[1] | Lee, L.C., Chou, Y.L., Chen H.H., Lee, Y.L.* and Shaw, J. F.* 2009. Functional role of a non-active site residue Trp23 on the enzyme activity of Escherichia coli thioesterase I/protease I/lysophospholipase L1. BBA-Proteins and Proteomics; 1794: 1467–1473. |
[2] | Lee, L.C., Liaw, Y.C., Lee, Y.L.* and Shaw, J.F.* 2007. Enhanced preference for π-bond containing substrates is correlated to Pro110 in the substrate-binding tunnel of Escherichia coli thioesterase I/protease I/lysophospholipase L1. BBA-Proteins and Proteomics 1774:959-967 |
[3] | Lee, L.C., Lee, Y.L.*, Leu, R.J. and Shaw, J.F.* 2006. Functional role of catalytic triad and oxyanion hole-forming residues on enzyme activity of Escherichia coli thioesterase I/protease I/phospholipase L1. Biochem. J. 397:69-76 |
[4] | Huang, L.C., Lee, Y.L., Huang, B.L., Kuo, C.I., and Shaw, J.F.* 2002. High polyphenol oxidase activity and low titratable acidity as causes of browning of bamboo tissue cultures in vitro. In Vitro Cellular & Developmental Biology Plant 38:358-365. |
[5] | Lee, Y.L., Sagare, A.P., Lee, Z.Y., Feng, H.T., Ko, Y.C., Shaw, J.F. and Tsay, H.S.* 2001. Formation of protoberberine-type alkaloids by the tubers of somatic embryo-derived plants of Corydalis yanhusuo. Planta Medica 67:839-842. |
[6] | Sagare, A.P., Lee, Y.L., and Tsay, H.S.* 2000. Cytokinin-induced somatic embryogenesis and plant regeneration in Corydalis yanhusuo (Fumariaceae), a medicinal plant. Plant Science 160:139-147. |
[7] | Lo, Y.C., Lee, Y.L., Shaw, J.F. and Liaw, Y.C.* 2000. Crystallization and preliminary X-ray crystallographic analysis of thioesterase I from Escherichia coli. Acta Cryst. D 56:756-757. |
[8] | Lee, Y.L., Su, M.S., Huang, T.H. and Shaw J.F.* 1999. C-terminal His-tagging Results in Substrate Specificity Changes of the Thioesterase I from Escherichia coli. J. Am. Oil Chem. Soc. 76:1113-1118. |
[9] | Lin, T.H., Chen, C., Huang, R.F., Lee, Y.L., Shaw, J.F. and Huang, T.H.* 1998. Multinuclear NMR resonance assignments and the secondary structure of Escherichia coli thioesterase I/protease I: a member of a new subclass of lipolytic enzymes. J. Biomol. NMR 11:363-380. |
[10] | Lee, Y.L., Chang, R.C. and Shaw, J.F.* 1997. Facile purification of a C-terminal extended His-tagged Vibrio mimicus arylesterase and characterization of the purified enzyme. J. Am. Oil Chem. Soc. 74:1371-1376. |
[11] | Lee, Y.L., Chen, J.C. and Shaw, J.F.* 1997. The thioesterase I of Escherichia coli is an arylesterase and shows stereospecificity for protease substrates. Biochem. Biophy. Res. Comm. 231:452-456. |
[12] | Musayev, F.N., Lee, Y.L., Shaw, J.F. and Liaw, Y.C.* 1995. Crystallization and preliminary X-ray crystallographic analysis of arylesterase from Vibrio mimicus. Protein Science 4:1931-1933. |