James Bruce

Associate Professor

Address

Fulmer 128
Pullman, WA 99164-4630

(509) 335-2116
email: james_bruce@wsu.edu
personal page: http://terabyte.chem.wsu.edu/proteomics/

Education

Research

Professor Bruce received his Ph.D. in physical chemistry in 1992 from the University of Florida under the direction of Professor John R. Eyler while studying fundamental ion-molecule chemistry with Fourier transform ion cyclotron resonance mass spectrometry (FTICR-MS). Dr Bruce then joined the Pacific Northwest National Laboratory, where as a Senior Research Scientist, his work focused on the development of high performance FTICR mass spectrometry for bioanalytical and proteomics applications. In 1999, Dr. Bruce joined the Novartis Institute for Functional Genomics, and later Merck Research Laboratories where his research centered on the application of mass spectrometry and proteomics to further enable basic research in the pharmaceutical industry. Dr. Bruce joined the faculty at Washington State University in 2002 to establish a cutting-edge biological mass spectrometry and proteomics research program.

With the availability of complete genomic sequences of many organisms, and the number of completed genomes increasing on nearly a daily basis, the potential to exploit this information with mass spectrometry and the new field of proteomics research for protein, posttranslational modification, and protein-protein interaction profiling is rapidly expanding. Ultimately, this type of information will one day be compiled to provide "systems-level" comprehension biological organisms and present researchers with an entirely new way of understanding and modifying biological function and system behavior. However, true "Systems Biology" approaches to study living organisms requires significant advancement of analytical capabilities from what exist today. Our laboratory is developing and applying new analytical capabilities and strategies to exploit high performance mass spectrometry to overcome today's barriers to systems-level comprehension of biological organisms. We are interested in using these advanced capabilities to provide information on posttranslational modifications and noncovalent interactions on a proteome-wide scale. This information will constitute a critical component of systems biology research that current technology and approaches can not provide. Our research and development efforts will provide major impact on biological, biomedical, and health-related research fields, by identifying relevant posttranslational and interaction networks critical for disease progression, adverse drug reaction and toxicology, as well as normal system function.

Publications