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@ARTICLE{Kube:827784,
      author       = {Kube, Sarah and Hersch, Nils and Naumovska, Elena and
                      Gensch, Thomas and Hendriks, Johnny and Franzen, Arne and
                      Landvogt, Lisa and Siebrasse, Jan-Peter and Kubitscheck,
                      Ulrich and Hoffmann, Bernd and Merkel, Rudolf and Csiszár,
                      Agnes},
      title        = {{F}usogenic {L}iposomes as {N}anocarriers for the
                      {D}elivery of {I}ntracellular {P}roteins},
      journal      = {Langmuir},
      volume       = {33},
      number       = {4},
      issn         = {1520-5827},
      address      = {Washington, DC},
      publisher    = {ACS Publ.},
      reportid     = {FZJ-2017-01888},
      pages        = {1051 - 1059},
      year         = {2017},
      abstract     = {Direct delivery of proteins and peptides into living
                      mammalian cells has been accomplished using phospholipid
                      liposomes as carrier particles. Such liposomes are usually
                      taken up via endocytosis where the main part of their cargo
                      is degraded in lysosomes before reaching its destination.
                      Here, fusogenic liposomes, a newly developed molecular
                      carrier system, were used for protein delivery. When such
                      liposomes were loaded with water-soluble proteins and
                      brought into contact with mammalian cells, the liposomal
                      membrane efficiently fused with the cellular plasma membrane
                      delivering the liposomal content to the cytoplasm without
                      degradation. To explore the key factors of proteofection
                      processes, the complex formation of fusogenic liposomes and
                      proteins of interest and the size and zeta potential of the
                      formed fusogenic proteoliposoms were monitored.
                      Intracellular protein delivery was analyzed using
                      fluorescence microscopy and flow cytometry. Proteins such as
                      EGFP, Dendra2, and R-phycoerythrin or peptides such as
                      LifeAct-FITC and NTF2-AlexaFluor488 were successfully
                      incorporated into mammalian cells with high efficiency.
                      Moreover, correct functionality and faithful transport to
                      binding sites were also proven for the imported proteins.},
      cin          = {ICS-7 / ICS-4},
      ddc          = {670},
      cid          = {I:(DE-Juel1)ICS-7-20110106 / I:(DE-Juel1)ICS-4-20110106},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000393269700026},
      pubmed       = {pmid:28059515},
      doi          = {10.1021/acs.langmuir.6b04304},
      url          = {https://juser.fz-juelich.de/record/827784},
}