167698-12-6Relevant academic research and scientific papers
Structure-reactivity relationships as probes for the inhibition mechanism of cholesterol esterase by aryl carbamates. I. Steady-state kinetics
Lin, Gialih,Lai, Cheng-Yue,Liao, Wei-Cheng,Kuo, Bing-Hong,Lu, Chun-Ping
, p. 489 - 500 (2000)
For substituted phenyl-N-butyl carbamates (1) and 4-nitrophenyl-N-substituted carbamates (2), linear relationships between values of NH proton chemical shift (δNH), pKa, and logk[OH] and Hammett substituent constant (σ) or Taft subst
Molecular recognition by acetylcholinesterase at the peripheral anionic site: Structure-activity relationships for inhibitions by aryl carbamates
Lin, Gialih,Lai, Cheng-Yue,Liao, Wei-Cheng
, p. 2683 - 2689 (2007/10/03)
Substituted phenyl-N-butyl carbamates (1-9Figure 2Chemical structures of carbamates 1-9 and edrophonium.) are potent irreversible inhibitors of Electrophorus electricus acetylcholinesterase. Carbamates 1-9 act as the peripheral anionic site-directed irrev
Hammett Analysis of the Inhibition of Pancreatic Cholesterol Esterase by Substituted Phenyl-N-Butylcarbamate
Lin, Gialih,Lai, Cheng-Yue
, p. 6117 - 6120 (2007/10/02)
Substituted phenyl-N-butylcarbamates (1) as active site-directed irreversible inhibitors of pancreatic cholesterol esterase are investigated for values of the dissociation constant (KI), the carbamylation constant (k2), and the bimol
