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P. Kursula, H. Sikkila, T. Fukao, N. Kondo and R. K. Wierenga, “High Resolution Crystal Structures of Human Cytosolic Thiolase (CT): A Comparison of the Active Sites of Human CT, Bacterial Thiolase, and Bacterial KAS I,” Journal of Molecular Biology, Vol. 347, No. 1, 2005, pp. 189-201. http://dx.doi.org/10.1016/j.jmb.2005.01.018

has been cited by the following article:

• TITLE: Physicochemical 2D-Qsar and 3D Molecular Docking Studies on N-Chlorosulfonyl Isocyanate Analogs as Sterol O-Acyl-Transferase-1 “Soat-1” Inhibitors

  AUTHORS: Khalid El Akri, Rokaya Mouhibi, Mohamed Zahouily, Naîma Hanafi, Moulay Abdellah Bahlaoui

  KEYWORDS: Sterol O-Acyl-Transferase-1; N-CSI Analogs; QSAR; MLR; ANN; 3D Molecular Docking

  JOURNAL NAME: Open Journal of Medicinal Chemistry, Vol.3 No.4, December 3, 2013

  ABSTRACT: A series of N-carbonyl-functionalized ureas, carbamates and thiocarbamates derivatives (or N-Chloro sulfonyl isocyanate “N-CSI”) were involved in linear and nonlinear physicochemical quantitative structure-activity relationship “QSAR” analysis to find out the structural keys to control the inhibition against Sterol O-Acyl-Transferase-1 “SOAT-1”. The results indicate the important effects of geometrical and chemical descriptors on the inhibitory activity of SOAT-1. The molecules were also screened for three-dimensional molecular docking on the crystal structure of ACAT-1 (1WL5 for ACAT-1, PDB). A comparison between 2D-QSAR and 3D molecular docking studies shows that the latter confirm the first results and represent a good prediction of the chemical and physical nature of interactions between our drug molecules and enzyme SOAT-1.