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CAMDA 2006 Conference Keynote Speakers

Dr. William Reeves
Chief Viral Exanthems and Herpesvirus Branch
Center for Disease Control
Atlanta, GA, USA
Dr. Reeves is currently Chief Viral Exanthems and Herpesvirus Branch for the CDC in Atlanta, GA.  He is an adjunct professor of psychiatry at Emory University, a member of Winship Cancer Center at Emory, and a clinical assistant professor of gynecology and obstetrics at the Emory University School of Medicine.  In 2003, Dr. Reeves was awarded the La Orden de Manuel Amador Guerrero Medal by the President of the Republic of Panama, the highest honor that Panama awards in the field of science.  In 1995, he was elected as Fellow by the American Association for Advancement of Science for leading contributions to understanding the role of human papillomavirus in cervical cancer through international studies.  Dr. Reeves's current interests include research of chronic viral diseases, primarily chronic fatigue syndrome (CFS) and diseases associated with human papillomavirus (HPV).

Dr. Christoph Borchers
Department of Biochemistry and Biophysics
University of North Carolina
Chapel Hill, NC, USA

Dr. Borchers is the head of the proteomics core at the University of North Carolina in Chapel Hill and holds the position of Assistant Professor at the University.  His main interests lie in methodologies for quantification of proteins and use of photochemical reactions to aid in protein identification.

Mass spectrometry has been well-recognized for its ability to provide accurate mass measurements of biomolecules which allows the rapid and sensitive study of proteins from a given genome in a large-scale manner at a single experiment (proteomics). The current proteomics approaches are very powerful in identifying proteins, however, they lack the ability of absolute protein quantification, comprehensive identification as well as in identification and quantification of protein modifications (like phosphorylation) in a large-scale manner. All these features are important for a more complete characterization of the protein differences in sick versus healthy cells which provides a more complete knowledge about the disease involving proteins and protein pathways. One of our research goals is to develop and apply novel proteomics methods based on the combination of protein chemistry and mass spectrometric approaches allowing protein characterization and its modification, comprehensively and quantitatively.

Another main focus of our research is the combined approach of photochemical reactions at proteins and mass spectrometric methods. This concept is suitable for identification of target proteins and components of protein complexes, structural characterization of protein-lagan and protein-biomolecule interaction, and elucidation of dynamic processes in proteins. The photochemical reactions at proteins used for this purpose can be classified as photoaffinity labeling, photo-crosslinking, or time-resolved photochemical reactions. The purpose of the research is to develop and apply this concept in order to provide information relevant to a number of health concerns and biochemical and pharmaceutical processes. For this research, our special interest is to identify the binding partners of the tumor suppressor protein p53 at different phosphorylation states of p53 and different cell states in a time-dependant manner to elucidate the involvement of p53 in the apoptosis and cell growth pathway.


Last modified on 12/15/2005 09:20:26

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