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B. Ferraz-de-Souza, R. E. Hudson-Davies, L. Lin, R. Parnaik, M. Hubank, M. T. Dattani and J. C. Achermann, “Sterol O-Acyltransferase 1 (SOAT1, ACAT) Is a Novel Target of Steroidogenic Factor-1 (SF-1, NR5A1, Ad4BP) in the Human Adrenal,” The Journal of Clinical Endocrinology & Metabolism, Vol. 96, No. 4, 2011, pp. 663-668.

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.