2001 - Center for Advanced Biotechnology and Medicine - Rutgers ...
2001 - Center for Advanced Biotechnology and Medicine - Rutgers ...
2001 - Center for Advanced Biotechnology and Medicine - Rutgers ...
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Ann Stock, Ph.D.<br />
Associate Investigator, Howard Hughes Medical Institute; Resident Faculty Member,<br />
CABM; Professor, UMDNJ-Robert Wood Johnson Medical School, Department of<br />
Biochemistry<br />
Protein Crystallography Laboratory<br />
Dr. Ann Stock per<strong>for</strong>med graduate work on the biochemistry of signal transduction proteins with Professor Daniel E. Koshl<strong>and</strong>, Jr. at the<br />
University of Cali<strong>for</strong>nia at Berkeley. From 1987 to 1991 she pursued structural analysis of these proteins while a postdoctoral fellow with<br />
Professor Clarence Schutt at Princeton University <strong>and</strong> Professor Gregory Petsko at the Structural Biology Laboratory in the Rosenstiel <strong>Center</strong> at<br />
Br<strong>and</strong>eis University. Her CABM laboratory has solved structures of several signal transduction proteins, including receptor modification<br />
enzymes <strong>and</strong> members of the two-components family of signal transduction proteins. Stock has received National Science Foundation<br />
Predoctoral <strong>and</strong> Damon Runyon-Walter Winchell Postdoctoral Fellowships, a Lucille P. Markey Scholar Award in Biomedical Science, the NSF<br />
Young Investigator Award <strong>and</strong> a Sinsheimer Scholar Award. She is an associate investigator of the Howard Hughes Medical Institute.<br />
Research in the Stock laboratory focuses on structure/function studies of signal transduction<br />
proteins. Ef<strong>for</strong>t is concentrated on bacterial histidine protein kinases <strong>and</strong> response regulator<br />
proteins that mediate the majority bacterial signaling processes. These systems are important <strong>for</strong><br />
virulence in pathogenic organisms <strong>and</strong> are currently targets <strong>for</strong> development of new antibiotics in<br />
several pharmaceutical companies. During the past year the Stock laboratory determined the<br />
first structure <strong>for</strong> a full-length member of the OmpR family of transcription factors, the largest<br />
subfamily of response regulator proteins. The structure provides insight into the mechanism of<br />
regulation of the protein by phosphorylation <strong>and</strong> suggests a limit to the extent of mechanistic<br />
similarities between proteins of similar structure <strong>and</strong> function.<br />
Publications:<br />
Schlichting, I., Berendzen, J., Chu, K., Stock, A.M., Maves, S.A., Benson, D.E., Sweet, R.M.,<br />
Ringe, D., Petsko, G.A., <strong>and</strong> Sligar, S.G. (2000). The catalytic pathway of cytochrome P450cam<br />
at atomic resolution. Science 287: 1615-1622.<br />
Stock, A.M., Robinson, V.L. <strong>and</strong> Goudreau, P.N. (2000). Two-component signal transduction.<br />
Annu. Rev. Biochem. 69: 183-215.<br />
Buckler, D.R., An<strong>and</strong>, G.S. <strong>and</strong> Stock, A.M. (2000). Response regulator phosphorylation <strong>and</strong><br />
activation: a two-way street? Trends Microbiol. 8: 153-155.<br />
An<strong>and</strong>, G.S., Goudreau, P.N., Lewis, J.K. <strong>and</strong> Stock, A.M. (2000). Evidence <strong>for</strong><br />
phosphorylation-dependent con<strong>for</strong>mational changes in methylesterase CheB. Protein Sci. 9: 898-<br />
906.<br />
Buckler, D.R. <strong>and</strong> Stock, A.M. (2000). Synthesis of [ 32 P]phosphoramidate <strong>for</strong> use as a low<br />
molecular weight phosphodonor reagent. Anal. Biochem. 283: 222-227.<br />
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<strong>Center</strong> <strong>for</strong> <strong>Advanced</strong> <strong>Biotechnology</strong> <strong>and</strong> <strong>Medicine</strong><br />
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