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Yisel A Rivera-Molina, Francisco Puerta Martínez, Qiyi Tang
Yisel A Rivera-Molina, Francisco Puerta Martínez, Qiyi Tang, Department of Microbiology/RCMI Program, Ponce School of Medicine and Health Sciences, Ponce, PR 00732-7004, United States
Author contributions: Rivera-Molina YA, Martínez FP and Tang Q contributed to this review.
Supported by A Pilot Grant from the National Center for Research Resources (G12 RR003050); and the National Institute on Minority Health and Health Disparities (8G12MD007579-27), both of the National Institutes of Health (To Tang Q), an American Cancer Society Grant (117448-RSG-09-289-01-MPC) (To Tang Q), and NIH/NCRR U54RR022762 (To Tang Q)
Correspondence to: Qiyi Tang, MD, PhD, Department of Microbiology/RCMI Program, Ponce School of Medicine and Health Sciences, PO Box 7004, Ponce, PR 00732, United States. firstname.lastname@example.org
Telephone: +1-787- 8402575 Fax: +1-787- 8415159
Received: January 27, 2013 Revised: May 31, 2013 Accepted: May 31, 2013 Published online: August 12, 2013
Core tip: We, for the first time, discussed the function of nuclear domain 10 (ND10) as a nuclear structure. Although the ND10 components, especially Promyelocytic Leukemia bodies, Speckled Protein of 100 kDa and death domain-associated protein, have been widely investigated for their roles in viral gene expression and viral replication, individual virus interacts with ND10 differentially as we summarized up in this review. This review is expected to guide readers especially virologists and cell biologists to understanding the interaction of ND10 with viruses.