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Stephen F. Martin

Department of Chemistry and Biochemistry

University of Texas at Austin 78712

USA

[email]@*.utexas.edu

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Affiliation

Department of Chemistry and Biochemistry, University of Texas at Austin 78712, USA. 1996 - 2003

References

Design, synthesis, and evaluation of water-soluble phospholipid analogues as inhibitors of phospholipase C from Bacillus cereus. Franklin, C.L., Li, H., Martin, S.F. J. Org. Chem. (2003) [Pubmed]
Determination of the substrate specificity of the phospholipase D from Streptomyces chromofuscus via an inorganic phosphate quantitation assay. Martin, S.F., DeBlanc, R.L., Hergenrother, P.J. Anal. Biochem. (2000) [Pubmed]
Solution conformations of short-chain phosphatidylcholine. Substrates of the phosphatidylcholine-preferring PLC of Bacillus cereus. Martin, S.F., Pitzer, G.E. Biochim. Biophys. Acta (2000) [Pubmed]
The choline binding site of phospholipase C (Bacillus cereus): insights into substrate specificity. Martin, S.F., Follows, B.C., Hergenrother, P.J., Trotter, B.K. Biochemistry (2000) [Pubmed]
Catalytic cycle of the phosphatidylcholine-preferring phospholipase C from Bacillus cereus. Solvent viscosity, deuterium isotope effects, and proton inventory studies. Martin, S.F., Hergenrother, P.J. Biochemistry (1999) [Pubmed]
An enantioselective total synthesis of (+)-geissoschizine. Martin, S.F., Chen, K.X., Eary, C.T. Org. Lett. (1999) [Pubmed]
General base catalysis by the phosphatidylcholine-preferring phospholipase C from Bacillus cereus: the role of Glu4 and Asp55. Martin, S.F., Hergenrother, P.J. Biochemistry (1998) [Pubmed]
Expression and site-directed mutagenesis of the phosphatidylcholine-preferring phospholipase C of Bacillus cereus: probing the role of the active site Glu146. Martin, S.F., Spaller, M.R., Hergenrother, P.J. Biochemistry (1996) [Pubmed]