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  2. Details for: In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis.
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In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis. [electronic resource]

By:
  • Obermann, W M
Contributor(s):
  • Sondermann, H
  • Russo, A A
  • Pavletich, N P
  • Hartl, F U
Producer: 19981221Description: 901-10 p. digitalISSN:
  • 0021-9525
Subject(s):
  • Adenosine Diphosphate -- metabolism
  • Adenosine Triphosphatases -- metabolism
  • Adenosine Triphosphate -- metabolism
  • Benzoquinones
  • Cell Division -- physiology
  • Chaperonins -- genetics
  • Crystallography
  • DNA Topoisomerases, Type II -- metabolism
  • Enzyme Inhibitors -- pharmacology
  • Fungal Proteins -- genetics
  • Gene Expression Regulation, Fungal
  • HSP90 Heat-Shock Proteins -- chemistry
  • Heat-Shock Proteins -- genetics
  • Humans
  • Hydrolysis
  • Lactams, Macrocyclic
  • Magnesium -- metabolism
  • Mutagenesis -- physiology
  • Protein Structure, Tertiary
  • Quinones -- pharmacology
  • Saccharomyces cerevisiae Proteins
  • Yeasts -- chemistry
Online resources:
  • Available from publisher's website
In: The Journal of cell biology vol. 143
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Publication Type: Journal Article

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In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis.

APA

Obermann W. M., Sondermann H., Russo A. A., Pavletich N. P. & Hartl F. U. (19981221). In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis. : The Journal of cell biology.

Chicago

Obermann W M, Sondermann H, Russo A A, Pavletich N P and Hartl F U. 19981221. In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis. : The Journal of cell biology.

Harvard

Obermann W. M., Sondermann H., Russo A. A., Pavletich N. P. and Hartl F. U. (19981221). In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis. : The Journal of cell biology.

MLA

Obermann W M, Sondermann H, Russo A A, Pavletich N P and Hartl F U. In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis. : The Journal of cell biology. 19981221.

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