% 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{Fenz:834206,
      author       = {Fenz, Susanne F. and Bihr, Timo and Schmidt, Daniel and
                      Merkel, Rudolf and Seifert, Udo and Sengupta, Kheya and
                      Smith, Ana-Sunčana},
      title        = {{M}embrane fluctuations mediate lateral interaction between
                      cadherin bonds},
      journal      = {Nature physics},
      volume       = {13},
      issn         = {1745-2481},
      address      = {Basingstoke},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2017-04189},
      pages        = {906–913},
      year         = {2017},
      abstract     = {The integrity of living tissues is maintained by adhesion
                      domains of trans-bonds formed between cadherin proteins
                      residing on opposing membranes of neighbouring cells. These
                      domains are stabilized by lateral cis-interactions between
                      the cadherins on the same cell. However, the origin of
                      cis-interactions remains perplexing since they are detected
                      only in the context of trans-bonds. By combining
                      experimental, analytical and computational approaches, we
                      identify bending fluctuations of membranes as a source of
                      long-range cis-interactions, and a regulator of
                      trans-interactions. Specifically, nanometric membrane
                      bending and fluctuations introduce cooperative effects that
                      modulate the affinity and binding/unbinding rates for
                      trans-dimerization, dramatically affecting the nucleation
                      and growth of adhesion domains. Importantly, this regulation
                      relies on physical principles and not on details of
                      protein–protein interactions. These omnipresent
                      fluctuations can thus act as a generic control mechanism in
                      all types of cell adhesion, suggesting a hitherto unknown
                      physiological role for recently identified active
                      fluctuations of cellular membranes.},
      cin          = {ICS-7},
      ddc          = {530},
      cid          = {I:(DE-Juel1)ICS-7-20110106},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000409235100026},
      doi          = {10.1038/nphys4138},
      url          = {https://juser.fz-juelich.de/record/834206},
}