S
Silvia Taramino
Researcher at University of Turin
Publications - 12
Citations - 108
Silvia Taramino is an academic researcher from University of Turin. The author has contributed to research in topics: Reductase & Ergosterol. The author has an hindex of 8, co-authored 12 publications receiving 103 citations.
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Inhibitory effect of umbelliferone aminoalkyl derivatives on oxidosqualene cyclases from S. cerevisiae, T. cruzi, P. carinii, H. sapiens, and A. thaliana: a structure-activity study.
Simonetta Oliaro-Bosso,Franca Viola,Silvia Taramino,Silvia Tagliapietra,Alessandro Barge,Giancarlo Cravotto,Gianni Balliano +6 more
TL;DR: Eighteen coumarin derivatives were tested as inhibitors of oxidosqualene cyclases from Saccharomyces cerevisiae, Trypanosoma cruzi, Pneumocystis carinii, Homo sapiens, and Arabidopsis thaliana and suggest the present series as a promising compound family for the development of novel antiparasitic agents.
Journal ArticleDOI
Oxidosqualene cyclase from Saccharomyces cerevisiae, Trypanosoma cruzi, Pneumocystis carinii and Arabidopsis thaliana expressed in yeast: a model for the development of novel antiparasitic agents.
Gianni Balliano,Henrietta Dehmlow,Simonetta Oliaro-Bosso,Matilde Scaldaferri,Silvia Taramino,Franca Viola,Giulia Caron,Johannes Aebi,Jean Ackermann +8 more
TL;DR: The screening identified three derivatives particularly promising for the development of novel anti-Trypanosoma agents and eight derivatives for theDevelopment of novelAnti-Pneumocystis agents.
Journal ArticleDOI
Umbelliferone aminoalkyl derivatives as inhibitors of human oxidosqualene-lanosterol cyclase
Simonetta Oliaro-Bosso,Silvia Taramino,Franca Viola,Silvia Tagliapietra,Giuseppe Ermondi,Giancarlo Cravotto,Gianni Balliano +6 more
TL;DR: In cell cultures of both human keratinocytes and mouse 3T3 fibroblasts, the observed inhibition of cholesterol biosynthesis was selective for oxidosqualene cyclase.
Journal ArticleDOI
Genetic analyses involving interactions between the ergosterol biosynthetic enzymes, lanosterol synthase (Erg7p) and 3-ketoreductase (Erg27p), in the yeast Saccharomyces cerevisiae.
B. Teske,Silvia Taramino,M.S.A. Bhuiyan,N.S. Kumaraswami,Stephen K. Randall,Robert J. Barbuch,James A. Eckstein,Gianni Balliano,Martin Bard +8 more
TL;DR: A novel phenotype demonstrated that the catalytic function of Erg27p can be separated from its Erg7p chaperone ability, and new insights are provided into the role of ErG27p in sterol biosynthesis.
Journal ArticleDOI
Access of the substrate to the active site of squalene and oxidosqualene cyclases: comparative inhibition, site-directed mutagenesis and homology-modelling studies.
Simonetta Oliaro-Bosso,Tanja Schulz-Gasch,Silvia Taramino,M. Scaldaferri,Franca Viola,Gianni Balliano +5 more
TL;DR: Crystal structure and homology modelling indicate that both enzymes possess a narrow constriction that separates an entrance lipophilic channel from the active-site cavity of squalene-hopene cyclase from Alicyclobacillus acidocaldarious and lanosterol synthase from Saccharomyces cerevisiae.