Ohio State University
Bowles, D.P.; Yuan, C.; Stephany, K.R.; Lavinder, J.J.; Hansen, A.L. & Magliery, T.J. (2018) “Resonance assignments of wild-type and two cysteine-free variants of the four-helix bundle protein, Rop,” Biomol NMR Assign., accepted, doi: 10.1007/s12104-018-9837-0.
Bowles, D.P.; Hansen, A.L.; Rhoads, C.A.; Mohan, S.; Yuan, C. & Magliery, T.J. (2018) “(1)H, (13)C, (15)N resonance assignment of recombinant Euplotes raikovi protein Er-23.,” Biomol NMR Assign., accepted, doi: 10.1007/s12104-018-9825-4.
Long, N.E.; Sullivan, B.J.; Ding, H.; Doll, S.R.; Ryan, M.A.; Hitchcock, C.L.; Martin E.W. Jr.; Kumar, K.; Tweedle, M.F. & Magliery, T.J. (2018) “Linker engineering in anti-TAG-72 antibody fragments optimizes biophysical properties, serum half-life, and high-specificity tumor imaging,” J. Biol. Chem., 293: 9030-9040, doi:10.1074/jbc.RA118.002538.
Goyal, V.D. & Magliery, T.J. (2018) “Phylogenetic spread of sequence data affects fitness of SOD1 consensus enzymes: Insights from sequence statistics and structural analyses,” Proteins, 86: 609-620, doi:10.1002/prot.25486.
Gong, L.; Ding, H.; Long, N.E.; Sullivan, B.J.; Martin, E.W. Jr.; Magliery, T.J. & Tweedle, M.F. (2018) “A 3E8.scFv.Cys-IR800 Conjugate Targeting TAG-72 in an Orthotopic Colorectal Cancer Model,” Mol. Imaging Biol., 20: 47-54, doi:10.1007/s11307-017-1096-4.
Hitchcock, C.L.; Magliery, T.J.; Mojzisik, C.; Johnson, M.; Arnold, M.W. & Martin, E.W. (2017) “Evolution of a System to Increase Precision in the Surgical Management of Colorectal Carcinoma,” Clinic. Surg. 2: 1491. Link to full text.
Choudhary, D; Kumar, A.; Magliery, T.J. & Sotomayor, M. (2017) “Using thermal scanning assays to test protein-protein interactions of inner-ear cadherins,” PLoS One, 12, e0189546, doi:10.1371/journal.pone.0189546.
Magliery, T.J. (2015) “Protein stability: Computation, sequence statistics, and new experimental methods,” Curr. Opin. Struct. Biol., 33: 161-168, doi:10.1016/j.sbi.2015.09.002.
Ray, W.C.; Rumpf, R.W.; Sullivan, B.; Callahan. N.; Magliery, T.; Machiraju, R.; Wong, B.; Krzywinski, M. & Bartlett, C.W. (2014) “Understanding the sequence requirements of protein families: insights from the BioVis 2013 contests,” BMC Proc., 8 (Suppl 2 Proceedings of the 3rd Annual Symposium on Biologica):S1, doi:10.1186/1753-6561-8-S2-S1.
Ray, W.C.; Wolock, S.L.; Callahan, N.W.; Dong, M.; Li, Q.Q.; Liang, C.; Magliery, T.J. & Bartlett, C.W. (2014) “Addressing the unmet need for visualizing conditional random fields in biological data,” BMC Bioinformatics, 15: 202, doi:10.1186/1471-2105-15-202.
Caleca, L.; Putignano, A.L.; Colombo, M.; Congregati, C.; Sarkar, M.; Magliery, T.J.; Ripamonti, C.B.; Foglia, C.; Peissel, B.; Zaffaroni, D.; Manoukian, S.; Tondini, C.; Barile, M.; Pensotti, V.; Bernard, L.; Papi, L. & Radice, P. (2014) “Characterization of an Italian Founder Mutation in the RING-Finger Domain of BRCA1,” PLoS One, 9: e86924, doi: 10.1371/journal.pone.0086924.
Zhang, Y.; Goswami, D.; Wang, D.; Wang, T.S.; Sen, S.; Magliery, T.J.; Griffin, P.R.; Wang, F. & Schultz, P.G. (2014) “An antibody with a variable-region coiled-coil ‘knob’ domain,” Angew. Chem. Int. Ed. Engl., 53: 132-135, doi:10.1002/anie.201307939.
Durani, V. & Magliery, T.J. (2013) “Protein Engineering and Stabilization from Sequence Statistics: Variation and Co-Variation Analysis,” Meth. Enzymol., 523: 237-256, doi:10.1016/B978-0-12-394292-0.00011-4.
Muthukrishnan, S.; Shete, V.; Sanan, T.; Vyas, S.; Oottikkal, S.; Porter, L.M.; Magliery, T.J. & Hadad, C.M. (2012) “Mechanistic insights into the hydrolysis of organophosphorus compounds by paraoxonase-1: Exploring the limits of substrate tolerance in a promiscuous enzyme,” J. Phys. Org. Chem., 25: 1247-1260, doi:10.1002/poc.3002.
Durani, V.; Sullivan, B.J. & Magliery, T.J. (2012) “Simplifying protein expression with ligation-free, traceless and tag-switching plasmids,” Protein Expr. Purif., 85: 9-17, doi: 10.1016/j.pep.2012.06.007.
Sullivan, B.J.; Nguyen, T.; Durani, V.; Mathur, D.; Rojas, S.; Thomas, M.; Syu, T. & Magliery, T.J. (2012) “Stabilizing proteins from sequence statistics: The interplay of conservation and correlation in triosephosphate isomerase stability,” J. Mol. Biol., 420: 384-399, doi:10.1016/j.jmb.2012.04.025.
Sarkar, M.; Harsch, C.K.; Matic, G.T.; Hoffman, K.; Norris III, J.R.; Otto, T.C.; Lenz, D.E.; Cerasoli, D.M. & Magliery, T.J. (2012) “Solubilization and humanization of paraoxonase-1,” J. Lipids, 2012: Article ID 610937, 13 pages, doi:10.1155/2012/610937.
Magliery, T.J.; Lavinder, J.J.; Sullivan, B.J. (2011) “Protein stability by number: high-throughput and statistical approaches to one of protein science’s most difficult problems,” Curr. Opin. Chem. Biol. 15: 443-451, doi:10.1016/j.cbpa.2011.03.015.
Sullivan, B.J.; Durani, V. & Magliery, T.J. (2011) “Triosephosphate isomerase by consensus design: Dramatic differences in physical properties and activity of related variants,” J. Mol. Biol., 413: 195-208, doi:10.1016/j.jmb.2011.08.001.
Nie, L.; Lavinder, J.J.; Sarkar, M.; Stephany, K. & Magliery, T.J. (2011) “Synthetic approach to stop-codon scanning mutagenesis,” J. Am. Chem. Soc. 133: 6177-6186, doi:10.1021/ja106894g.
Hari, S.B.; Byeon, C.; Lavinder, J.J & Magliery, T.J. (2010) “Cysteine-free Rop: a four-helix bundle core mutant has wild-type stability and structure but dramatically different unfolding kinetics,” Protein Sci., 19: 670-679, doi:10.1002/pro.342.
Nadaud, P.S.; Sarkar, M.; Wu, B.; Macphee, C.E.; Magliery, T.J. & Jaroniec, C.P. (2009) “Expression and purification of a recombinant amyloidogenic peptide from transthyretin for solid-state NMR spectroscopy,” Protein Expr. Purif. 70: 101-108, doi:10.1016/j.pep.2009.09.017.
Otto, T.C.; Harsch, C.K.; Yeung, D.T.; Magliery, T.J.; Cerasoli, D.M. & Lenz, D.E. (2009) “Dramatic differences in organophosphorus hydrolase activity between human and chimeric recombinant mammalian paraoxonase-1 enzymes,” Biochemistry 48: 10416-10422, doi:10.1021/bi901161b.
Gambin, Y.; Schug, A.; Lemke, E.A.; Lavinder, J.J.; Ferreon, A.C.; Magliery, T.J.; Onuchic, J.N. & Deniz, A.A. (2009) “Direct single-molecule observation of a protein living in two opposed native structures,” Proc. Natl. Acad. Sci. U.S.A. 106: 10153-10158, doi:10.1073/pnas.0904461106.
Lavinder, J.J.; Hari, C.B.; Sullivan, B.J. & Magliery, T.J. (2009) “High-throughput thermal scanning: a general, rapid dye-binding thermal shift screen for protein engineering,” J. Am. Chem. Soc. 131: 3794-3795, doi:10.1021/ja8049063.
Sarkar, M. & Magliery, T.J. (2008) “Re-engineering a split-GFP reassembly screen to examine RING-domain interactions between BARD1 and BRCA1 mutants observed in cancer patients,” Mol. BioSyst. 4: 599-605, doi:10.1039/b802481b.
Training (Kenyon, U.C. Berkeley, TSRI, Yale)
Magliery, T.J. & Regan, L. (2005) “Reassembled GFP: detecting protein-protein interactions and protein expression patterns.” In Green Fluorescent Protein: Properties, Applications, and Protocols, 2nd ed., eds. Chalfie, M.; Kain, S. John Wiley & Sons: Hoboken, NJ, pp. 391-405 (also listed as Methods Biochem. Anal., 2006, 47: 391-405).
Chin, J.W. & Magliery, T.J. (2005) “Protein expression by expansion of the genetic code.” In Encyclopedia of Molecular Cell Biology and Molecular Medicine, 2nd ed., Vol. 11, ed. Meyers, R.A. Wiley-VCH: Weinheim, Germany, pp. 45-68.
Magliery, T.J. & Regan, L. (2005) “Sequence variation in ligand binding sites in proteins,” BMC Bioinformatics 6: 240.
Magliery, T.J. (2005) “Unnatural protein engineering: producing proteins with unnatural amino acids” (review), Med. Chem. Rev. Online 2: 303-323.
Magliery, T.J.; Wilson, C.G.M.; Pan, W.; Mishler, D.; Ghosh, I.; Hamilton, A.D. & Regan, L. (2005) “Detecting protein-protein interactions with a green fluorescent protein fragment reassembly trap: scope and mechanism,” J. Am. Chem. Soc. 127: 146-157.
Wilson, C.G.M.; Magliery, T.J. & Regan, L. (2004) “Detecting protein-protein interactions with GFP fragment reassembly,” Nat. Methods, 1: 255-262.
Magliery, T.J. & Regan, L. (2004) “Beyond consensus: statistical free energies reveal hidden interactions in the design of a TPR motif,” J. Mol. Biol. 343: 731-745.
Magliery, T.J. & Regan, L. (2004) “Library approaches to biophysical problems” (editorial overview), Eur. J. Biochem. 271: 1593-1594.
Magliery, T.J. & Regan, L. (2004) “Combinatorial approaches to protein structure and stability” (review), Eur. J. Biochem. 271: 1595-1608.
Magliery, T.J. & Regan, L. (2004) “A cell-based screen for function of the four-helix bundle protein Rop: a new tool for combinatorial experiments in biophysics,” Protein Eng. Des. Select. 17: 77-83.
Magliery, T.J. & Liu, D.R. (2004) “Expanding the genetic code in vitro and in vivo.” In The Genetic Code and the Origin of Life, ed. Ribas de Pouplana, L. Landes Bioscience: Georgetown, TX, pp. 221-249.
Magliery, T.J.; Pastrnak, M.; Anderson, J.C.; Santoro, S.W.; Meggers, E.; Herberich, B.; Wang, L. & Schultz, P.G. (2003) “Incorporation of unnatural amino acids into proteins.” In Translation Mechanisms, eds. Lapointe, J.; Brakier-Gingras, L. Landes Bioscience: Georgetown, TX, pp. 95-114.
Anthony-Cahill, S.J. & Magliery, T.J. (2002) “Expanding the natural repertoire of protein structure and function” (review), Curr. Pharm. Biotech. 3: 299-315.
Anderson, J.C.; Magliery, T.J. & Schultz, P.G. (2002) “Exploring the limits of codon and anticodon size,” Chem. Biol. 9: 237-244.
See commentary: Landweber, L. (2002) “Custom codons come in threes, fours and fives,” Chem. Biol. 9: 143.
Magliery, T.J.; Anderson, J.C. & Schultz, P.G. (2001) “Expanding the genetic code: selection of efficient suppressors of four-base codons and identification of ‘shifty’ 4-base codons with a library approach in Escherichia coli,” J. Mol. Biol. 307: 755-769.
Pastrnak, M.; Magliery, T.J. & Schultz, P.G. (2000) “A new orthogonal suppressor tRNA/aminoacyl-tRNA synthetase pair for evolving an organism with an expanded genetic code,” Helv. Chim. Acta 83: 2277-2286.
Wang L.; Magliery, T.J.; Liu, D.R. & Schultz, P.G. (2000) “A new functional suppressor tRNA/aminoacyl-tRNA synthetase pair for the in vivo incorporation of unnatural amino acids into proteins,” J. Am. Chem. Soc. 122: 5010-5011.
Liu, D.R.; Magliery, T.J.; Pastrnak, M. & Schultz, P.G. (1997) “Engineering a tRNA and aminoacyl-tRNA synthetase for the site-specific incorporation of unnatural amino acids into proteins in vivo,” Proc. Natl. Acad. Sci. U.S.A. 94: 10092-10097.
See commentary: Schimmel, P. & Söll, D. (1997) “When protein engineering confronts the tRNA world,” Proc. Natl. Acad. Sci. U.S.A. 94: 10007-10009.
Liu, D.R; Magliery, T.J. & Schultz, P.G. (1997) “Characterization of an ‘orthogonal’ suppressor tRNA derived from E. coli tRNA2Gln,” Chem. Biol. 4: 685-691.
Magliery, T.J.; Vitellaro, L.K.; Diop, N.K. & Marusak, R.A. (1997) “Fe-EDTA-bisamide and Fe-ADR-925, the iron-bound hydrolysis product of the cardioprotective agent dexrazoxane, cleave DNA via the hydroxyl radical,” Metal Based Drugs, 4: 199-205.