7 research outputs found

    Interactions among genes in the ErbB-Neuregulin signalling network are associated with increased susceptibility to schizophrenia-0

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    <p><b>Copyright information:</b></p><p>Taken from "Interactions among genes in the ErbB-Neuregulin signalling network are associated with increased susceptibility to schizophrenia"</p><p>http://www.behavioralandbrainfunctions.com/content/3/1/31</p><p>Behavioral and Brain Functions 2007;3():31-31.</p><p>Published online 28 Jun 2007</p><p>PMCID:PMC1934910.</p><p></p>intervals. The region covered by the gene is indicated in the centre of the figure by a horizontal line, with an arrow head indicating the direction of transcription. A crossing vertical line indicates the position of each exon. At the base of the figure, LD between SNP loci is indicated by shading. White: = 0; black: = 1

    Interactions among genes in the ErbB-Neuregulin signalling network are associated with increased susceptibility to schizophrenia-3

    No full text
    <p><b>Copyright information:</b></p><p>Taken from "Interactions among genes in the ErbB-Neuregulin signalling network are associated with increased susceptibility to schizophrenia"</p><p>http://www.behavioralandbrainfunctions.com/content/3/1/31</p><p>Behavioral and Brain Functions 2007;3():31-31.</p><p>Published online 28 Jun 2007</p><p>PMCID:PMC1934910.</p><p></p>action presented in that table for the gene combination in question

    Large-Scale Label-Free Quantitative Mapping of the Sputum Proteome

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    Analysis of induced sputum supernatant is a minimally invasive approach to study the epithelial lining fluid and, thereby, provide insight into normal lung biology and the pathobiology of lung diseases. We present here a novel proteomics approach to sputum analysis developed within the U-BIOPRED (unbiased biomarkers predictive of respiratory disease outcomes) international project. We present practical and analytical techniques to optimize the detection of robust biomarkers in proteomic studies. The normal sputum proteome was derived using data-independent HDMS<sup>E</sup> applied to 40 healthy nonsmoking participants, which provides an essential baseline from which to compare modulation of protein expression in respiratory diseases. The ā€œcoreā€ sputum proteome (proteins detected in ā‰„40% of participants) was composed of 284 proteins, and the extended proteome (proteins detected in ā‰„3 participants) contained 1666 proteins. Quality control procedures were developed to optimize the accuracy and consistency of measurement of sputum proteins and analyze the distribution of sputum proteins in the healthy population. The analysis showed that quantitation of proteins by HDMS<sup>E</sup> is influenced by several factors, with some proteins being measured in all participantsā€™ samples and with low measurement variance between samples from the same patient. The measurement of some proteins is highly variable between repeat analyses, susceptible to sample processing effects, or difficult to accurately quantify by mass spectrometry. Other proteins show high interindividual variance. We also highlight that the sputum proteome of healthy individuals is related to sputum neutrophil levels, but not gender or allergic sensitization. We illustrate the importance of design and interpretation of disease biomarker studies considering such protein population and technical measurement variance

    Large-Scale Label-Free Quantitative Mapping of the Sputum Proteome

    No full text
    Analysis of induced sputum supernatant is a minimally invasive approach to study the epithelial lining fluid and, thereby, provide insight into normal lung biology and the pathobiology of lung diseases. We present here a novel proteomics approach to sputum analysis developed within the U-BIOPRED (unbiased biomarkers predictive of respiratory disease outcomes) international project. We present practical and analytical techniques to optimize the detection of robust biomarkers in proteomic studies. The normal sputum proteome was derived using data-independent HDMS<sup>E</sup> applied to 40 healthy nonsmoking participants, which provides an essential baseline from which to compare modulation of protein expression in respiratory diseases. The ā€œcoreā€ sputum proteome (proteins detected in ā‰„40% of participants) was composed of 284 proteins, and the extended proteome (proteins detected in ā‰„3 participants) contained 1666 proteins. Quality control procedures were developed to optimize the accuracy and consistency of measurement of sputum proteins and analyze the distribution of sputum proteins in the healthy population. The analysis showed that quantitation of proteins by HDMS<sup>E</sup> is influenced by several factors, with some proteins being measured in all participantsā€™ samples and with low measurement variance between samples from the same patient. The measurement of some proteins is highly variable between repeat analyses, susceptible to sample processing effects, or difficult to accurately quantify by mass spectrometry. Other proteins show high interindividual variance. We also highlight that the sputum proteome of healthy individuals is related to sputum neutrophil levels, but not gender or allergic sensitization. We illustrate the importance of design and interpretation of disease biomarker studies considering such protein population and technical measurement variance

    Large-Scale Label-Free Quantitative Mapping of the Sputum Proteome

    No full text
    Analysis of induced sputum supernatant is a minimally invasive approach to study the epithelial lining fluid and, thereby, provide insight into normal lung biology and the pathobiology of lung diseases. We present here a novel proteomics approach to sputum analysis developed within the U-BIOPRED (unbiased biomarkers predictive of respiratory disease outcomes) international project. We present practical and analytical techniques to optimize the detection of robust biomarkers in proteomic studies. The normal sputum proteome was derived using data-independent HDMS<sup>E</sup> applied to 40 healthy nonsmoking participants, which provides an essential baseline from which to compare modulation of protein expression in respiratory diseases. The ā€œcoreā€ sputum proteome (proteins detected in ā‰„40% of participants) was composed of 284 proteins, and the extended proteome (proteins detected in ā‰„3 participants) contained 1666 proteins. Quality control procedures were developed to optimize the accuracy and consistency of measurement of sputum proteins and analyze the distribution of sputum proteins in the healthy population. The analysis showed that quantitation of proteins by HDMS<sup>E</sup> is influenced by several factors, with some proteins being measured in all participantsā€™ samples and with low measurement variance between samples from the same patient. The measurement of some proteins is highly variable between repeat analyses, susceptible to sample processing effects, or difficult to accurately quantify by mass spectrometry. Other proteins show high interindividual variance. We also highlight that the sputum proteome of healthy individuals is related to sputum neutrophil levels, but not gender or allergic sensitization. We illustrate the importance of design and interpretation of disease biomarker studies considering such protein population and technical measurement variance
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