The Herpesvirus Nuclear Egress Complex Component, UL31, Can Be Recruited to Sites of DNA Damage Through Poly-ADP Ribose Binding

MLA

Maxwell R Sherry, et al. “The Herpesvirus Nuclear Egress Complex Component, UL31, Can Be Recruited to Sites of DNA Damage Through Poly-ADP Ribose Binding.” Scientific Reports, vol. 7, no. 1, May 2017, pp. 1–18. EBSCOhost, widgets.ebscohost.com/prod/customlink/proxify/proxify.php?count=1&encode=0&proxy=&find_1=&replace_1=&target=https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&scope=site&db=edsair&AN=edsair.doi.dedup.....e97100fa1ce62e3e6d88284f9689f02b&authtype=sso&custid=ns315887.

APA

Maxwell R Sherry, Arash Nassiri, Renée L. Finnen, Thomas J. M. Hay, Michael A. Gulak, & Bruce W. Banfield. (2017). The Herpesvirus Nuclear Egress Complex Component, UL31, Can Be Recruited to Sites of DNA Damage Through Poly-ADP Ribose Binding. Scientific Reports, 7(1), 1–18.

Chicago

Maxwell R Sherry, Arash Nassiri, Renée L. Finnen, Thomas J. M. Hay, Michael A. Gulak, and Bruce W. Banfield. 2017. “The Herpesvirus Nuclear Egress Complex Component, UL31, Can Be Recruited to Sites of DNA Damage Through Poly-ADP Ribose Binding.” Scientific Reports 7 (1): 1–18. http://widgets.ebscohost.com/prod/customlink/proxify/proxify.php?count=1&encode=0&proxy=&find_1=&replace_1=&target=https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&scope=site&db=edsair&AN=edsair.doi.dedup.....e97100fa1ce62e3e6d88284f9689f02b&authtype=sso&custid=ns315887.