Identification and Structural Characterization of an Intermediate in the Folding of the Measles Virus X Domain-Reference-Cited by-同舟云学术

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Identification and Structural Characterization of an Intermediate in the Folding of the Measles Virus X Domain

Published:2016-05 Issue:20 Volume:291 Page:10886-10892
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Bonetti Daniela,Camilloni Carlo,Visconti Lorenzo,Longhi Sonia,Brunori Maurizio,Vendruscolo Michele,Gianni Stefano

Funder

Ministero dell'Istruzione, dell'Università e della Ricerca

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference38 articles.

1. Im7 folding mechanism: misfolding on a path to the native state;Capaldi;Nat. Struct. Biol,2002

2. Ultrarapid mixing experiments reveal that Im7 folds via an on-pathway intermediate;Capaldi;Nat. Struct. Biol,2001

3. Structural characterization of a misfolded intermediate populated during the folding process of a PDZ domain;Gianni;Nat. Struct. Mol. Biol,2010

4. Transient folding intermediates characterized by protein engineering;Matouschek;Nature,1990

5. An integrated kinetic analysis of intermediates and transition states in protein folding reactions;Parker;J. Mol. Biol,1995

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3. Structural Dynamics of the C-terminal X Domain of Nipah and Hendra Viruses Controls the Attachment to the C-terminal Tail of the Nucleocapsid Protein;Journal of Molecular Biology;2022-05

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