Insights on the structural dynamics of Leishmania braziliensis Hsp90 molecular chaperone by small angle X-ray scattering-Reference-Cited by-同舟云学术

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Insights on the structural dynamics of Leishmania braziliensis Hsp90 molecular chaperone by small angle X-ray scattering

Published:2017-04 Issue: Volume:97 Page:503-512
ISSN:0141-8130
Container-title:International Journal of Biological Macromolecules
language:en
Short-container-title:International Journal of Biological Macromolecules

Author:

Seraphim Thiago V.,Silva Kelly P.,Dores-Silva Paulo R.,Barbosa Leandro R.S.,Borges Júlio C.

Funder

FAPESP

CNPq

Publisher

Elsevier BV

Subject

Molecular Biology,General Medicine,Biochemistry,Structural Biology

Reference43 articles.

1. Hsp90: a chaperone for protein folding and gene regulation;Zhao;Biochem. Cell Biol.,2005

2. Regulation of protein turnover by heat shock proteins;Bozaykut;Free Radic. Biol. Med.,2014

3. The middle domain of Hsp90 acts as a discriminator between different types of client proteins;Hawle;Mol. Cell. Biol.,2006

4. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone;Prodromou;Cell,1997

5. Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions;Meyer;Mol. Cell,2003

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3. Design, Synthesis and In Vitro Investigation of Novel Basic Celastrol Carboxamides as Bio-Inspired Leishmanicidal Agents Endowed with Inhibitory Activity against Leishmania Hsp90;Biomolecules;2021-01-05

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