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GRANT WRITING
WORKSHOPS SERIES |
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AGENDA
Thursday, March 24th,
Bryan Center Von
Canon B
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General introduction and technical arrangements. Distribute handouts |
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Introduce the invited speakers Faculty will give a brief overview of material they will cover during the workshop |
Dr. Tomalei Vess,
Program Director, Graduate School |
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Dr. Harold Erickson, Professor in the department
of Cell Biology Dr. Alex Roland, Professor in the Department of
History Dr. Kenneth Kreuzer, Professor in the Department
of Biochemistry |
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Group arrangement: divide participants into breakout groups. Each group will work on one of three topics: predoctoral/fellowship grant, postdoctoral grant or faculty grant |
Dr. |
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Discussion of case study proposals. Focus on reviewers comments |
Dr. Harold Erickson Dr. Alex Roland Dr. |
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Summarize material covered in each of the breakout sessions |
Dr. Harold Erickson Dr. Alex Roland Dr. Kenneth Kreuzer |
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General questions and comments |
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Questions or comments: discuss them online: http://cierd.cs.duke.edu/forum/
Workshop Speakers
Dr. Harold Erickson, Professor in the department of Cell Biology
Dr. Erickson's research interests include Cytoskeleton and cell motility, bacterial cell division, and extracellular matrix. Dr. Erickson received his undergraduate degree from Carnegie-Mellon University and his Ph.D. in biophysics from Johns Hopkins University. As an NIH fellow, Dr. Erickson completed postdoctoral training at the MRC laboratory of molecular biology in Cambridge, England.
Our laboratory is interested in the structural biochemistry of two systems - the cytoskeleton and the extracellular matrix. Our work on cytoskeleton is now focused on FtsZ, the major bacterial cytoskeletal protein that powers division in all bacteria. FtsZ is a homolog of tubulin, so what we learn has implications for the eukaryotic cytoskeleton. We are trying to determine how FtsZ assembles into the contractile ring and generates the force to divide bacteria. We are using in vitro assembly studies and site directed mutagenesis. Recently we have developed fluorescence techniques, which demonstrate extremely fast assembly dynamics in vitro and in vivo. We are now working to develop single molecule (TIRF) fluorescence microscopy to follow the assembly dynamics of single FtsZ protofilaments. Our ultimate goal is to be able to recreate a contractile band based on FtsZ. Our work on the extracellular matrix focuses primarily on fibronectin. We have made a GFP-fibronectin construct that permits us to follow the assembly of the fibronectin matrix in real time. We have found that the matrix fibrils are highly elastic, and are now seeking the mechanism for stretching. Again, fluorescence techniques are proving powerful tools to probe stretching at the molecular level.
Dr. Alex Roland, Professor in the department of History
I study military history and the history of technology. My focus has ranged over all of Western experience, and I have recently converted my undergraduate course in military history to a comparative world military history course. I have written about chariots in the second millenium B.C., Greek fire in medieval Byzantium, and computers and aerospace technology in the twentieth century. While I study the history of technology in general, I also focus on the ways in which technology has shaped war and war has altered technology.
Awards/Recognitions: Harold K. Johnson Professor of Military History, Military History Institute, U.S. Army War College, 1988-1989 Fellow, Dibner Institute for the History of Science and Technology, Massachusetts Institute of Technology, 1994-1995 Dr. Leo Shifrin Professor of Naval-Military History, U.S. Naval Academy, 2001-2002
Separate from my scholarship and teaching, I am a student and critic of the United States civilian space program. I spent eight stimulating and rewarding years (1973-1981) as a historian with the National Aeronautics and Space Administration, but I have come to believe that the agency lost its way after the Apollo program. I have written extensively on this topic.
Dr. Kenneth Kreuzer, Professor in the department of Biochemistry
Dr. Kreuzer’s laboratory studies the mechanisms of DNA replication, recombination and repair.In particular, we are analyzing how DNA replication begins from two different replication origins within the bacteriophage T4. We also use the simple T4 system to study how antitumor agents inhibit the action of topoisomerases. Topoisomerases are enzymes which relax the DNA helix during replication and transcription. Antitumor agents block the topoisomerases by trapping an intermediate complex, blocking cell replication and thereby killing off tumor cells. We are analyzing just how this intermediate complex is trapped ,and what pathways of DNA repair a cell can use to overcome it. Replication from T4 origins requires a stable RNA-DNA hybrid generated from a promoter within the origin. This hybrid is also a target for regulation: UvsW helicase can remove the RNA from the hybrid, blocking replication from the origin. A second mechanism for starting replication requires phage-encoded recombination proteins but is independent of the origin sequences. We have shown that this recombination-dependent replication can be triggered by double-strand breaks in the genome. It appears that the repair of double-strand breaks in a T4 infection occurs by precisely this method,and recent research on a variety of organisms indicates that DNA replication can play a key role in repairing double-strand breaks. Phage T4 encodes a type II topoisomerase that is similar to its eukaryotic counterpart. We have demonstrated that this topoisomerase is a target for drug action. Antitumor agents trap a reaction intermediate, called the cleavage complex, in which the topoisomerase is covalently attached to cleaved DNA. We have shown not only that this cleavage complex can block a replication fork in vivo, but also that recombinational repair provides some insensitivity to the antitumor agents, probably by repairing the complex. We are analyzing when and how the complex is repaired. We are also studying the mechanism of enzyme inhibition, and our results demonstrate that the inhibitor binds DNA at the enzyme active site.