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PrintProfessor
Professor
Personal Data
Office Phone: 410-706-4354
Office Address: Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 108 N. Greene Street, 439, Baltimore, MD 21201
Email: dweber@umaryland.edu
Education
1993 - present: Promoted through the academic ranks at the University of Maryland School of Medicine. Granted tenure in 1999 and promoted to Full Professor in 2004.
1988-1992: Post Doctoral Fellow, The Johns Hopkins University School of Medicine Department of Biological Chemistry, Advisor: Dr. Albert S. Mildvan
1984-1988: Ph.D., University of North Carolina, Chapel Hill, NC Department of Chemistry, Advisor: Dr. Richard G. Hiskey; Dissertation: "Investigation of Gla-domain Peptides of Prothrombin Binding to Synthetic Phospholipid Membranes"
1980-1984: B.S., Chemistry, Muhlenberg College, Allentown, PA
1988-1992: Post Doctoral Fellow, The Johns Hopkins University School of Medicine Department of Biological Chemistry, Advisor: Dr. Albert S. Mildvan
1984-1988: Ph.D., University of North Carolina, Chapel Hill, NC Department of Chemistry, Advisor: Dr. Richard G. Hiskey; Dissertation: "Investigation of Gla-domain Peptides of Prothrombin Binding to Synthetic Phospholipid Membranes"
1980-1984: B.S., Chemistry, Muhlenberg College, Allentown, PA
Research Interests
The major project in my laboratory involves studying the structure and function of S100B, a growth factor in the brain and skin. S100B is a dimeric Calcium-binding protein that is overproduced during gliosis in patients with Alzheimer disease, Down syndrome, and Aids related dementia. In addition, S100B and/or other members of the S100 protein family (mts1, S100ï¡, S100L, etc.) are found at high concentrations in several tumor cell lines including skin, lung, bladder, kidney, cervix, breast, head and neck, larynx, lymph, and mouth. Thus, overproduction of S100 proteins may cause problems in the regulation of cell growth in these diseases. Presumably, the function of S100B is related to its ability to bind a variety of target proteins in a Ca2+-dependent manner. One such target is the tumor suppressor protein, p53. For this protein, we have shown that up-regulation of S100B abrogates p53 transcription activation and apoptosis in tumor cell lines and that S100B binds and inhibits both the protein kinase C-dependent phosphorylation and the oligomerization of p53. Therefore, the focus of our laboratory is to determine, at atomic resolution, the mechanism by which S100B can affect p53 transcription activation and promote uncontrolled cell growth. In this regard, we have determined the three-dimensional structure of apo-S100B and the S100B-Ca2+ complex using NMR spectroscopy, and the structure of the S100B-Ca2+-p53 peptide complex is also complete. The structural studies of S100B are imperative for the efficient design of biochemistry and the molecular biology experiments that are also done in our laboratory. Knowledge about the structure and function of S100B are now used to design molecules that inhibit S100B from binding to p53. Patent applications are under review for several of these molecules, and perhaps one or more of these molecules will be practical as a drug for regulating uncontrolled cell growth in vivo. Similarly, structure/function studies are underway for several other members of the S100 protein family including S100A1,mts1 (S100A4), S100A2, S100A3, and others.
