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Träfflista för sökning "WFRF:(Nilsson Christer) ;pers:(Wingren Christer)"

Sökning: WFRF:(Nilsson Christer) > Wingren Christer

  • Resultat 1-9 av 9
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1.
  • El-Schich, Zahra, et al. (författare)
  • Interfacing antibody-based microarrays and digital holography enables label-free detection for loss of cell volume
  • 2015
  • Ingår i: Future Science OA. - : Future Science Group. - 2056-5623. ; 1:3
  • Tidskriftsartikel (refereegranskat)abstract
    • Background: We introduce the combination of digital holographic microscopy (DHM) and antibody microarrays as a powerful tool to measure morphological changes in specifically antibody-captured cells. The aim of the study was to develop DHM for analysis of cell death of etoposide-treated suspension cells. Result/Methodology: We demonstrate that the cell number, mean area, thickness, and volume were non-invasively measured by using DHM. The cell number was stable over time, but the two cell lines showed changes of cell area and cell irregularity after treatment. The cell volume in etoposide-treated cells was decreased, whereas untreated cells showed stable volume. Conclusions: Our results provide proof of concept for using DHM combined with antibody-based microarray technology for detecting morphological changes in captured cells.
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2.
  • Ellmark, Peter, et al. (författare)
  • Attovial-based antibody nanoarrays.
  • 2009
  • Ingår i: Proteomics. - : Wiley. - 1615-9861 .- 1615-9853. ; 9:24, s. 5406-5413
  • Tidskriftsartikel (refereegranskat)abstract
    • Antibody array-based technology is a powerful emerging tool in proteomics, but to enable global proteome analysis, antibody array layouts with even higher density has to be developed. To this end, we have further developed the first generation of a nanoarray platform, based on attoliter sized vials, attovials, which we have characterized and used for the detection of complement factor C1q in human serum samples. Finally, we demonstrated proof-of-concept for individual functionalisation of the attovials with a recombinant antibody.
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  • Ghatnekar-Nilsson, Sara, et al. (författare)
  • Design of atto-vial based recombinant antibody arrays combined with a planar wave-guide detection system
  • 2007
  • Ingår i: Proteomics. - : Wiley. - 1615-9861 .- 1615-9853. ; 7:4, s. 540-547
  • Tidskriftsartikel (refereegranskat)abstract
    • Antibody microarray is a rapidly emerging, powerful approach with great promise within high-throughput proteomics. However, before a truly proteome-wide analysis can be performed, the antibody array format needs to be miniaturized even further in order to enable ultradense arrays to be fabricated. To this end, we have designed and generated proof-of-concept for the first generation of an atto-vial based recombinant antibody array platform. Briefly, we have designed a novel nanostructured substrate using electron beam lithography. Vials, ranging in volume/size from 6 (200 nm in diameter) to 4000 aL (5 mu m in diameter), were fabricated. Human recombinant single-chain Fv antibody fragments, microarray adopted by design, were used as probes. The set-up was interfaced with planar wave-guide technology for evanescant field fluorescence detection. The results showed that protein analytes could be specifically detected in the subzeptomole range for pure systems, using vials down to 57 aL. Further, low-abundant (pg/mL) protein analytes could be detected in directly labeled complex proteomes, such as human whole serum, using 157 aL-vials. Taken together, these results outline the potential of the atto-vial array set-up for miniaturized affinity proteomics-based approaches.
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  • Olsson, Niclas, et al. (författare)
  • Proteomic analysis and discovery using affinity proteomics and mass spectrometry.
  • 2011
  • Ingår i: Molecular & Cellular Proteomics. - 1535-9484. ; 10
  • Tidskriftsartikel (refereegranskat)abstract
    • Antibody-based microarrays are a rapidly evolving affinity-proteomic methodology that recently has shown great promise in clinical applications. The resolution of these proteomic analyses is, however, directly related to the number of data-points, i.e. antibodies, included on the array. Currently, this is a key bottleneck due to limited availability of numerous highly-characterized antibodies. Here, we present a conceptually new method, denoted global proteome survey, opening up the possibility to probe any proteome in a species independent manner while still using a limited set of antibodies. We use context-independent-motif-specific antibodies directed against short amino acid motifs, where each motif is present in up to a few hundred different proteins. First, the digested proteome is exposed to these antibodies, whereby motif-containing peptides are enriched, which then are detected and identified by mass spectrometry. In this study, we profiled extracts from human colon tissue, yeast cells lysate, and mouse liver tissue to demonstrate proof-of-concept.
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7.
  • Söderlind, Eskil, et al. (författare)
  • Recombining germline-derived CDR sequences for creating diverse single-framework antibody libraries
  • 2000
  • Ingår i: Nature Biotechnology. - : Springer Science and Business Media LLC. - 1087-0156 .- 1546-1696. ; 18:8, s. 852-856
  • Tidskriftsartikel (refereegranskat)abstract
    • We constructed a single-chain Fv antibody library that permits human complementarity-determining region (CDR) gene fragments of any germline to be incorporated combinatorially into the appropriate positions of the variable-region frameworks VH-DP47 and VL-DPL3. A library of 2 x 109 independent transformants was screened against haptens, peptides, carbohydrates, and proteins, and the selected antibody fragments exhibited dissociation constants in the subnanomolar range. The antibody genes in this library were built on a single master framework into which diverse CDRs were allowed to recombine. These CDRs were sampled from in vivo-processed gene sequences, thus potentially optimizing the levels of correctly folded and functional molecules, and resulting in a molecule exhibiting a lower computed immunogenicity compared to naive immunoglobulins. Using the modularized assembly process to incorporate foreign sequences into an immunoglobulin scaffold, it is possible to vary as many as six CDRs at the same time, creating genetic and funcfional variation in antibody molecules.
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  • Resultat 1-9 av 9

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