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Development of a novel peptide microarray for large-scale epitope mapping of food allergens
Lin, Jing,Bardina, Ludmilla,Shreffler, Wayne G.,Andreae, Doerthe A.,Ge, Yongchao,Wang, Julie,Bruni, Francesca M.,Fu, Zhiyan,Han, Youngshin,Sampson, Hugh A. Elsevier 2009 The Journal of allergy and clinical immunology Vol.124 No.2
<P><B>Background</B></P><P>The peptide microarray is a novel assay that facilitates high-throughput screening of peptides with a small quantity of sample.</P><P><B>Objective</B></P><P>We sought to use overlapping peptides of milk allergenic proteins as a model system to establish a reliable and sensitive peptide microarray-based immunoassay for large-scale epitope mapping of food allergens.</P><P><B>Methods</B></P><P>A milk peptide microarray was developed by using commercially synthesized peptides (20-mers, 3 offset) covering the primary sequences of α<SUB>s1</SUB>-casein, α<SUB>s2</SUB>-casein, β-casein, κ-casein, and β-lactoglobulin. Conditions for printing and immunolabeling were optimized using a serum pool of 5 patients with milk allergy. Reproducibility of the milk peptide microarray was evaluated using replicate arrays immunolabeled with the serum pool, whereas specificity and sensitivity were assessed by using serial dilution of the serum pool and a peptide inhibition assay.</P><P><B>Results</B></P><P>Our results show that epitopes identified by the peptide microarray were mostly consistent with those identified previously by SPOT membrane technology, but with specific binding to a few newly identified epitopes of milk allergens. Data from replicate arrays were reproducible (<I>r</I> ≥ 0.92) regardless of printing lots, immunolabeling, and serum pool batches. Using the serially diluted serum pool, we confirmed that IgE antibody binding detected in the array was specific. Peptide inhibition of IgE binding to the same peptide and overlapping peptides further confirmed the specificity of the array.</P><P><B>Conclusion</B></P><P>A reliable peptide microarray was established for large-scale IgE epitope mapping of milk allergens, and this robust technology could be applied for epitope mapping of other food allergens.</P>
Wilson, William C.,Hornig-Do, Hue-Tran,Bruni, Francesco,Chang, Jeong Ho,Jourdain, Alexis A.,Martinou, Jean-Claude,Falkenberg, Maria,Spå,hr, Henrik,Larsson, Nils-Gö,ran,Lewis, Richard J.,Hewit Oxford University Press 2014 Human Molecular Genetics Vol.23 No.23
<P>The p.N478D missense mutation in human mitochondrial poly(A) polymerase (mtPAP) has previously been implicated in a form of spastic ataxia with optic atrophy. In this study, we have investigated fibroblast cell lines established from family members. The homozygous mutation resulted in the loss of polyadenylation of all mitochondrial transcripts assessed; however, oligoadenylation was retained. Interestingly, this had differential effects on transcript stability that were dependent on the particular species of transcript. These changes were accompanied by a severe loss of oxidative phosphorylation complexes I and IV, and perturbation of <I>de novo</I> mitochondrial protein synthesis. Decreases in transcript polyadenylation and in respiratory chain complexes were effectively rescued by overexpression of wild-type mtPAP. Both mutated and wild-type mtPAP localized to the mitochondrial RNA-processing granules thereby eliminating mislocalization as a cause of defective polyadenylation. <I>In vitro</I> polyadenylation assays revealed severely compromised activity by the mutated protein, which generated only short oligo(A) extensions on RNA substrates, irrespective of RNA secondary structure. The addition of LRPPRC/SLIRP, a mitochondrial RNA-binding complex, enhanced activity of the wild-type mtPAP resulting in increased overall tail length. The LRPPRC/SLIRP effect although present was less marked with mutated mtPAP, independent of RNA secondary structure. We conclude that (i) the polymerase activity of mtPAP can be modulated by the presence of LRPPRC/SLIRP, (ii) N478D mtPAP mutation decreases polymerase activity and (iii) the alteration in poly(A) length is sufficient to cause dysregulation of post-transcriptional expression and the pathogenic lack of respiratory chain complexes.</P>
ZEUS Collaboration,Chekanov, S.,Derrick, M.,Magill, S.,Musgrave, B.,Nicholass, D.,Repond, J.,Yoshida, R.,Mattingly, M.C.K.,Antonioli, P.,Bari, G.,Bellagamba, L.,Boscherini, D.,Bruni, A.,Bruni, G.,Cind North-Holland Pub. Co 2009 Physics letters: B Vol.672 No.2
A search for events with an isolated high-energy lepton and large missing transverse momentum has been performed with the ZEUS detector at HERA using a total integrated luminosity of 504 pb<SUP>-1</SUP>. The results agree well with Standard Model predictions. The cross section for production of single W bosons in electron-proton collisions with unpolarised electrons is measured to be 0.89<SUB>-0.22</SUB><SUP>+0.25</SUP>(stat.)+/-0.10(syst.)pb.
Measurement of D ± and D 0 production in deep inelastic scattering using a lifetime tag at HERA
Chekanov, S.,Derrick, M.,Magill, S.,Musgrave, B.,Nicholass, D.,Repond, J.,Yoshida, R.,Mattingly, M. C. K.,Antonioli, P.,Bari, G.,Bellagamba, L.,Boscherini, D.,Bruni, A.,Bruni, G.,Cindolo, F.,Corradi, Springer-Verlag 2009 European Physical Journal C Vol.63 No.2
Production of excited charm and charm-strange mesons at HERA
Chekanov, S.,Derrick, M.,Magill, S.,Musgrave, B.,Nicholass, D.,Repond, J.,Yoshida, R.,Mattingly, M. C. K.,Antonioli, P.,Bari, G.,Bellagamba, L.,Boscherini, D.,Bruni, A.,Bruni, G.,Cindolo, F.,Corradi, Springer-Verlag 2009 European Physical Journal C Vol.60 No.1
Measurement of J/ψ photoproduction at large momentum transfer at HERA
Chekanov, S.,Derrick, M.,Magill, S.,Musgrave, B.,Nicholass, D.,Repond, J.,Yoshida, R.,Mattingly, M. C. K.,Antonioli, P.,Bari, G.,Bellagamba, L.,Boscherini, D.,Bruni, A.,Bruni, G.,Cindolo, F.,Corradi, Springer-Verlag 2010 Journal of high energy physics Vol.2010 No.5
Measurement of the longitudinal proton structure function at HERA
ZEUS Collaboration,Chekanov, S.,Derrick, M.,Magill, S.,Musgrave, B.,Nicholass, D.,Repond, J.,Yoshida, R.,Mattingly, M.C.K.,Antonioli, P.,Bari, G.,Bellagamba, L.,Boscherini, D.,Bruni, A.,Bruni, G.,Cind North-Holland Pub. Co 2009 Physics letters: B Vol.682 No.1
The reduced cross sections for ep deep inelastic scattering have been measured with the ZEUS detector at HERA at three different centre-of-mass energies, 318, 251 and 225 GeV. From the cross sections, measured double differentially in Bjorken x and the virtuality, Q<SUP>2</SUP>, the proton structure functions F<SUB>L</SUB> and F<SUB>2</SUB> have been extracted in the region 5x10<SUP>-4</SUP><x<0.007 and 20<Q<SUP>2</SUP><130 GeV<SUP>2</SUP>.