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Epstein-Barr virus replication factor

Hydrophobic interactions between nonpolar amino-acid residues and the bases of DNA contribute to the function of DNA binding proteins through conformational effects and direct interactions with the DNA nucleotides. Direct evidence of the role of hydrophobic interactions in DNA-protein complexes has been found for T7 RNA polymerase [69, 70], Epstein-Barr virus replication factor EBNAl [71], and bovine papillomavirus helicase El [72, 73], for example. [Pg.192]

Chaudhuri B, Xu H, Todorov 1, Dutta A, Yates JL (2001) Human DNA replication initiation factors, ORC and MCM, associate with oriP of Epstein-Barr virus. Proc Natl Acad Sci USA 98 10085-10089... [Pg.312]

See other pages where Epstein-Barr virus replication factor is mentioned: [Pg.22]    [Pg.627]    [Pg.248]    [Pg.226]    [Pg.57]    [Pg.35]    [Pg.199]    [Pg.183]    [Pg.699]    [Pg.341]    [Pg.237]   
See also in sourсe #XX -- [ Pg.192 ]



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