High affinity binding between Hsp70 and the C-terminal domain of the measles virus nucleoprotein requires an Hsp40 co-chaperone-Reference-Cited by-同舟云学术

High affinity binding between Hsp70 and the C-terminal domain of the measles virus nucleoprotein requires an Hsp40 co-chaperone

Published:2009 Issue: Volume: Page:n/a-n/a
ISSN:0952-3499
Container-title:Journal of Molecular Recognition
language:en
Short-container-title:J. Mol. Recognit.

Author:

Couturier Marie,Buccellato Matt,Costanzo Stéphanie,Bourhis Jean-Marie,Shu Yaoling,Nicaise Magali,Desmadril Michel,Flaudrops Christophe,Longhi Sonia,Oglesbee Michael

Publisher

Wiley

Subject

Molecular Biology,Structural Biology

Reference73 articles.

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3. Efficient Hsp90-independent in vitro activation by Hsc70 and Hsp40 of duck hepatitis B virus reverse transcriptase, an assumed Hsp90 client protein;Beck;J. Biol. Chem.,2003

4. Mapping alpha-helical induced folding within the intrinsically disordered C-terminal domain of the measles virus nucleoprotein by site-directed spin-labeling EPR spectroscopy;Belle;Proteins,2008

5. Characterization of measles polypeptides by monoclonal antibodies;Birrer;Virology,1981

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