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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Robert S. Phillips

Department of Chemistry

University of Georgia


GA 30602



Name/email consistency: high



  • Department of Chemistry, University of Georgia, Athens, GA 30602, USA. 2002 - 2011


  1. Properties of tryptophan indole-lyase from a piezophilic bacterium, Photobacterium profundum SS9. Phillips, R.S., Ghaffari, R., Dinh, P., Lima, S., Bartlett, D. Arch. Biochem. Biophys. (2011) [Pubmed]
  2. Effects of hydrostatic pressure on the conformational equilibrium of tryptophan synthase from Salmonella typhimurium. Phillips, R.S., Miles, E.W., McPhie, P., Marchal, S., Lange, R., Holtermann, G., Goody, R.S. Ann. N. Y. Acad. Sci. (2010) [Pubmed]
  3. Insights into the mechanism of Pseudomonas dacunhae aspartate beta-decarboxylase from rapid-scanning stopped-flow kinetics. Phillips, R.S., Lima, S., Khristoforov, R., Sudararaju, B. Biochemistry (2010) [Pubmed]
  4. Pressure and temperature jump relaxation kinetics of the conformational change in Salmonella typhimurium tryptophan synthase L-serine complex: large activation compressibility and heat capacity changes demonstrate the contribution of solvation. Phillips, R.S., Miles, E.W., McPhie, P., Marchal, S., Georges, C., Dupont, Y., Lange, R. J. Am. Chem. Soc. (2008) [Pubmed]
  5. Quantitative effects of allosteric ligands and mutations on conformational equilibria in Salmonella typhimurium tryptophan synthase. Phillips, R.S., McPhie, P., Miles, E.W., Marchal, S., Lange, R. Arch. Biochem. Biophys. (2008) [Pubmed]
  6. Aminoacrylate intermediates in the reaction of Citrobacter freundii tyrosine phenol-lyase. Phillips, R.S., Chen, H.Y., Faleev, N.G. Biochemistry (2006) [Pubmed]
  7. Hydrostatic pressure affects the conformational equilibrium of Salmonella typhimurium tryptophan synthase. Phillips, R.S., Miles, E.W., Holtermann, G., Goody, R.S. Biochemistry (2005) [Pubmed]
  8. Differential effects of temperature and hydrostatic pressure on the formation of quinonoid intermediates from L-Trp and L-Met by H463F mutant Escherichia coli tryptophan indole-lyase. Phillips, R.S., Holtermann, G. Biochemistry (2005) [Pubmed]
  9. Role of lysine-256 in Citrobacter freundii tyrosine phenol-lyase in monovalent cation activation. Phillips, R.S., Chen, H.Y., Shim, D., Lima, S., Tavakoli, K., Sundararaju, B. Biochemistry (2004) [Pubmed]
  10. Structure and mechanism of tryptophan indole-lyase and tyrosine phenol-lyase. Phillips, R.S., Demidkina, T.V., Faleev, N.G. Biochim. Biophys. Acta (2003) [Pubmed]
  11. Crystals of tryptophan indole-lyase and tyrosine phenol-lyase form stable quinonoid complexes. Phillips, R.S., Demidkina, T.V., Zakomirdina, L.N., Bruno, S., Ronda, L., Mozzarelli, A. J. Biol. Chem. (2002) [Pubmed]
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