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Gianni Balliano

Researcher at University of Turin

Publications -  87
Citations -  1789

Gianni Balliano is an academic researcher from University of Turin. The author has contributed to research in topics: Cyclase & 2,3-Oxidosqualene. The author has an hindex of 22, co-authored 87 publications receiving 1721 citations.

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Systematic analysis of yeast strains with possible defects in lipid metabolism.

TL;DR: A group of five European laboratories established methods suitable to screen for novel genes of the yeast Saccharomyces cerevisiae involved in lipid metabolism, regulation of lipid biosynthesis and the role of lipids in organellar membranes, and found evidence suggesting a possible role in cholesterol metabolism.
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Conversion of Squalene to the Pentacarbocyclic Hopene

TL;DR: The membrane protein squalene-hopene cyclase was cocrystallized with 2-azasqualene and analyzed by X-ray diffraction to 2.13 A resolution, which revealed a mobile region between the active center cavity and the membrane, which may melt, opening a passage for Squalene and hopene.
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In vitro inhibition of animal and higher plants 2,3-oxidosqualene-sterol cyclases by 2-aza-2,3-dihydrosqualene and derivatives, and by other ammonium-containing molecules.

TL;DR: 2-Aza-2,3-dihydrosqualene and related molecules, a series of new compounds designed as analogues of the transient carbocationic high energy intermediate, occurring in the oxirane ring opening during the cyclization of 2, 3-oxidosqualene, were tested in vitro as inhibitors of the microsomal 2,4,10beta-Trimethyl-trans-decal-3 beta-ol and 4,10 beta-dim
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Yeast oxidosqualene cyclase (Erg7p) is a major component of lipid particles.

TL;DR: In this article, Xenstaedt et al. showed that Erg7p is almost exclusively associated with this compartment as shown by analysis of enzymatic activity, Western blot analysis, and in vivo localization of erg7p-GFP.
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The squalene-2,3-epoxide cyclase as a model for the development of new drugs

TL;DR: 2-aza-2,3-dihydrosqualene and its derivatives strongly inhibited the cyclases, the site of the enzyme responsible for binding to the inhibitor is quite sensitive to the steric hindrance, and the degree of the inhibitory activity is greater in higher plants than in rat liver or fungi.