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Volumn 278, Issue 40, 2003, Pages 38117-38120
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Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37
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Author keywords
[No Author keywords available]
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Indexed keywords
CELLS;
ENZYMES;
MODULATION;
SWITCHING;
PHOSPHORYLATION;
BIOCHEMISTRY;
ADENOSINE TRIPHOSPHATE;
ALANINE;
CASEIN KINASE II;
CELL CYCLE PROTEIN 37;
CHAPERONE;
GLUTAMINE;
HEAT SHOCK PROTEIN 90;
PROTEIN KINASE;
RECOMBINANT PROTEIN;
SERINE;
UNCLASSIFIED DRUG;
AMINO ACID SUBSTITUTION;
ARTICLE;
CONFORMATIONAL TRANSITION;
ENZYME BINDING;
MUTATION;
PRIORITY JOURNAL;
PROTEIN BINDING;
PROTEIN PHOSPHORYLATION;
QUANTITATIVE ANALYSIS;
RABBIT;
RETICULOCYTE LYSATE;
ADENOSINE TRIPHOSPHATE;
ALKALINE PHOSPHATASE;
ANIMALS;
CELL CYCLE PROTEINS;
CHAPERONINS;
DROSOPHILA PROTEINS;
GLUTAMIC ACID;
HSP90 HEAT-SHOCK PROTEINS;
HUMANS;
K562 CELLS;
MOLECULAR CHAPERONES;
MOLYBDENUM;
MUTAGENESIS, SITE-DIRECTED;
MUTATION;
PHOSPHORYLATION;
POINT MUTATION;
PROTEIN BINDING;
PROTEIN CONFORMATION;
PROTEIN FOLDING;
PROTEIN STRUCTURE, TERTIARY;
RABBITS;
RECOMBINANT PROTEINS;
SERINE;
SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;
MAMMALIA;
ORYCTOLAGUS CUNICULUS;
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EID: 0141755381
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.C300330200 Document Type: Article |
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Times cited : (98)
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References (18)
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