Charles Craik, PhD
|School||UCSF School of Pharmacy|
|Address||600 16th Street|
San Francisco CA 94158
|National Honor Society||1972
|Phi Beta Kappa||1974
||1975||Doane Distinguished Scholar|
||1975||Richard Edwin Lee Scholar|
|The Amer. Assoc. for the Advan. of Science||1978
||1978||Member, The Amer. Chem. Soc|
|American Cancer Society ||1982
| American Society of Biological Chemists||1983
|National Institutes of Health||1983
| Science Digest||1985
||1986||Top 100 Innovators|
||1997||Editorial Board Member|
||1988||Editorial Board Member|
||1989||Editorial Board Member|
|Member, The Protein Society||1989
|National Science Foundation Molecular Biochemistry||1993
|Gordon Conference on Proteolytic Enzymes and Inhibitors||1996
||1996||Vice Chair |
|Gordon Conference on Proteolytic Enzymes and Inhibitors||1998
|Cold Spring Harbor Meeting on the Biology of Proteolysis||1997
|Cold Spring Harbor Meeting on the Biology of Proteolysis||1999
|Cold Spring Harbor Meeting on the Biology of Proteolysis||2001
|Immunex Corporation (Seattle, WA)||2000
|United States Pharmacopeia||2009||Council of Experts|
|Allegheney College (Meadville, PA)||2010
|American Association for the Advancement of Science||2011
|Institute of Organic Chemistry and Biochemistry, Academy of Sciences, Prague, Czech Republic||2013
||2013||Institute Medal Lecture and Award|
My research focuses on structure-function analysis of proteases and their inhibitors. In my lab we use a combination of genetic, biochemical, and biophysical methods, with particular emphasis on identifying the roles and regulating the activity of proteases associated with infectious diseases, cancer, and development.
Proteases are directly or indirectly involved in virtually every biological function or dysfunction. The omnipresence of proteases and their natural inhibitors has placed them among the most studied proteins in biochemistry. The research efforts of the lab focus primarily on the structure-function analysis of proteases and their inhibitors using a combination of genetic, biochemical and biophysical methods. Chemical biological approaches are used or are being developed to study the substrate specificity, catalytic mechanism and biological role of proteases and their macromolecular inhibitors. The genes for serine (trypsin, serine collagenase, easter, prostate specific antigen, T-cell specific granzymes, MT-SP1 and 2, KSHV protease), cysteine (cruzain and falcipain) and aspartyl (HIV1 & HIV2 & SIV) proteases and macromolecular inhibitors such as ecotin and single chain antibodies are manipulated and expressed in heterologous expression systems. Targeted, region specific or random substitutions are introduced recombinantly to create variants that provide insight into the structure and activity of the target protein. A particular emphasis of our work is on identifying the roles and regulating the activity of proteases associated with infectious diseases, cancer and development. These studies are providing a better understanding of both the chemical make-up and the biological importance of these critical proteins. This in turn is leading to the development of strategies for regulating proteolytic activity as a means of therapeutic intervention. Further study of these proteins holds promise for better understanding, rapid detection and eventual control of infectious diseases and cancer.
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