Quantifying measurement: the tyranny of numbers

Measurements and experiments are made each and every day, in fields as disparate as particle physics, chemistry, economics and medicine, but have you ever wondered why it is that a particular experiment has been designed to be the way it is. Indeed, how do you design an experiment to measure something whose value is unknown, and what should your considerations be on deciding whether an experiment has yielded the sought after, or indeed any useful result? These are old questions, and they are the reason behind this volume. We will explore the origins of the methods of data analysis that are today routinely applied to all measurements, but which were unknown before the mid-19th Century. Anyone who is interested in the relationship between the precision and accuracy of measurements will find this volume useful. Whether you are a physicist, a chemist, a social scientist, or a student studying one of these subjects, you will discover that the basis of measurement is the struggle to identify the needle of useful data hidden in the haystack of obscuring background noise

Additional file 1: of Electroacupuncture for abdominal pain relief in patients with acute pancreatitis: study protocol for a randomized controlled trial

SPIRIT 2013 Checklist: Recommended items to address in a clinical trial protocol and related documents. (DOCX 59 kb

Iron chelator induces IL-8 protein secretion (A, C) and IL-8 mRNA accumulation (B, D) in IHOK and HN12 cells in a time-dependent manner

<p><b>Copyright information:</b></p><p>Taken from "Differential regulation of iron chelator-induced IL-8 synthesis via MAP kinase and NF-κB in immortalized and malignant oral keratinocytes"</p><p>http://www.biomedcentral.com/1471-2407/7/176</p><p>BMC Cancer 2007;7():176-176.</p><p>Published online 13 Sep 2007</p><p>PMCID:PMC2078595.</p><p></p> Cells were incubated with DFO (1.0 mM) or IL1-β (10 ng/ml) for the indicated time periods. Levels of IL-8 protein and mRNA were determined by ELISA and semiquantitative RT-PCR, respectively. Numbers below the gels represent the intensity of IL-8 mRNA relative to GAPDH mRNA. These data are representative of three independent experiments

The effect of inhibitor for p38 and ERK MAPK on iron chelator induced IL-8 protein secretion and IL-8 mRNA in IHOK and HN12 cells

<p><b>Copyright information:</b></p><p>Taken from "Differential regulation of iron chelator-induced IL-8 synthesis via MAP kinase and NF-κB in immortalized and malignant oral keratinocytes"</p><p>http://www.biomedcentral.com/1471-2407/7/176</p><p>BMC Cancer 2007;7():176-176.</p><p>Published online 13 Sep 2007</p><p>PMCID:PMC2078595.</p><p></p> IHOK (A) & HN12 cells (C) were pretreated with ERK inhibitor PD98059 and the p38 inhibitor SB203580 for 1 h and followed by the treatment with DFO (1.0 mM) for 16 h. Levels of IL-8 secretion and IL-8 mRNA were determined by ELISA and RT-PCR in IHOK (B) & HN12 cells (D). Same procedure as described in the legend to Fig. 1 was performed. Results are expressed as means ± SD of three independent experiments. *: Statistically significant difference compared to control group: p < 0.05, #: Statistically significant difference compared to DFO group, < 0.05

Surplus skeletal muscle NT3 alters proprioceptor gene expression.

<p>(a, b) Analysis of 25 upregulated (a) or downregulated (b) probes in <i>mlc^NT3</i> mice is displayed. Average values of p0 TrkC^on proprioceptors (left; TrkC) and TrkC^off non-proprioceptors (right; non-TrkC) isolated from wild-type and <i>mlc^NT3</i> mice are shown. Grey scale values represent row z-score values and log unit average expression values are shown to the right of each probe (scales plotted top right of each panel). Probe names are displayed to the left of each row. The number of probes regulated in proprioceptors (p≤0.02; regulation ≥1.5 fold) is shown below the plots. (c, d) Detailed expression analysis of two individual genes upregulated (<i>Igf1</i> and <i>Shc4</i>) and two genes downregulated (<i>Tacr3</i> and <i>Myb</i>) in proprioceptors of <i>mlc^NT3</i> mice is shown (Affymetrix analysis: y-scale displays raw expression values; ±SEM).</p

Iron chelator stabilized IL-8 mRNA through activation of p38 and ERK1/2

<p><b>Copyright information:</b></p><p>Taken from "Differential regulation of iron chelator-induced IL-8 synthesis via MAP kinase and NF-κB in immortalized and malignant oral keratinocytes"</p><p>http://www.biomedcentral.com/1471-2407/7/176</p><p>BMC Cancer 2007;7():176-176.</p><p>Published online 13 Sep 2007</p><p>PMCID:PMC2078595.</p><p></p> IHOK and HN12 cells were treated with DFO (1.0 mM) for 16 h to allow accumulation of IL-8 mRNA. Cells were then treated with the mRNA synthesis inhibitor actinomycin D (ActD; 5 μg/ml), and either ERK pathway inhibitor (PD98059) or p38 inhibitor (SB203580). GAPDH mRNA was used as an endogenous control message. Same procedure as described in the legend to Fig. 1 was performed. Results are representative of three independent experiments

Iron chelator induced phosphorylated IκB-α in IHOK and HN12 cells on time dependent

<p><b>Copyright information:</b></p><p>Taken from "Differential regulation of iron chelator-induced IL-8 synthesis via MAP kinase and NF-κB in immortalized and malignant oral keratinocytes"</p><p>http://www.biomedcentral.com/1471-2407/7/176</p><p>BMC Cancer 2007;7():176-176.</p><p>Published online 13 Sep 2007</p><p>PMCID:PMC2078595.</p><p></p> Cells were treated with DFO (1.0 mM) or IL-1α (10 ng/ml) for the indicated time periods. Levels of IκB-α, p IκB-α were determined by Western blotting. The protein fraction was extracted, electrophoresed, transferred to membrane and blotted with respective antibodies. These data are representative of three independent experiments

Genes with anticorrelation in NT3 regulation profiles.

<p>(a) Flow diagram to illustrate analysis of gene expression data extracted from proprioceptors and non-proprioceptors of various mouse strains. To isolate genes with anticorrelative expression profile, genes with expression changes in opposing directions in proprioceptors of <i>NT3^−/−Bax^−/−</i> mice and <i>mlc^NT3</i> mice were isolated (purple arrows 1 and 2). (b, c) Detailed expression analysis of three individual genes following anticorrelation scheme 1 (<i>Gas6</i>, <i>Ndst4</i>, and <i>Crim1</i>) and three genes following scheme 2 (<i>Mrg1</i>, <i>Nova1</i>, and <i>P2rx1</i>). Affymetrix analysis: y-scale displays raw expression values; ± SEM.</p

Chemical Constituents from the Aerial Parts of <i>Aster koraiensis</i> with Protein Glycation and Aldose Reductase Inhibitory Activities

Two new eudesmane-type sesquiterpene glucosides, 9β-<i>O</i>-(<i>E</i>-<i>p</i>-hydroxycinnamoyl)-1β,6β-dihydroxy-<i>trans</i>-eudesm-3-en-6-<i>O</i>-β-d-glucopyranoside (<b>1</b>) and 9α-<i>O</i>-(<i>E</i>-<i>p</i>-hydroxycinnamoyl)-1α,6α-11-trihydroxy-<i>trans</i>-eudesm-3-en-6-<i>O</i>-β-d-glucopyranoside (<b>2</b>), were isolated by the activity-guided fractionation of an EtOAc-soluble fraction from the aerial parts of <i>Aster koraiensis</i>. A new dihydrobenzofuran glucoside, (2<i>R</i>,3<i>S</i>)-6-acetyl-2-[1-<i>O</i>-(β-d-glucopyranosyl)-2-propenyl]-5-hydroxy-3-methoxy-2,3-dihydrobenzofuran (<b>3</b>), was also isolated, in addition to 15 known compounds. The structures of <b>1</b>–<b>3</b> were determined by spectroscopic data interpretation. All of the isolates were evaluated for in vitro inhibitory activity against the formation of advanced glycation end-products and rat lens aldose reductase

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