Current position: University of Michigan, Ann Arbor, Medicinal Chemistry, Ph.D. candidate with Prof. Anna Mapp Education: University of California, Los Angeles, B.S. in chemical engineering, 2001 Nonscientific interests: Basketball, running, mountain biking
Transcriptional activators are responsible for the recruitment of coactivators and RNA polymerase II to gene promoters. My research is focused on understanding the role of individual protein–protein contacts on transcriptional activator function by using short peptides as probes to disrupt or promote transcriptional activation. We have converted inactive Mediator-targeted peptide activation domains into robust activators by inclusion of a hydrophobic binding surface. Both interactions are necessary for activity and provide evidence that features beyond coactivator contact are necessary for natural activator function and future artificial activator design. (Read Lum’s article on p 639.)
Douglas Mitchell
Current position: University of California, San Diego, Departments of Pharmacology, Cellular and Molecular Medicine, and Chemistry and Biochemistry, postdoctoral associate with Prof. Jack E. Dixon Education: Carnegie Mellon University, B.S. in chemistry, 2002; University of California, Berkeley, Ph.D. in chemistry with Prof. Michael A. Marletta, 2006 Nonscientific interests: Enjoying life by whatever means necessary
Although it is well documented that signaling concentrations of NO inhibit apoptosis and that S-nitrosation of the caspase proteases plays an important role in apoptotic inhibition, the precise mechanisms and targets of S-nitrosation have yet to be fully elucidated. We have engineered a small molecule that is capable of selective transnitrosation with the active site of caspase3/7. Expansion of our method to encompass other caspases provides an avenue for addressing specific questions about when, where, and how NO inhibits apoptosis. My future research interests include the design, synthesis, and characterization of new reagents to facilitate the study of signal transduction. (Read Mitchell’s article on p 659 and Point of View on p 615.)
Nicholas Agard
Current position: University of California, Berkeley, Department of Chemistry, Chemical Biology Program, Ph.D. candidate with Prof. Carolyn R. Bertozzi Education: Brown University, B.S. in chemistry, 2002 Nonscientific interests: Hiking and camping, wine tasting in the Napa and Sonoma valleys, and attending football games
In this work, we’ve compared strain-promoted chemistry and improvements to it with previously existing chemistries for modification of unnatural substrates. Use of these chemistries has been fundamental in exploring classes of biomolecules, particularly post-translationally modified proteins, by enabling their purification and imaging in complex mixtures. This paper provides a framework from which to choose an appropriate chemistry for tagging proteins modified by unnatural substrates and thus should serve as a guide to biologists. (Read Agard’s article on p 644.)
Current position: University of California, Berkeley, Department of Chemistry, Ph.D. candidate with Prof. Carolyn R. Bertozzi Education: Massachusetts Institute of Technology, S.B. in chemistry, 2004 Nonscientific interests: Classical music and playing piano
My research focuses on developing bioorthogonal chemistries for labeling biomolecules in living systems. The challenge here is taking the concepts of traditional organic synthesis and transplanting them from a roundbottom flask to a dish of cells or even a living animal. This paper discusses bioorthogonal chemistries for detecting the azide, a chemical reporter used to study aspects of cellular biochemistry, with a focus on strained alkyne probes. To me, the promise of bioorthogonal chemistries is the ability to visualize the molecular details of any physiological process, timeresolved, inside a living organism. (Read Baskin’s article on p 644.)
Current position: University of Alberta, Department of Chemistry, assistant professor Education: State University of New York–Albany, B.Sc. in chemistry, 1996; University of Wisconsin– Madison, Ph.D. in chemistry with Prof. Laura L. Kiessling, 2002 Postdoctoral work: Harvard Medical School with Prof. David E. Golan, 2002–2006 Nonscientific interests: Reading, music, hiking, and herpetology
My research interests focus on using chemistry and biophysics to study the interaction and function of membrane receptors. We used non-ensemble measurements of receptor mobility in conjunction with fluorescence microscopy to study the T cell adhesion receptor CD2. By applying a novel affinity analysis, we were able to integrate measurements of receptor mobility, number, and affinity to understand the mechanisms T cells use to regulate adhesion. We infer that the cell uses these parameters, including location and conformation, to generate context-specific regulation of the receptor, thereby enhancing adhesion. (Read Cairo’s article on p 649.)
Jenifer Lum
Jeremy Baskin
Christopher W. Cairo
Published online November 17, 2006 • 10.1021/cb600441f CCC: $33.50 © 2006 by American Chemical Society
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