14 research outputs found

    SOSORT consensus paper: school screening for scoliosis. Where are we today?

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    This report is the SOSORT Consensus Paper on School Screening for Scoliosis discussed at the 4th International Conference on Conservative Management of Spinal Deformities, presented by SOSORT, on May 2007. The objectives were numerous, 1) the inclusion of the existing information on the issue, 2) the analysis and discussion of the responses by the meeting attendees to the twenty six questions of the questionnaire, 3) the impact of screening on frequency of surgical treatment and of its discontinuation, 4) the reasons why these programs must be continued, 5) the evolving aim of School Screening for Scoliosis and 6) recommendations for improvement of the procedure

    Different subcellular localizations and functions of Arabidopsis myosin VIII-0

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    P starting from the ATG and a reverse primer corresponding to the 3' end of ATM1 including its stop codon. The size of the expected fragment was 1734 bp. The template DNA was as follows: Lane 1. DNA from transgenic plants expressing GFP-ATM1(IQ-tail). Lane 2. DNA from wt plants. Lane 3. DNA from the plasmid used to generate the transgenic plants. Lane 4. Molecular weight markers. B. Western blot analysis showing sizes and levels of the expressed transgenes: Lane 1. GFP alone. Lane 2. GFP-ATM1(IQ-tail). Detection was performed with anti-GFP antibody.<p><b>Copyright information:</b></p><p>Taken from "Different subcellular localizations and functions of Arabidopsis myosin VIII"</p><p>http://www.biomedcentral.com/1471-2229/8/3</p><p>BMC Plant Biology 2008;8():3-3.</p><p>Published online 8 Jan 2008</p><p>PMCID:PMC2275265.</p><p></p

    Different subcellular localizations and functions of Arabidopsis myosin VIII-2

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    D with a confocal microscope. A-B. Cells with GFP-ATM1(IQ-tail) organized in dots (arrows). A. GFP-ATM1. B. BFA bodies formed in these cells, shown by FM4-64. Note that the dotted pattern is not disrupted by the treatment (arrows). C. Overlay of A and B. Scale bar 10 μm. D-F Showing cells near the root cap where ATM1 is found in BFA bodies. D. GFP-ATM1, E. BFA bodies stained by FM4-64, F. overlay of D and E. Scale bar 10 μm. All images in this figure are composed of one optic section.<p><b>Copyright information:</b></p><p>Taken from "Different subcellular localizations and functions of Arabidopsis myosin VIII"</p><p>http://www.biomedcentral.com/1471-2229/8/3</p><p>BMC Plant Biology 2008;8():3-3.</p><p>Published online 8 Jan 2008</p><p>PMCID:PMC2275265.</p><p></p

    Different subcellular localizations and functions of Arabidopsis myosin VIII-6

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    Ocal microscopy. A. Root of 5-day-old seedling. Scale bar: 50 μm. B. Lateral root of 20-day-old seedling. Scale bar: 20 μm. C(1) and C(2). Two images of the same 20-day-old seedling root. C(1) shows the root cap, scale bar: 20 μm, and C(2) shows the upper part. Scale bar: 50 μm. A similar pattern of GFP-ATM1 localization is seen in all roots: diffuse at the root cap, then dots, then more polarized organization along the transverse sides. D. GFP-ATM1 in root hair, scale bar: 10 μm. Arrows show the direction of the root caps.<p><b>Copyright information:</b></p><p>Taken from "Different subcellular localizations and functions of Arabidopsis myosin VIII"</p><p>http://www.biomedcentral.com/1471-2229/8/3</p><p>BMC Plant Biology 2008;8():3-3.</p><p>Published online 8 Jan 2008</p><p>PMCID:PMC2275265.</p><p></p

    Different subcellular localizations and functions of Arabidopsis myosin VIII-5

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    P starting from the ATG and a reverse primer corresponding to the 3' end of ATM1 including its stop codon. The size of the expected fragment was 1734 bp. The template DNA was as follows: Lane 1. DNA from transgenic plants expressing GFP-ATM1(IQ-tail). Lane 2. DNA from wt plants. Lane 3. DNA from the plasmid used to generate the transgenic plants. Lane 4. Molecular weight markers. B. Western blot analysis showing sizes and levels of the expressed transgenes: Lane 1. GFP alone. Lane 2. GFP-ATM1(IQ-tail). Detection was performed with anti-GFP antibody.<p><b>Copyright information:</b></p><p>Taken from "Different subcellular localizations and functions of Arabidopsis myosin VIII"</p><p>http://www.biomedcentral.com/1471-2229/8/3</p><p>BMC Plant Biology 2008;8():3-3.</p><p>Published online 8 Jan 2008</p><p>PMCID:PMC2275265.</p><p></p

    Different subcellular localizations and functions of Arabidopsis myosin VIII-4

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    ATM1(IQ-tail) (dots of 980 ± 145 nm in diameter). B. FM4-64. C. Overlay of A and B (1 optic section). D. GFP-ATM1(IQ-tail) (dots of 630 ± 60 nm). E. FYVE-DsRED. F. Overlay of D and E (1 optic section). G. RFP-ATM1(IQ-tail) (dots of 300 ± 100, colored green for ease of demonstration). H. GFP-ARA7 (colored magenta for ease of demonstration). I. Overlay of G and H (1 optic section). J. RFP-ATM1(IQ-tail) (dots of 570 ± 75 nm, colored green for ease of demonstration). K. ARA6-GFP (colored magenta for ease of demonstration). L. Overlay of J. and K (1 optic section). Arrows show co-localization. Scale bars 5 μm. The microscope focus in A-I was in the cytoplasm while the focus in J-L was on the plasma membrane.<p><b>Copyright information:</b></p><p>Taken from "Different subcellular localizations and functions of Arabidopsis myosin VIII"</p><p>http://www.biomedcentral.com/1471-2229/8/3</p><p>BMC Plant Biology 2008;8():3-3.</p><p>Published online 8 Jan 2008</p><p>PMCID:PMC2275265.</p><p></p

    Importin 7 and Exportin 1 Link c-Myc and p53 to Regulation of Ribosomal Biogenesis

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    Members of the β-karyopherin family mediate nuclear import of ribosomal proteins and export of ribosomal subunits, required for ribosome biogenesis. We report that transcription of the β-karyopherin genes importin 7 (IPO7) and exportin 1 (XPO1), and several additional nuclear import receptors, is regulated positively by c-Myc and negatively by p53. Partial IPO7 depletion triggers p53 activation and p53-dependent growth arrest. Activation of p53 by IPO7 knockdown has distinct features of ribosomal biogenesis stress, with increased binding of Mdm2 to ribosomal proteins L5 and L11 (RPL5 and RPL11). Furthermore, p53 activation is dependent on RPL5 and RPL11. Of note, IPO7 and XPO1 are frequently overexpressed in cancer. Altogether, we propose that c-Myc and p53 counter each other in the regulation of elements within the nuclear transport machinery, thereby exerting opposing effects on the rate of ribosome biogenesis. Perturbation of this balance may play a significant role in promoting cancer
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