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Eric Johannsen

Researcher at University of Wisconsin-Madison

Publications -  70
Citations -  4911

Eric Johannsen is an academic researcher from University of Wisconsin-Madison. The author has contributed to research in topics: Epstein–Barr virus & Lytic cycle. The author has an hindex of 34, co-authored 65 publications receiving 4403 citations. Previous affiliations of Eric Johannsen include Brigham and Women's Hospital & Harvard University.

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Proteins of purified Epstein-Barr virus

TL;DR: Mature Epstein-Barr virus was purified from the culture medium of infected lymphocytes made functionally conditional for Zta activation of lytic replication by an in-frame fusion with a mutant estrogen receptor.
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Epstein–Barr virus and virus human protein interaction maps

TL;DR: The authors' EBV–EBV interactome map is enriched for interactions among proteins in the same evolutionary class, and human proteins targeted by EBV proteins were enriched for highly connected or “hub” proteins and for proteins with relatively short paths to all other proteins inThe human interactome network.
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The Epstein-Barr virus nuclear antigen 2 transactivator is directed to response elements by the J kappa recombination signal binding protein.

TL;DR: Purified or recombinant in vitro-translated J kappa binds to the MNYYGTGGGAA EBNA-2 response element sequence and interacts with EBNA, but does not bind to theJ kappa 1 heptamer recombination signal sequence.
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Interpreting cancer genomes using systematic host network perturbations by tumour virus proteins

TL;DR: It is shown that systematic analyses of host targets of viral proteins can identify cancer genes with a success rate on a par with their identification through functional genomics and large-scale cataloguing of tumour mutations, to increase the specificity of cancer gene identification.
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Epstein-Barr virus nuclear protein 2 transactivation of the latent membrane protein 1 promoter is mediated by J kappa and PU.1.

TL;DR: EBNA-2 transactivation of the LMP-1 promoter is dependent on interaction with at least two distinct sequence-specific DNA-binding proteins, J kappa and PU.1.