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Identification of Compounds Targeting Hepatitis B Virus Core Protein Dimerization through a Split Luciferase Complementation Assay
Author(s) -
Xiafei Wei,
Chun-Yang Gan,
Jing Cui,
Yingying Luo,
Xue-Fei Cai,
Yuan Yi,
Jing Shen,
Zhiying Li,
Wenlu Zhang,
Quanxin Long,
Yuan Hu,
Juan Chen,
Ni Tang,
Haitao Guo,
Ailong Huang,
Jieli Hu
Publication year - 2018
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.01302-18
Subject(s) - luciferase , complementation , virology , protein fragment complementation assay , hepatitis b virus , identification (biology) , biology , virus , chemistry , microbiology and biotechnology , computational biology , biochemistry , transfection , gene , phenotype , botany
The capsid of the hepatitis B virus is an attractive antiviral target for developing therapies against chronic hepatitis B infection. Currently available core protein allosteric modulators (CpAMs) mainly affect one of the two major types of protein-protein interactions involved in the process of capsid assembly, namely, the interaction between the core dimers.

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