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研究领域

Dr. Hershey retired in 2004 and then closed his laboratory in 2010. Although no longer directing research, he remains active in the field of protein biosynthesis through an association with Dr. Christopher Fraser in the Dept. of Molecular and Cell Biology on the Davis campus. He also serves as a Co-Editor-in-Chief of a new journal called Translation, published by Landes Biosciences.

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Roobol, A., J. Roobol, M.J. Carden, M.E. Smith J.W. Hershey, A. Bastide, J.R. Knight, A.E. Willis and C.M. Smales (2013) The chaperonin CCT interacts with and mediates the correct folding and activity of three subunits of translation initiation factor eIF3: 3b, 3i and 3h. Biochem. J. PMID 24320561. Villa, N., A. Do, J.W. Hershey and C.S. Fraser (2013) Human Eukaryotic Initiation Factor 4G (eIF4G) Protein Binds to eIF3c, -d, and –e to Promote mRNA Recruitment to the Ribosome. J. Biol. Chem. 288, 32932-32940. Hershey, J.W.B., N. Sonenberg and M.B. Mathews (2012) Principle of translation control: an overview. In: Protein Synthesis and Translational Control (JWB Hershey, N Sonenberg and MB Mathews, eds), pp 1-10, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. Sokabe, M., C.S. Fraser and J.W.B. Hershey (2011) The Human Translation Initiation Multi-Factor Complex Promotes Methionyl-tRNAi Binding to the 40S Ribosomal Subunit. Nucl. Acids Res. 40: 905-913. Henderson, A., and J.W.B. Hershey (2011) The role of eIF5A in protein synthesis. Cell Cycle 10 (21): 3517-3618. Andaya, A., W. Jia, M. Sokabe, C.S. Fraser, J.W.B. Hershey and J.A. Leary (2011) Phosphorylation of Human Eukaryotic Initiation Factor 2g: Novel Site Identification and Targeted PKC Involvement. J. Proteome Res. 10, 4613-4623. Henderson, C.A., and J.W.B. Hershey (2011) Translation Initiation Factor eIF5A Stimulates Protein Synthesis in Saccharomyces cerevisie. Proc. Natl. Acad. Sci. USA 108, 6415-6419. Ludwig, A.L., J.W.B. Hershey and P.J. Hagerman (2011) Initiation of translation of the FMR1 mRNA occurs predominantly through 5’end-dependent ribosomal scanning. J. Mol. Biol. 407, 21-34.

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