Výsledky vyhledávání

Molecular modeling and docking calculations of 4-acyloxy-biphenyl-4′-N-butylcarbamates as potential inhibitors of human butyrylcholinesterase

Autor: Shu-Hsien Lin, Gan-Hong Chen, Gialih Lin, Yu-Fang Shen

Publikováno v: Canadian Journal of Chemistry. 94:72-77

The kinetic studies and drug designs of butyrylcholinesterase play an important role in the development of Alzheimer’s disease therapeutics. In this research, automated docking studies were performed to provide useful insights into butyrylcholinest

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::4905b91d59dba337b9c27440b3461211
https://doi.org/10.1139/cjc-2015-0414

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Akademický článek

Ortho Effects in Quantitative Structure-activity Relationships for Acetylcholinesterase Inhibition by Aryl Carbamates.

Autor: Gialih Lin¹ gilin@dragon.nchu.edu.tw, Yu-Chen Liu¹, Yan-Fu Lin¹, Yon-Gi Wu¹

Publikováno v: Journal of Enzyme Inhibition & Medicinal Chemistry. Oct2004, Vol. 19 Issue 5, p395-401. 7p. 4 Diagrams, 2 Charts, 1 Graph.

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Synthesis and evaluation of a new series of tri-, di-, and mono-N-alkylcarbamylphloroglucinols as conformationally constrained inhibitors of cholesterol esterase

Autor: Gialih Lin, Yu-Fong Shen, Shuo-Yung Jian, Gin-Zen Lin, Ching-In Hwang, Ming-Cheng Lin, James Lin

Publikováno v: Protein Science. 21:1344-1357

1,3,5-Tri-N-alkylcarbamylphloroglucinols (1–4) are synthesized as conformationally constrained analogs of triacylglycerols (TGs) to probe Jenck's proximity effect in the cholesterol esterase inhibition. For the cholesterol esterase inhibition, inhi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a092a7ebd21fdfcbadd068ddcbf63afa
https://doi.org/10.1002/pro.2121

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Kinetics and Protein-Inhibitor Docking Studies of Enantiomers of exo-2-Norbornyl-N-n-butylcarbamates as Pseudomonas Lipase Inhibitors to Probe the Enantioselectivity of the Enzyme

Autor: Yu-Fang Shen, Gialih Lin

Publikováno v: Journal of the Chinese Chemical Society. 59:60-65

The Pseudomonas species lipase inhibition shows enantioselectivity for R-enantiomer over S-enantiomer of exo-2-norbornyl-N-n-butylcarbamates. R-, S-, and racemic-exo-2-norbornyl-N-n-butylcarbamates are all characterized as pseudo substrate inhibitors

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a3c2aefb5a50c11e343f6ef042104f9d
https://doi.org/10.1002/jccs.201100252

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Synthesis and Pseudomonas Lipase Inhibition Study of Stereoisomers of Decahydro-2-naphthyl-N-n-butylcarbamate

Autor: Ming-Cheng Lin, Yu-Fang Shen, Gialih Lin

Publikováno v: Protein & Peptide Letters. 18:1168-1176

(2S,4aR,8aS)-Cis,cis-, (2R,4aS,8aR)-cis,cis-, rac-cis,cis-, and rac-trans,cis-decahydro-2-naphthyl-N-n-butylcarbamates are synthesized from condensation of (2S,4aR,8aS)-cis,cis-, (2R,4aS,8aR)-cis,cis-, rac-cis,cis-, and rac-trans,cisdecahydro- 2-naph

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da36df55521a2a4cd90c100c43b807eb
https://doi.org/10.2174/092986611797200913

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E339…R416 salt bridge of nucleoprotein as a feasible target for influenza virus inhibitors

Autor: Hui Wen Liu, Ming-Daw Tsai, Yih-Shyun E. Cheng, Pang-Hung Hsu, Chi-Huey Wong, Yu-Hou Chen, Ying-Ta Wu, Chao-Jung Wu, An-Suei Yang, Pei-Yu Wu, Fu-Yang Lin, Hua-Ting Hsu, Gialih Lin, Yu-Fang Shen, Mengi Lin, Shao-Ying Chu

Publikováno v: Proceedings of the National Academy of Sciences. 108:16515-16520

The nucleoprotein (NP) of the influenza virus exists as trimers, and its tail-loop binding pocket has been suggested as a potential target for antiinfluenza therapeutics. The possibility of NP as a drug target was validated by the recent reports that

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d0c03602794d8b3ceadc9938deeecfc
https://doi.org/10.1073/pnas.1113107108

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Stereoselective Inhibition of Cholesterol Esterase by Enantiomers of exo- and endo-2-Norbornyl-N–n-butylcarbamates

Autor: I-Ru Chen, Shyh-Jei Yeh, Gialih Lin, Ming-Cheng Lin

Publikováno v: The Protein Journal. 30:220-227

Four stereoisomers of 2-norbornyl-N-n-butylcarbamates are characterized as the pseudo substrate inhibitors of cholesterol esterase. Cholesterol esterase shows enantioselective inhibition for enantiomers of exo- and endo-2-norbornyl-N-n-butylcarbamate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21e95cf982da4d83ce7e65a2ebf0ad83
https://doi.org/10.1007/s10930-011-9323-3

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Comparison of active sites of butyrylcholinesterase and acetylcholinesterase based on inhibition by geometric isomers of benzene-di-N-substituted carbamates

Autor: Gialih Lin, Mei-Ting Hwang, Shyh-Ying Chiou, Chuan-Fu Huang

Publikováno v: Journal of Biochemical and Molecular Toxicology. 23:303-308

We have reported that benzene-1,2-, 1,3-, and 1,4-di-N-substituted carbamates (1-15) are characterized as the conformationally constrained inhibitors of acetylcholinesterase and mimic gauche, eclipsed, and anti-conformations of acetylcholine, respect

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3518b7626c22b789bba8bdc5b00e9e97
https://doi.org/10.1002/jbt.20286

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