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Comparative studies of the low-resolution structure of two p23 co-chaperones for Hsp90 identified in Plasmodium falciparum genome

  • Published:2018-03 Issue: Volume:108 Page:193-204
  • ISSN:0141-8130
  • Container-title:International Journal of Biological Macromolecules
  • language:en
  • Short-container-title:International Journal of Biological Macromolecules

Author:

Silva Noeli S.M.,Seraphim Thiago V.,Minari Karine,Barbosa Leandro R.S.,Borges Júlio C.

Funder

São Paulo Research Foundation

CNPq

CNPq Research Fellow

FAPESP

Publisher

Elsevier BV

Subject

Molecular Biology,General Medicine,Biochemistry,Structural Biology

Reference59 articles.

1. Evolution and function of diverse Hsp90 homologs and cochaperone proteins;Johnson;Biochim. Biophys. Acta − Mol. Cell Res.,1823

2. Hsp90: breaking the symmetry;Mayer;Mol. Cell.,2015

3. An interaction network predicted from public data as a discovery tool: application to the Hsp90 molecular chaperone machine;Echeverría;PLoS One,2011

4. Substrate binding drives large-scale conformational changes in the hsp90 molecular chaperone;Street;Mol. Cell.,2011

5. The Hsp90 ensemble: coordinated Hsp90-cochaperone complexes regulate diverse cellular processes;Schwenkert;Nat. Struct. Mol. Biol.,2014

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