Localizing Conformational Hinges by NMR: Where Do Hepatitis B Virus Core Proteins Adapt for Capsid Assembly?-Reference-Cited by-同舟云学术

Localizing Conformational Hinges by NMR: Where Do Hepatitis B Virus Core Proteins Adapt for Capsid Assembly?

Published:2018-04-06 Issue:11 Volume:19 Page:1336-1340
ISSN:1439-4235
Container-title:ChemPhysChem
language:en
Short-container-title:ChemPhysChem

Author:

Lecoq Lauriane¹^ORCID,Wang Shishan¹,Wiegand Thomas²^ORCID,Bressanelli Stéphane³^ORCID,Nassal Michael⁴^ORCID,Meier Beat H.²^ORCID,Böckmann Anja¹^ORCID

Affiliation:

1. Molecular Microbiology and Structural Biochemistry; Labex Ecofect; UMR 5086 CNRS/; Université de Lyon; 69367 Lyon France

2. Physical Chemistry; ETH Zurich; 8093 Zurich Switzerland

3. Institute for Integrative Biology of the Cell (I2BC); CEA; CNRS; Univ Paris Sud; Université Paris-Saclay 91198 Gif sur Yvette France

4. University Hospital Freiburg; Dept. of Medicine II/Molecular Biology; Medical Center; University of Freiburg; Hugstetter Straße 55 79106 Freiburg Germany

Funder

Swiss National Science Foundation

French National Research Agency

LABEX ECOFECT

Federal Ministry for Economic Affairs and Energy

Publisher

Wiley

Subject

Physical and Theoretical Chemistry,Atomic and Molecular Physics, and Optics

Reference34 articles.

1. Physical Principles in the Construction of Regular Viruses

2. Quantitative method for the assignment of hinge and shear mechanism in protein domain movements

3. Hepatitis B virus nucleocapsid assembly: primary structure requirements in the core protein

4. A recombinant hepatitis B core antigen polypeptide with the protamine-like domain deleted self-assembles into capsid particles but fails to bind nucleic acids

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