Thermodynamic Analysis of the Geldanamycin-Hsp90 Interaction in a Whole Cell Lysate Using a Mass Spectrometry-Based Proteomics Approach.

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Discovery of Tamoxifen and N-Desmethyl Tamoxifen Protein Targets in MCF-7 Cells Using Large-Scale Protein Folding and Stability Measurements.

P2860

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Thermodynamic Analysis of the Geldanamycin-Hsp90 Interaction in a Whole Cell Lysate Using a Mass Spectrometry-Based Proteomics Approach.

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Thermodynamic Analysis of the ...... try-Based Proteomics Approach.

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Thermodynamic Analysis of the ...... try-Based Proteomics Approach.

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Thermodynamic Analysis of the ...... try-Based Proteomics Approach.

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Thermodynamic Analysis of the ...... try-Based Proteomics Approach.

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Thermodynamic Analysis of the ...... try-Based Proteomics Approach.

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Thermodynamic Analysis of the ...... try-Based Proteomics Approach.

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P1476

Thermodynamic Analysis of the ...... try-Based Proteomics Approach.

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P2093

M Ariel Geer Wallace

http://www.w3.org/2001/XMLSchema#string

Michael C Fitzgerald

http://www.w3.org/2001/XMLSchema#string

Yingrong Xu

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P2860

Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation.

Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent

Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone

Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin

Chaperone ligand-discrimination by the TPR-domain protein Tah1.

Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone.

The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation

Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex

Thermodynamic analysis of protein stability and ligand binding using a chemical modification- and mass spectrometry-based strategy.

ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo.

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s13361-016-1457-2

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1670-1676

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scholarly article

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10.1007/S13361-016-1457-2

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P478

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2016-08-16T00:00:00Z

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1033088254

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27530778

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Thermodynamic Analysis of the Geldanamycin-Hsp90 Interaction in a Whole Cell Lysate Using a Mass Spectrometry-Based Proteomics Approach.

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P2860

Thermodynamic Analysis of the Geldanamycin-Hsp90 Interaction in a Whole Cell Lysate Using a Mass Spectrometry-Based Proteomics Approach.

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P1476

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P2860

P2888

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P2093

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P2888

P304

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P356

P433

P478

P577

P6179

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