% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Unsay:141196,
      author       = {J. D. Unsay$^*$ and F. Murad and E. Hermann and J. Ries and
                      A. J. García-Sáez},
      title        = {{S}canning {F}luorescence {C}orrelation {S}pectroscopy for
                      {Q}uantification of the {D}ynamics and {I}nteractions in
                      {T}ube {O}rganelles of {L}iving {C}ells.},
      journal      = {ChemPhysChem},
      volume       = {19},
      number       = {23},
      issn         = {1439-4235},
      address      = {Weinheim},
      publisher    = {Wiley-VCH Verl.},
      reportid     = {DKFZ-2018-01719},
      pages        = {33273-3278},
      year         = {2018},
      note         = {ChemPhysChem2018,19, 3273–3278},
      abstract     = {Single-molecule spectroscopic quantification of
                      protein-protein interactions directly in the organelles of
                      living cells is highly desirable but remains challenging.
                      Bulk methods, such as Förster resonance energy transfer
                      (FRET), currently only give a relative quantification of the
                      strength of protein-protein interactions. Here, we introduce
                      tube scanning fluorescence cross-correlation spectroscopy
                      (tubeSFCCS) for the absolute quantification of diffusion and
                      complex formation of fluorescently labeled molecules in the
                      mitochondrial compartments. We determined the extent of
                      association between the apoptosis regulators Bcl-xL and tBid
                      at the mitochondrial outer membrane of living cells and
                      discovered that practically all mitochondria-bound Bcl-xL
                      and tBid are associated with each other, in contrast to
                      undetectable association in the cytosol. Furthermore, we
                      show further applicability of our method to other
                      mitochondrial proteins, as well as to proteins in the
                      endoplasmic reticulum (ER) membrane.},
      cin          = {B160},
      ddc          = {540},
      cid          = {I:(DE-He78)B160-20160331},
      pnm          = {312 - Functional and structural genomics (POF3-312)},
      pid          = {G:(DE-HGF)POF3-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30335213},
      doi          = {10.1002/cphc.201800705},
      url          = {https://inrepo02.dkfz.de/record/141196},
}