D Liebowitz
Harvard University
16 Papers
240 Citations
D Liebowitz is an academic researcher from Harvard University. The author has contributed to research in topics: Epstein–Barr virus & Vimentin. The author has an hindex of 8, co-authored 10 publications.
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Papers
Epstein-Barr virus latent infection membrane protein alters the human B-lymphocyte phenotype: deletion of the amino terminus abolishes activity.
David Q.-H. Wang,D Liebowitz,F. Wang,C Gregory,A Rickinson,Richard S. Larson,Timothy A. Springer,Elliott Kieff +7 more
TL;DR: EBV LMP appears to be a mediator of EBV effects on B-cell transformation and may result in more effective T-cell immune surveillance, since cytoskeletal association may be integral to LMP activity.
406
Orientation and patching of the latent infection membrane protein encoded by Epstein-Barr virus.
TL;DR: Studies of the plasma membrane localization and orientation of LMP by protease digestion of live cells and by immunofluorescence indicated that LMP is present in patches in the cell plasma membrane.
243
An Epstein-Barr virus transforming protein associates with vimentin in lymphocytes.
TL;DR: The basis of LMP patching in EBV-infected, transformed lymphocytes is examined and data indicate that LMP is associated with the cytoskeletal protein vimentin, which is a transducer of an LMP transmembrane effect in lymphoproliferation.
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Epstein-Barr virus latent infection membrane protein increases vimentin expression in human B-cell lines.
TL;DR: Vimentin induction was reproduced by the expression of the single EBV gene which encodes the latent infection membrane protein (LMP), and the interaction between vimentin and LMP observed in immunofluorescent colocalization and cell fractionation studies is of particular interest.
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Epstein-Barr virus latent membrane protein: induction of B-cell activation antigens and membrane patch formation does not require vimentin.
D Liebowitz,Elliott Kieff +1 more
TL;DR: Encoding LMP in an EBV-positive Burkitt's lymphoma cell line, Daudi, indicates that LMP can form plasma membrane patches and induce B-lymphocyte activation independent of vimentin association.
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