Proteases and Tissue Remodeling Unit, OPCB
NATIONAL INSTITUTES OF HEALTH/NIDCR![Thomas Bugge](https://webarchive.library.unt.edu/web/20090507033723im_/http://www.nidcr.nih.gov/NR/rdonlyres/A58326AE-7CF5-4A49-A2C2-5F5AE7E37D98/3591/bugge.jpg)
BUILDING 30 ROOM 211
30 CONVENT DR MSC 4340
BETHESDA MD 20892-4340
Phone: (301) 435-1840
Fax: (301) 402-0823
E-mail: Dr. Thomas Bugge
Research Interests
The laboratory studies the biochemistry, biology, and pathology of cell surface serine proteases, in particular their relationship to the development, regeneration, and malignant transformation of oral tissues.
Education
1989 M.Sc. The Institute of Microbiology, University of Copenhagen, Copenhagen, Denmark
1993 Ph.D. European Molecular Biology Laboratory, Heidelberg, Germany
Recent publications
Hobson, J. P., Liu S., Rønø, B., Leppla, S. H., and Bugge, T.H. Imaging specific cell surface proteolytic activity in single living cells. Nature Methods, 3, 259 – 261, 2006 .
Bugge, T.H. and Leppla, S. H. Anthrax target in macrophages pinpointed. Nature Genetics, 38, 137-138, 2006.
List, K., Szabo, R., Molinolo, A., Sriuranpong, V., Redeye, V., Burke B., Murdock, T., Nielsen, B.S., Gutkind, J.S., and Bugge, T. H. Deregulated matriptase proteolysis causes ras-independent multistage carcinogenesis and promotes ras-mediated malignant transformation. Genes & Dev., 19, 1934-1950, 2005.
Curino, A. C., Nielsen, B. S., Engelholm, L. H., Molinolo, A. A., Behrendt, N., and Bugge, T. H. Intracellular collagen degradation mediated by uPARAP/Endo180 is a major pathway of extracellular matrix turnover during malignancy. J. Cell Biol. 169, 977-986, 2005.
Complete CV