NUCLEOTIDASE; PROTEIN SERINE THREONINE KINASE; SACCHAROMYCES CEREVISIAE PROTEIN; SERINE; SODIUM;

AMINO ACID TRANSPORT; ARTICLE; DRUG SENSITIVITY; EUKARYOTE; FUNGAL GENE; FUNGAL STRAIN; FUNGUS GROWTH; GCN4 GENE; GENE MUTATION; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN MALNUTRITION; PROTEIN PHOSPHORYLATION; PROTEIN SYNTHESIS; SALT STRESS; TRANSLATION INITIATION; TRANSLATION REGULATION; YEAST; DRUG EFFECT; GENETICS; METABOLISM; PHOSPHORYLATION; PHYSIOLOGY; SACCHAROMYCES CEREVISIAE;

EUKARYOTA; FUNGI;

AMINO ACIDS; DNA-BINDING PROTEINS; EUKARYOTIC INITIATION FACTOR-2; EUKARYOTIC INITIATION FACTOR-2B; FUNGAL PROTEINS; NUCLEOTIDASES; PEPTIDE ELONGATION FACTORS; PHOSPHORYLATION; PROTEIN BIOSYNTHESIS; PROTEIN KINASES; PROTEIN-SERINE-THREONINE KINASES; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SERINE; SODIUM;

EID: 0035903194     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M102960200     Document Type: Article

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