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HCS-Analyzer: open source software for high-content screening data correction and analysis.
Ogier, Arnaud,Dorval, Thierry Oxford University Press 2012 Bioinformatics Vol.28 No.14
<P>High-throughput screening is a powerful technology principally used by pharmaceutical industries allowing the identification of molecules of interest within large libraries. Originally target based, cellular assays provide a way to test compounds (or other biological material such as small interfering RNA) in a more physiologically realistic in vitro environment. High-content screening (HCS) platforms are now available at lower cost, giving the opportunity for universities or research institutes to access those technologies for research purposes. However, the amount of information extracted from each experiment is multiplexed and hence difficult to handle. In such context, there is an important need for an easy-to-use, but still powerful software able to manage multidimensional screening data by performing adapted quality control and classification. HCS-analyzer includes: a user-friendly interface specifically dedicated to HCS readouts, an automated approach to identify systematic errors potentially occurring during screening and a set of tools to classify, cluster and identify phenotypes of interest among large and multivariate data.</P>
Kim, Jiho,Lee, Honggun,Lee, Joo Hyun,Kwon, Do-yoon,Genovesio, Auguste,Fenistein, Denis,Ogier, Arnaud,Brondani, Vincent,Grailhe, Regis American Society for Biochemistry and Molecular Bi 2014 The Journal of biological chemistry Vol.289 No.21
<P>More than 100 copper/zinc superoxide dismutase 1 (SOD1) genetic mutations have been characterized. These mutations lead to the death of motor neurons in ALS. In its native form, the SOD1 protein is expressed as a homodimer in the cytosol. <I>In vitro</I> studies have shown that SOD1 mutations impair the dimerization kinetics of the protein, and <I>in vivo</I> studies have shown that SOD1 forms aggregates in patients with familial forms of ALS. In this study, we analyzed WT SOD1 and 9 mutant (mt) forms of the protein by non-invasive fluorescence techniques. Using microscopic techniques such as fluorescence resonance energy transfer, fluorescence complementation, image-based quantification, and fluorescence correlation spectroscopy, we studied SOD1 dimerization, oligomerization, and aggregation. Our results indicate that SOD1 mutations lead to an impairment in SOD1 dimerization and, subsequently, affect protein aggregation. We also show that SOD1 WT and mt proteins can dimerize. However, aggregates are predominantly composed of SOD1 mt proteins.</P>