Comparative analysis of the ATP-binding sites of Hsp90 by nucleotide affinity cleavage: a distinct nucleotide specificity of the C-terminal ATP-binding site (Q28205041)

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scientific article (publication date: June 2003)

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English	Comparative analysis of the ATP-binding sites of Hsp90 by nucleotide affinity cleavage: a distinct nucleotide specificity of the C-terminal ATP-binding site	scientific article (publication date: June 2003)

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Comparative analysis of the ATP-binding sites of Hsp90 by nucleotide affinity cleavage: a distinct nucleotide specificity of the C-terminal ATP-binding site (English)

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Timothy A J Haystead

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Timothy A J Haystead

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author name string

Csaba Soti

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Akos Vermes

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Péter Csermely

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publication date

June 2003

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270

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11

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2421-8

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The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Hsp90: chaperoning signal transduction

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ATP-binding properties of human Hsp90.

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

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Radicicol leads to selective depletion of Raf kinase and disrupts K-Ras-activated aberrant signaling pathway

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A Nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90. N-terminal nucleotide binding unmasks a C-terminal binding pocket

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Evidence that the novobiocin-sensitive ATP-binding site of the heat shock protein 90 (hsp90) is necessary for its autophosphorylation

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10.1046/J.1432-1033.2003.03610.X

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