Dr. James Wohlschlegel and his colleagues research the use of proteomic mass spectrometry to study the regulatory networks mediated by the ubiquitin family of small protein modifiers. They are particularly interested in understanding the role of small ubiquitin-related modifier (SUMO) and ubiquitin in regulating chromatin structure and the cellular response to genotoxic stress.
Selected Cancer-Related Publications:
Venable JD, Wohlschlegel J, McClatchy D, Park SK, Yates JR. Relative quantitation of stable isotope labeled peptides using a linear ion trap - orbitrap hybrid mass spectrometer. Analytical Chemistry. 2007; 79:3056-64.
Duchaine TF, Wohlschlegel JA, Kennedy S, Bei Y, Conte D, Pang K, Brownell D, Mitani S, Harding S, Ruvkun G, Yates JR, Mello CC. Functional proteomics reveals the biochemical niche of C. elegans DCR-1 in multiple small-RNA-mediated pathways. Cell. 2006; 12.
Wohlschlegel JA, Johnson ES, Reed SI, Yates JR. Improved identification of SUMO attachment sites using C-terminal SUMO mutants and tailored protease digestion strategies. Journal of Proteome Research. 2006; 5:761-770.
Kaiser P, Wohlschlegel JA. Identification of Ubiquitination Sites and Determination of Ubiquitin-Chain Architectures by Mass Spectrometry. Methods in Enzymology. 2005; 399:266-277.
Wohlschlegel JA, Johnson ES, Reed SI, Yates JR. Global analysis of protein sumoylation in Saccharomyces cerevisiae. Journal of Biological Chemistry. 2004; 44:45662-8.