Dr. Bruce A. Stanley - Research

Dr. Bruce Stanley

Director, Scientific Programs

Section of Research Resources

Graduate Program Affiliations: Cell and Molecular Biology

  • Ph.D. Degree, Cornell University, 1987;
  • Postdoctoral Training, The Pennsylvania State University College of Medicine, 1987-1989;
  • Visiting Scientist, Strasbourg, France, 1984-1985

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Email: bstanley@psu.edu

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Stanley Lab Research:

Mass Spectrometric Methods for Proteomic Analysis; Structure-Function Determinants of Rapid Protein Degradation; Arginine/Nitric Oxide/Ornithine Metabolism and Growth Control

The primary current lab focus is development of Mass Spectrometric and Bioinformatic methods for quantitative proteomic analysis and biomarker discovery. These methods include 1D and 2D liquid chromatographic separations of both whole proteins and proteolytically digested peptide fragments; the use of iTRAQ isotope-coded affinity tags; the development of improved mass spec analysis software (with commercial and other academic centers); the development of improved MALDI plate surfaces and MALDI matrix deposition methods (in conjunction with the Penn State Nanofabrications Facility), and improved bioinformatic and biostatistical methods, e.g., for calculating the False Discovery Rates required in large scale proteomic studies.

Past goals of the lab research program have been to understand the mechanisms of control of intracellular levels of rapidly degraded proteins and how this subclass of proteins is involved in control of cell growth and differentiation, particularly how enzyme half-life changes contribute to rapid cell proliferation. The enzymes of the polyamine biosynthetic pathway, particularly S-adenosylmethionine decarboxylase, have been studied both as general model proteins to define proteolytic signals which target proteins for rapid proteolysis, and for their specific contributions to control of cell growth. Experimental approaches include cell culture and transfection studies, in vitro expression of wildtype versus mutant proteins, and the development of new in vitro systems to study protein degradation. Structure-function studies are done by specific replacement of amino acid residues in the model proteins, and assessment of the effect of these mutations on either degradative rate or other enzymologic characteristics of the proteins.

Finally, the lab maintains an interest in Arginine/Nitric Oxide/Ornithine Metabolism and Growth Control, particularly how changes in substrate levels may act as control points in metabolic flux independently of changes in enzyme activity.

Selected Publications

(for most up-to-date list, see Dr. Stanley's page in profiles.psu.edu

 

 

  • The good old days...

Stanley Lab Fall '99: Bruce Stanley, Kim Stambaugh, Azmi Yerlikaya, & Wil Martin