Xiao Tong

The Bovine Papillomavirus E6 Protein Binds to the LD Motif Repeats of Paxillin and Blocks Its Interaction with Vinculin and the Focal Adhesion Kinase*

R. Salgia, P. Howley, Jian-Liang Li, 1997, The Journal of Biological Chemistry.

The bovine papillomavirus E6 oncoprotein interacts with paxillin and disrupts the actin cytoskeleton.

P. Howley, X. Tong, Xiao Tong, 1997, Proceedings of the National Academy of Sciences of the United States of America.

The Epstein-Barr virus nuclear protein 2 acidic domain forms a complex with a novel cellular coactivator that can interact with TFIIE

E. Kieff, R. Drapkin, G. Mosialos, 1995, Molecular and cellular biology.

The Epstein-Barr virus nuclear antigen 2 transactivator is directed to response elements by the J kappa recombination signal binding protein.

E. Kieff, E. Johannsen, S. Grossman, 1994, Proceedings of the National Academy of Sciences of the United States of America.

Characterization of an Epstein-Barr virus receptor on human epithelial cells

E. Kieff, T. Tedder, X. Tong, 1992, The Journal of experimental medicine.

The EBNA-2 arginine-glycine domain is critical but not essential for B-lymphocyte growth transformation; the rest of region 3 lacks essential interactive domains

E. Kieff, R. Yalamanchili, X. Tong, 1994, Journal of virology.

The 62- and 80-kDa subunits of transcription factor IIH mediate the interaction with Epstein-Barr virus nuclear protein 2.

D. Reinberg, E. Kieff, R. Drapkin, 1995, Proceedings of the National Academy of Sciences of the United States of America.

The Epstein-Barr virus nuclear protein 2 acidic domain can interact with TFIIB, TAF40, and RPA70 but not with TATA-binding protein

E. Kieff, C. Thut, F. Wang, 1995, Journal of virology.

Epstein-Barr virus nuclear protein 2 transactivation of the latent membrane protein 1 promoter is mediated by J kappa and PU.1

E. Kieff, E. Johannsen, S. Grossman, 1995, Journal of virology.