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Gialih Lin

Departnment of Chemistry and Institute of Biochemistry

National Chung-Hsing University




Name/email consistency: medium



  • Departnment of Chemistry and Institute of Biochemistry, National Chung-Hsing University, Taichung, Taiwan. 2000 - 2006


  1. Probing structure-function relationships of serine hydrolases and proteases with carbamate and thiocarbamate inhibitors. Lin, G., Chiou, S.Y., Hwu, B.C., Hsieh, C.W. Protein J. (2006) [Pubmed]
  2. Ortho effects for inhibition mechanisms of butyrylcholinesterase by o-substituted phenyl N-butyl carbamates and comparison with acetylcholinesterase, cholesterol esterase, and lipase. Lin, G., Lee, Y.R., Liu, Y.C., Wu, Y.G. Chem. Res. Toxicol. (2005) [Pubmed]
  3. Probing the peripheral anionic site of acetylcholinesterase with quantitative structure activity relationships for inhibition by biphenyl-4-acyoxylate-4'-N-Butylcarbamates. Lin, G., Chen, G.H., Yeh, S.C., Lu, C.P. J. Biochem. Mol. Toxicol. (2005) [Pubmed]
  4. Quantitative structure-activity relationships for the pre-steady state of Pseudomonas species lipase inhibitions by p-nirophenyl-N-substituted carbamates. Lin, G., Liao, W.C., Ku, Z.H. Protein J. (2005) [Pubmed]
  5. Benzene-di-N-octylcarbamates as conformationally constrained phospholipase A(2) inhibitors. Lin, G., Lin, Y.F., Hwang, M.T., Lin, Y.Z. Bioorg. Med. Chem. Lett. (2004) [Pubmed]
  6. Ortho effects in quantitative structure-activity relationships for acetylcholinesterase inhibition by aryl carbamates. Lin, G., Liu, Y.C., Lin, Y.F., Wu, Y.G. J. Enzyme. Inhib. Med. Chem (2004) [Pubmed]
  7. Quantitative structure-activity relationships for the pre-steady state acetylcholinesterase inhibition by carbamates. Lin, G., Liao, W.C., Chan, C.H., Wu, Y.H., Tsai, H.J., Hsieh, C.W. J. Biochem. Mol. Toxicol. (2004) [Pubmed]
  8. Cage amines as the stopper inhibitors of cholinesterases. Lin, G., Tsai, H.J., Tsai, Y.H. Bioorg. Med. Chem. Lett. (2003) [Pubmed]
  9. Quantitative structure-activity relationships for the pre-steady-state inhibition of cholesterol esterase by 4-nitrophenyl-N-substituted carbamates. Lin, G., Liao, W.C., Chiou, S.Y. Bioorg. Med. Chem. (2000) [Pubmed]
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