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  • br Specification Table br Value of the data br

    2018-11-07


    Specification Table
    Value of the data
    Data Here, we present data regarding the effect of mitochondrial fission inhibition on skeletal muscle differentiation. Although similar experiments have been published by others [1,2], the data presented here support and add to the conclusions made by these researchers. Of note, the relatively higher concentration of mdivi-1 utilized here demonstrates the dose-dependence of its effect on C2C12 differentiation [1]. We additionally include data characterizing the activity of caspase-2 during this process.
    Experimental design, materials and methods
    Acknowledgments This research was supported by funds provided by the Natural Sciences and Engineering Research Council of Canada (NSERC) (Grant no. 341256) to Joe Quadrilatero. Darin Bloemberg is the recipient of a NSERC postgraduate scholarship. NSERC did not participate in study design, the collection, analysis and interpretation of data, the writing of the report, or the decision to submit the article for publication.
    1. Data In order to understand autophagy dynamics [1] and develop a robust methodological assay, we used four cell models: MEFs, HFs, SH-SY5Y human neuroblastoma cells, and N27 rat mesencephalic dopaminergic cells. LC3 and p62 protein levels were analyzed by Western-blotting assay, using SB 1X as a lysis buffer (Fig. 1). Furthermore, we measured the endogenous immunostaining of LC3 and p62 proteins in all cell models used in this report (Fig. 2). To complete this data analysis, p62 mRNA procyanidin b2 was performed in all cell lines (Fig. 3).
    2. Experimental design, materials and methods
    Acknowledgments We thank George Auburger (Experimental Neurology, Goethe University Medical School, Frankfurt am Main, Germany) for the MEFs, Adolfo López de Munaín (Neurology service, Instituto BioDonostia, Hospital Donostia, San Sebastian, Spain) for the HFs, and Anumantha G. Kanthasamy (Iowa State University, Ames, IA) for the N27 cells. M. R.-A. was supported by a FPU predoctoral fellowship (FPU13/01237) from Ministerio de Educación, Cultura y Deporte, Spain. R. G.-S. was supported by a Marie Sklodowska-Curie Individual Fellowship (IF-EF) from the European Commission. J. M. F. received research support from the Ministerio de Economia y Competitividad, Spain, CIBERNED (CB06/05/004 and PI12/02280). R. A. G.-P. was supported by a \"Contrato destinado a la retención y atracción del talento investigador, TA130009\" from Junta de Extremadura, Spain, and she received research support from Ministerio de Economía y Competitividad, Spain (PI14/00170). This work is supported also by “Fondo Europeo de Desarrollo Regional” (FEDER), from European Union. The authors also thank FUNDESALUD for helpful assistance.
    Data The data provides a variety of analysis methods to characterize protein–lipid interactions. These analysis methods used can be applied to any protein-lipid system, and can provide detailed information about protein structural changes over time when in contact with lipid membrane surfaces of differing composition. The design of the initial structures of the dimer protein and lipid bilayer systems can be found in the Material and Methods section of the research article [1].
    Experimental design, materials and methods We provide an analysis of a human beta-amyloid protein D42 (dimer of DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA) as well as some comparisons with the beta-amyloid D40 (same sequence less the 2 terminal amino acids IA) [2]. The initial protein structures of D42 and D40 were derived from published NMR experiments, i.e., PDB structures 2BEG[3] and 1BA4 [4]. We investigate structure formation and evolution [5] and binding kinetics on a symmetric 1-palmitoyl-2-oleoyl-phosphatidylcholine (PC) single bilayer system and an asymmetric 1-palmitoyl-2-oleoyl-phosphatidylcholine/1-palmitoyl-2-oleoyl-phosphatidylserine (PC/PS) double bilayer system (Figs. 1–7). We also provide residue contact-maps of the dimer on the symmetric and asymmetric bilayer systems (Figs. 9–11).