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The anticancer drug AUY922 generates a proteomics fingerprint that is highly conserved among structurally diverse Hsp90 inhibitors.
High affinity binding of Hsp90 is triggered by multiple discrete segments of its kinase clients.
Pierce, Stephanie
Fluoride Poisoning
Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37.
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Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37.
Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37. J Biol Chem. 2003 Oct 03; 278(40):38117-20.
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subject areas
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
authors with profiles
Robert Matts