个人简介
B.S. McGill University
Ph.D. Harvard University
研究领域
Organic Chemistry and Biochemistry, The use of organic chemistry to study biochemical problems such the folding of disulfide containing proteins. Many extracellular proteins and almost all pharmaceutically relevant proteins contain disulfide bonds. The folding of these proteins in vitro is slow and methods of increasing the folding rate are being investigated.
近期论文
查看导师新发文章
（温馨提示：请注意重名现象，建议点开原文通过作者单位确认）
25. "Effects of Aromatic Thiols on Reactions that Occur During Protein Folding"
T. V. DeCollo W. J. Lees (2001) J. Org. Chem., 66, 4244-4249.
24. "Improved Synthesis of Indolyl Fulgides"
C. J. Thomas, M. A. Wolak, R. R. Birge. W. J. Lees (2001) J. Org. Chem., 66, 1914-1918.
23. "The Stereochemical Course of Enzymatic Enolpyruvyl Transfer and Catalytic Conformation of the Active Site Revealed by the Crystal Structure of the Fluorinated Analog of the Reaction Tetrahedral Intermediate Bound to the Active Site of the C115A Mutant of MurA"
T. Skarzynski, D. H. Kim, W. J. Lees, C. T. Walsh, K. Duncan (1998) Biochemistry, 37, 2572-2577.
22. "Analysis of Fluoromethyl Group Chirality Establishes a Common Stereochemical Course for the Enolpyruvyl Transfers Catalyzed by EPSP Synthase and UDP-GlcNAc Enolpyruvyl Transferase "
D. H. Kim, G. W. Tucker-Kellogg, W. J. Lees, C. T. Walsh (1996) Biochemistry, 35, 5435-5440.
21. "Characterization of a Cys115 to Asp Substitution in the E. coli Cell Wall Biosynthetic Enzyme UDP-GlcNAc Enolpyruvyl Transferase (MurA)That Confers Resistance to Inactivation by the Antibiotic Fosfomycin"
D. H. Kim, W. J. Lees, K. E. Kempsell, W. S. Lane, K. Duncan, C. T. Walsh (1996) Biochemistry, 35, 4923-4928.
20. "The Versatility of Phosphoenolpyruvate and its Vinyl Ether Products in Biosynthesis"
C. T. Walsh, T. E. Benson, D. H. Kim, W. J. Lees (1996) Chem. Biol., 3, 83-91.
19. "(E)-Enolbutyryl-UDP-N-Acetylglucosamine as a Mechanistic Probe of UDP-N-Acetylenolpyruvylglucosamine Reductase (MurB)"
W. J. Lees, T. E. Benson, J. M. Hogle, C. T. Walsh (1996) Biochemistry, 35, 1342-1351.
18. "Acetyl Transfer Precedes Uridylyl Transfer in the Formation of UDP-N-Acetylglucosamine in Separable Active Sites of the Bifunctional GlmU Protein of Escherichia coli"
A. Gehring, W. J. Lees, D. J. Mindiola, C. T. Walsh, E. D. Brown (1996) Biochemistry, 35, 579-585.
17. "Analysis of the Enol Ether Transfer Catalyzed by UDP-GlcNAc Enolpyruvyl Transferase Using (E)- and (Z)- Isomers of Phosphoenolbutyrate: Stereochemical, Partitioning, and Isotope Effect Studies"
W. J. Lees, C. T. Walsh (1995) J. Am. Chem. Soc., 117, 7329-7337.
16. "Stereochemical Analysis of the Tetrahedral Adduct Formed at the Active Site of UDP-GlcNAc Enolpyruvyl Transferase from the Pseudosubstrates, (E)- and (Z)-3-Fluorophosphoenolpyruvate, in D2O"
D. H. Kim, W. J. Lees, C. T. Walsh (1995) J. Am. Chem. Soc., 117, 6380-6381.
15. "Kinetic Characterization of the Inactivation of UDP-GlcNAc Enolpyruvyl Transferase by (Z)-3-Fluorophosphoenolpyruvate: Evidence for Two Oxocarbenium Ion Intermediates in Enolpyruvyl Transfer Catalysis"
D. H. Kim, W. J. Lees, T. M. Haley, C. T. Walsh (1995) J. Am. Chem. Soc., 117, 1494-1502.
14. "Reagents for Rapid Reduction of Disulfide Bonds"
R. Singh, G. V. Lamoureux, W. J. Lees, G. M. Whitesides (1995) Methods Enzymol., 251, 167-173.
13. "Formation of Two Enzyme-Bound Reaction Intermediate Analogs during Inactivation of UDP-GlcNAc Enolpyruvyl Transferase by (E)- or (Z)-3-Fluorophosphoenolpyruvate"
京公网安备 11010802027423号