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  • br Data Fasting during the

    2018-11-01


    Data Fasting during the light phase reduced oxygen consumption in female mice fed either a high-fat or standard diet (SD) for 3 days (Fig. 1B), but during the dark phase, fasting only reduced oxygen consumption when mice were fed a background high-fat diet (Fig. 1A). In both the dark and light phases, fasted mice fed a high-fat diet (HFD) had reduced oxygen consumption when compared to fasted mice fed SD (Fig. 1). Fasting significantly reduced the respiratory exchange ratio (RER) in mice fed either background diet, and consuming a HFD resulted in a lower non-fasted RER than consuming a SD, regardless of the phase of study (Fig. 2). Fasted mice fed a SD had increased activity during the dark cycle compared to non-fasted mice, although these data do not show a similar increase in activity during the dark cycle with fasting when mice are given a background HFD (Fig. 3A). During the light cycle, these data show no significant differences between dietary or fasting/non-fasting groups with regards to activity (Fig. 3B).
    Experimental design, materials and methods
    Acknowledgments The authors thank Jean Flanagan, Nancy Gibson and Angela Wagler for expert assistance in animal care. This work was supported by grants to RED from the Canada Foundation for Innovation – Leader’s Opportunity Fund and Ontario Research Fund (Project#30259), and a Discovery Grant (#418213-2012) from the Natural Sciences and Engineering Research Council (NSERC) of Canada. EBM was supported by an NSERC undergraduate student research fellowship and is the recipient of an NSERC PGS-M Master’s Scholarship.
    Value of the data
    Data We present results from Drosophila genetic modifier screens that can be used to score genetic interactions that impact Hh signal transduction as in [1]. Wing phenotypes induced by dominant negative Smo5A protein [2] were cataloged into buy Exendin-3 (9-39) amide based upon severity of fusions between longitudinal veins 3 and 4 (LV3/LV4, Fig. 1). Classes were used to quantify phenotypic modification resulting from introduction of a loss-of-function allele of the negative pathway regulator Suppressor of Fused (Su(fu), Fig. 2). Loss-of-function alleles of the known positive pathway effector Fused (fu) or select Ras family small G proteins were introduced into the hh gain-of-function background [3,4] and modification of phenotypic class distribution was quantified (Figs. 3 and 4).
    Experimental design, materials and methods A transgene encoding the Smo5A mutant with S/T to A changes of five essential PKA phosphorylation sites (Smo5A) was expressed in the developing wing imaginal disc using the C765-GAL4 driver [2]. Mutant alleles of the indicated genes were crossed into C765>smo5A or hh backgrounds using standard techniques [1]. Wings from ~75–100 male progeny were analyzed from each class to quantify phenotypic modification.
    Acknowledgments This work was supported by SJCRH Comprehensive Cancer Center Developmental Funds from the National Cancer InstituteP30CA021765, National Institute of General Medical Science grant R01GM101087 (S.K.O.) and ALSAC of SJCRH. We thank J. Curtiss, M. Peifer, D. Harrison, U. Gaul, D. Kalderon and the Bloomington Stock Center for fly lines. We thank W. Bodeen for help with establishing the C765>smo5A classes.
    Data We show that STAT5A is downregulated in breast cancer using several large-scale gene expression analyses available at Oncomine: https://www.oncomine.org/resource/main.html[1].
    Experimental design, materials and methods
    Acknowledgements Funded by CIHR to GF (229774).
    Data This article presents data on the HpFlgD stability in terms of the protein size. This investigation was done in order to understand which part of the degraded protein crystallized. The data is based on the CD and mass spectra analysis (RP-HPLC, nano-ESI). In addition, comparison of different types of interfaces found in the crystal structures of the two crystal forms of HpFlgD [1] are given, as well as the amino acid residues responsible for the quaternary structure assembly. The difference between the domain orientation in HpFlgD and the similar domains in other organisms is also shown.