19F NMR Reveals Multiple Conformations at the Dimer Interface of the Nonstructural Protein 1 Effector Domain from Influenza A Virus-Reference-Cited by-同舟云学术

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19F NMR Reveals Multiple Conformations at the Dimer Interface of the Nonstructural Protein 1 Effector Domain from Influenza A Virus

Published:2014-04 Issue:4 Volume:22 Page:515-525
ISSN:0969-2126
Container-title:Structure
language:en
Short-container-title:Structure

Author:

Aramini James M.,Hamilton Keith,Ma Li-Chung,Swapna G.V.T.,Leonard Paul G.,Ladbury John E.,Krug Robert M.,Montelione Gaetano T.

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference67 articles.

1. Specific fluorine labeling of the HyHEL10 antibody affects antigen binding and dynamics;Acchione;Biochemistry,2012

2. Preparation of protein samples for NMR structure, function, and small-molecule screening studies;Acton;Methods Enzymol.,2011

3. Dynamics of the S1S2 glutamate binding domain of GluR2 measured using 19F NMR spectroscopy;Ahmed;J. Biol. Chem.,2007

4. Dimer interface of the effector domain of non-structural protein 1 from influenza A virus: an interface with multiple functions;Aramini;J. Biol. Chem.,2011

5. Contribution of NS1 effector domain dimerization to influenza A virus replication and virulence;Ayllon;J. Virol.,2012

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