Older Publications

List of publications from 2003 and before:

Sonenberg, N. and Dever, T.E.: Eukaryotic translation initiation factors and regulators. Curr. Opin. Struct. Biol. 13:56-63, 2003
Lee, J.H., Pestova, T.V., Shin, B.-S., Cao, C., Choi, S.K., and Dever, T.E.: Initiation factor eIF5B catalyzes second GTP-dependent step in eukaryotic translation initiation. Proc. Natl. Acad. Sci. USA 99:16689-16694, 2002.
Ramelot, T.A., Cort, J.R., Yee, A.A., Liu, F., Goshe, M.B., Edwards, A.M., Smith, R.D., Arrowsmith, C.H., Dever, T.E., and Kennedy, M.A.: Myxoma virus immunomodulatory protein M156R is a structural mimic of eukaryotic translation initiation factor eIF2α. J. Mol. Biol. 322:943-954, 2002.
Shin, B.-S., Maag, D., Roll-Mecak, A., Arefin, M.S., Burley, S.K., Lorsch, J.R., and Dever, T.E.: Uncoupling of initiation factor eIF5B/IF2 GTPase and translational activities by mutations that lower ribosome affinity. Cell 111:1015-1025, 2002.
Zhan, K., Vattem, K.M., Bauer, B.N., Dever, T.E., Chen, J.-J., and Wek, R.C.: Phosphorylation of eukaryotic initiation factor-2 (eIF2) by HRI-related protein kinases in Schizosaccharomyces pombe is important for resistance to environmental stresses. Mol. Cell. Biol. 22:7134-7146, 2002.
Dever, T.E.: Gene-specific regulation by general translation factors. Cell 108:545-556, 2002.
Roll-Mecak, A., Shin, B.Y., Dever, T.E., and Burley, S.K.: Engaging the ribosome: universal IFs of translation. Trends Biochem. Sci. 26:705-709, 2001.
Ung, T.L., Cao, C., Lu, J., Ozato, K., and Dever, T.E.: Heterologous dimerization domains functionally substitute for the double-stranded RNA binding domains of the kinase PKR. EMBO J. 20:3728-3737, 2001.
Choi, S.K., Olsen, D.S., Roll-Mecak, A., Martung, A., Remo, K.L., Burley, S.K., Hinnebusch, A.G., and Dever, T.E.: Physical and functional interaction between the eukaryotic orthologs of prokaryotic translation initiation factors IF1 and IF2. Mol. Cell. Biol. 20:7183-7191, 2000.
Kawagishi-Kobayashi, M., Cao, C., Lu, J., Ozato, K., and Dever, T.E.: Pseudosubstrate inhibition of protein kinase PKR by swine pox virus C8L gene product. Virology 276:424-434, 2000.
Pestova, T.V., Dever, T.E., and Hellen, C.U.T.: Ribosomal subunit joining. In: Sonenberg, N., Hershey, J.W.B., and Matthews, M.B., eds. Translational Control of Gene Expression. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 425-445, 2000.
Pestova, T.V., Lomakin, I.B., Lee, J.H., Choi, S.K., Dever, T.E., and Hellen, C.U.T.: The joining of ribosomal subunits in eukaryotes requires eIF5B. Nature 403:332-335, 2000.
Roll-Mecak, A., Cao, C., Dever, T.E., and Burley, S.K.: X-ray structures of the universal translation initiation factor IF2/eIF5B: conformational changes on GDP and GTP binding. Cell 103:781-792, 2000.
Dever, T.E.: Translation initiation: adept at adapting. Trends Biochem. Sci. 24:398-403, 1999.
Lee, J.H., Choi, S.K., Roll-Mecak, A., Burley, S.K. and Dever, T.E.: Universal conservation in translation initiation revealed by human and archaeal homologs of bacterial translation initiation factor IF2. Proc. Natl. Acad. Sci. USA 96:4342-4347, 1999.
Lu, J., O'Hara, E.B., Trieselmann, B.A., Romano, P.R., and Dever, T.E.: The interferon-induced double-stranded RNA-activated protein kinase PKR will phosphorylate serine, threonine or tyrosine at residue-51 in eIF2α. J. Biol. Chem. 274:32198-32203, 1999.
Choi, S.K., Lee, J.H., Zoll, W.L., Merrick, W.C., and Dever, T.E.: Promotion of Met-tRNA_i^Met binding to ribosomes by yIF2, a bacterial IF2 homolog in yeast. Science 280:1757-1760, 1998.
Dever, T.E.: Analysis of eIF2a kinases in yeast. In: Methods in Molecular Biology: Protein Synthesis: Methods and Protocols (ed. R. Martin). Humana Press, Inc., Totawa, NJ, 1998; pp. 167-178.
Dever, T.E., Sripriya, R., McLachlin, J.R., Lu, J., Fabian, J.R., Kimball, S.R., and Miller, L.K.: Disruption of cellular translational control by a viral truncated eIF2α kinase homolog. Proc. Natl. Acad. Sci. USA 95:4164-4169, 1998.
Kawagishi-Kobayashi, M., Silverman, J.B., Ung, T.L., and Dever, T.E.: Regulation of protein kinase PKR by the vaccinia virus pseudosubstrate inhibitor K3L is dependent on residues conserved between the K3L protein and the PKR substrate eIF2α. Mol. Cell. Biol. 17:4146-4158, 1997.