Overexpression, Purification, and Crystallization of the DNA Binding and Dimerization Domains of the Epstein-Barr Virus Nuclear Antigen 1
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference18 articles.
1. Replication of latent Epstein-Barr virus genomes in Raji cells
2. Functional domains of Epstein-Barr virus nuclear antigen EBNA-1
3. Separation of the complex DNA binding domain of EBNA-1 into DNA recognition and dimerization subdomains of novel structure
4. MERLOT, an integrated package of computer programs for the determination of crystal structures by molecular replacement
5. Overproduction, purification, and characterization of EBNA1, the origin binding protein of Epstein-Barr virus.
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1. Modelling the structure of full-length Epstein–Barr virus nuclear antigen 1;Virus Genes;2014-07-11
2. Combinatory use of cell-free protein expression, limited proteolysis and mass spectrometry for the high-throughput protein domain identification;Biochemical and Biophysical Research Communications;2014-02
3. Small molecule and peptide-mediated inhibition of Epstein-Barr virus nuclear antigen 1 dimerization;Biochemical and Biophysical Research Communications;2012-07
4. EBNA1-Mediated Recruitment of a Histone H2B Deubiquitylating Complex to the Epstein-Barr Virus Latent Origin of DNA Replication;PLoS Pathogens;2009-10-16
5. Kinetically driven refolding of the hyperstable EBNA1 origin DNA-binding dimeric β-barrel domain into amyloid-like spherical oligomers;Proteins: Structure, Function, and Bioinformatics;2007-08-06
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