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Mediation of Epstein-Barr virus EBNA2 transactivation by recombination signal-binding protein J kappa.
TLDR
Here, CBF1 was purified and was found to directly interact with EBNA2, identical to a protein thought to be involved in immunoglobulin gene rearrangement, RBPJ kappa, which bound to sites in the EBV C-promoter and in the CD23 promoter. Expand
The Epstein-Barr virus immortalizing protein EBNA-2 is targeted to DNA by a cellular enhancer-binding protein.
TLDR
It is demonstrated that EBNA-2 is targeted to the Epstein-Barr virus latency C promoter (Cp) through interaction with a cellular DNA binding protein designated Cp binding factor 1 (CBF1) and mutated sequence CNGTGGGAA was unable to mediate EB NA-2 transactivation. Expand
Three unrelated viral transforming proteins (vIRF, EBNA2, and E1A) induce the MYC oncogene through the interferon-responsive PRF element by using different transcription coadaptors.
TLDR
It is shown that induction of the MYC protooncogene is required for cell transformation by vIRF, and that vIRf increases MYC transcription up to 15-fold through specific promoter interactions at an ISRE sequence called the plasmacytoma repressor factor (PRF) element. Expand
Sequence and Functional Analysis of EBNA-LP and EBNA2 Proteins from Nonhuman Primate Lymphocryptoviruses
TLDR
There is strong structural and functional conservation among the simian EBNA-LP homologues, including a highly conserved Wp EBNA promoter with strong conservation of upstream activating sequences important for Wp transcriptional regulation. Expand
Human Cytomegalovirus Infection Causes Degradation of Sp100 Proteins That Suppress Viral Gene Expression
TLDR
It is shown that Sp100 proteins are lost largely in the late stages of HCMV infection, suggesting that the IE1-induced disruption of PML NBs is not sufficient for the complete loss of Sp 100 proteins. Expand
Transcriptional activation of the Epstein-Barr virus latency C promoter after 5-azacytidine treatment: evidence that demethylation at a single CpG site is crucial
TLDR
The CBF2 binding activity is shown to be methylation sensitive and crucial to EBNA-2-mediated activation of the Cp in the Epstein-Barr Virus. Expand
Conserved Regions in the Epstein-Barr Virus Leader Protein Define Distinct Domains Required for Nuclear Localization and Transcriptional Cooperation with EBNA2
TLDR
EBNA-LP has a bipartite nuclear localization signal and that efficient nuclear localization is essential for EBNA2 cooperativity function, and Interestingly, EBNA- LP with only a single repeat localized exclusively to the cytoplasm, providing an explanation for why this isoform has no activity. Expand
Mediation of Epstein–Barr virus EBNA‐LP transcriptional coactivation by Sp100
TLDR
It is found that EBNA‐LP interacts with the promyelocytic leukemia nuclear body (PML NB)‐associated protein Sp 100 and displaces Sp100 and heterochromatin protein 1α (HP1α) from PML NBs and suggests that Sp100 is a major mediator of EBNA•LP coactivation. Expand
Contribution of conserved amino acids in mediating the interaction between EBNA2 and CBF1/RBPJk
TLDR
Overall, the data indicated that CR5 contributes to an optimal interaction, perhaps through stabilizing contacts, while CR6 forms a crucial interface with CBF1/RBPJk. Expand
Detection of pathogenic elephant endotheliotropic herpesvirus in routine trunk washes from healthy adult Asian elephants (Elephas maximus) by use of a real-time quantitative polymerase chain reaction
TLDR
EEHV1 was shed in the trunk secretions of healthy Asian elephants and may provide a mode of transmission for this virus, which may be useful for the diagnosis, treatment, and management of EEHV 1-associated disease and the overall management of captive elephant populations. Expand
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