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The Fe/S assembly protein IscU behaves as a substrate for the molecular chaperone Hsc66 from Escherichia coli.
Silberg, J J; Hoff, K G; Tapley, T L; Vickery, L E.
Affiliation
  • Silberg JJ; Department of Physiology and Biophysics, University of California, Irvine, California 92697, USA.
J Biol Chem ; 276(3): 1696-700, 2001 Jan 19.
Article in En | MEDLINE | ID: mdl-11053447
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Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Adenosine Triphosphatases / Molecular Chaperones / HSP70 Heat-Shock Proteins / Escherichia coli Proteins / Escherichia coli / Iron-Sulfur Proteins Language: En Journal: J Biol Chem Year: 2001 Document type: Article Affiliation country: Estados Unidos Country of publication: Estados Unidos
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Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Adenosine Triphosphatases / Molecular Chaperones / HSP70 Heat-Shock Proteins / Escherichia coli Proteins / Escherichia coli / Iron-Sulfur Proteins Language: En Journal: J Biol Chem Year: 2001 Document type: Article Affiliation country: Estados Unidos Country of publication: Estados Unidos