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@ARTICLE{Ringer:840578,
      author       = {Ringer, Pia and Weißl, Andreas and Cost, Anna-Lena and
                      Freikamp, Andrea and Sabass, Benedikt and Mehlich, Alexander
                      and Tramier, Marc and Rief, Matthias and Grashoff, Carsten},
      title        = {{M}ultiplexing molecular tension sensors reveals piconewton
                      force gradient across talin-1},
      journal      = {Nature methods},
      volume       = {14},
      number       = {11},
      issn         = {1548-7105},
      address      = {London [u.a.] Nature Publishing Group},
      reportid     = {FZJ-2017-08083},
      pages        = {1090 - 1096},
      year         = {2017},
      abstract     = {Förster resonance energy transfer (FRET)-based tension
                      sensor modules (TSMs) are available for investigating how
                      distinct proteins bear mechanical forces in cells. Yet,
                      forces in the single piconewton (pN) regime remain difficult
                      to resolve, and tools for multiplexed tension sensing are
                      lacking. Here, we report the generation and calibration of a
                      genetically encoded, FRET-based biosensor called FL-TSM,
                      which is characterized by a near-digital force response and
                      increased sensitivity at 3–5 pN. In addition, we present a
                      method allowing the simultaneous evaluation of coexpressed
                      tension sensor constructs using two-color fluorescence
                      lifetime microscopy. Finally, we introduce a procedure to
                      calculate the fraction of mechanically engaged molecules
                      within cells. Application of these techniques to new talin
                      biosensors reveals an intramolecular tension gradient across
                      talin-1 that is established upon integrin-mediated cell
                      adhesion. The tension gradient is actomyosin- and
                      vinculin-dependent and sensitive to the rigidity of the
                      extracellular environment.},
      cin          = {ICS-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-2-20110106},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:28945706},
      UT           = {WOS:000414120400024},
      doi          = {10.1038/nmeth.4431},
      url          = {https://juser.fz-juelich.de/record/840578},
}