Modeling and experimental assessment of a buried Leu–Ile mutation in dengue envelope domain III-Reference-Cited by-同舟云学术

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Modeling and experimental assessment of a buried Leu–Ile mutation in dengue envelope domain III

Published:2016-02 Issue:1 Volume:471 Page:163-168
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Kulkarni Manjiri R.,Numoto Nobutaka,Ito Nobutoshi,Kuroda Yutaka

Funder

Medical Research Institute of Tokyo Medical and Dental University

Japanese government (MEXT)

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference22 articles.

1. Global spread and persistence of dengue;Kyle;Annu. Rev. Microbiol.,2008

2. Antibodies determine virulence in dengue;Halstead;Ann. N. Y. Acad. Sci.,2009

3. Ultrastructural characterization and three-dimensional architecture of replication sites in dengue virus-infected mosquito cells;Junjhon;J. Virol.,2014

4. Monoclonal antibodies that bind to domain III of dengue virus E glycoprotein are the most efficient blockers of virus adsorption to Vero cells;Crill;J. Virol.,2001

5. Bacterially expressed and refolded envelope protein (domain III) of dengue virus type-4 binds heparan sulfate;Pattnaik;J. Chromatogr. B Anal. Technol. Biomed. Life Sci.,2007

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1. Direct Analysis of Mitochondrial Damage Caused by Misfolded/Destabilized Proteins;International Journal of Molecular Sciences;2022-08-31

2. DENV-3 precursor membrane (prM) glycoprotein enhances E protein immunogenicity and confers protection against DENV-2 infections in a murine model;Human Vaccines & Immunotherapeutics;2020-10-29

3. A Multi-Perspective Review on Dengue Research;Current Drug Targets;2019-11-12

4. Folding of the Ig-Like Domain of the Dengue Virus Envelope Protein Analyzed by High-Hydrostatic-Pressure NMR at a Residue-Level Resolution;Biomolecules;2019-07-26

5. Hydrophobic surface residues can stabilize a protein through improved water–protein interactions;The FEBS Journal;2019-06-17

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