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Träfflista för sökning "WFRF:(Gullberg Mats) ;pers:(Larsson Lars Gunnar)"

Sökning: WFRF:(Gullberg Mats) > Larsson Lars Gunnar

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  • Söderberg, Ola, et al. (författare)
  • Characterizing proteins and their interactions in cells and tissues using the in situ proximity ligation assay.
  • 2008
  • Ingår i: Methods. - : Elsevier BV. - 1046-2023 .- 1095-9130. ; 45:3, s. 227-32
  • Tidskriftsartikel (refereegranskat)abstract
    • The activity of proteins is typically regulated by secondary modifications and by interactions with other partners, resulting in the formation of protein complexes whose functions depend on the participating proteins. Accordingly, it is of central importance to monitor the presence of interaction complexes as well as their localization, thus providing information about the types of cells where the proteins are located and in what sub-cellular compartment these interactions occur. Several methods for visualizing protein interactions in situ have been developed during the last decade. These methods in most cases involve genetic constructs, and they have been successfully used in assays of living cell maintained in tissue culture, but they cannot easily be implemented in studies of clinical specimens. For such samples, affinity reagents like antibodies can be used to target the interacting proteins. In this review we will describe the in situ proximity ligation assays (in situ PLA), a method that is suitable for visualizing protein interactions in both tissue sections and in vitro cell lines, and we discuss research tasks when this or other method may be selected.
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  • Söderberg, Ola, et al. (författare)
  • Direct observation of individual endogenous protein complexes in situ by proximity ligation
  • 2006
  • Ingår i: Nature Methods. - : Springer Science and Business Media LLC. - 1548-7091 .- 1548-7105. ; 3:12, s. 995-1000
  • Tidskriftsartikel (refereegranskat)abstract
    • Cellular processes can only be understood as the dynamic interplay of molecules. There is a need for techniques to monitor interactions of endogenous proteins directly in individual cells and tissues to reveal the cellular and molecular architecture and its responses to perturbations. Here we report our adaptation of the recently developed proximity ligation method to examine the subcellular localization of protein-protein interactions at single-molecule resolution. Proximity probes-oligonucleotides attached to antibodies against the two target proteins-guided the formation of circular DNA strands when bound in close proximity. The DNA circles in turn served as templates for localized rolling-circle amplification (RCA), allowing individual interacting pairs of protein molecules to be visualized and counted in human cell lines and clinical specimens. We used this method to show specific regulation of protein-protein interactions between endogenous Myc and Max oncogenic transcription factors in response to interferon-gamma (IFN-gamma) signaling and low-molecular-weight inhibitors.
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