Screening data for: A key mammalian cholesterol synthesis enzyme, squalene monooxygenase, is allosterically stabilized by its substrate

Published: 07-03-2020| Version 1 | DOI: 10.17632/53dxyt4rnd.1
Contributors:
Hiromasa Yoshioka,
Hudson W. Coates,
Ngee Kiat Chua,
Yuichi Hashimoto,
Andrew J. Brown,
Kenji Ohgane

Description

To identify compounds that modulate squalene monooxygenase (SM) stability, screening of FDA-approved drug library was performed with HEK293 cells stably expressing SM-emerald luciferase fusion protein. For experimental details, see the accompanying article. The data is a table with the following columns: position, [ROW].[COLUMN].[PLATE ID]; name, name of compounds; conc, concentration of the compounds in µM; type, types of the treatment (conotrol "ctrl" or "library"); plate, plate id (number); row, row number (A to H) within 96-well plates; column, column number (1 to 12) within 96-well plates; luc_10, luminescence data for 10 µM treatment screen; luc_1, luminescence data for 1 µM treatment screen; nluc_10, luminecence data for 10 µM treatment screen, normalized in a plate-wise manner; nluc_1, luminecence data for 1 µM treatment screen, normalized in a plate-wise manner; rsn_10, robust signal-to-noise ratio (robust Z score) for 10 µM screen; rsn_1, robust signal-to-noise ratio (robust Z score) for 1 µM screen.

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