Disruption of PML-Associated Nuclear Bodies by IE1 Correlates with Efficient Early Stages of Viral Gene Expression and DNA Replication in Human Cytomegalovirus Infection
Author:
Publisher
Elsevier BV
Subject
Virology
Reference64 articles.
1. Disruption of PML subnuclear domains by the acidic IE1 protein of human cytomegalovirus is mediated through interaction with PML and may modulate a RING finger-dependent cryptic transactivator function of PML;Ahn;Mol. Cell. Biol.,1998
2. The major immediate early proteins IE1 and IE2 of human cytomegalovirus co-localize with and disrupt PML-associated nuclear bodies at very early times in infected permissive cells;Ahn;J. Virol.,1997
3. The human cytomegalovirus IE2 and UL112-113 proteins accumulate in viral DNA replication compartments that initiate from the periphery of promyelocytic leukemia protein (PML)-associated nuclear bodies;Ahn;J. Virol.,1999
4. Identification of a novel nuclear domain;Ascoli;J. Cell Biol.,1991
5. Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix-associated PML bodies;Carvalho;J. Cell Biol.,1995
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