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@ARTICLE{Giani:280487,
      author       = {Giani, M. and den Otter, W. K. and Briels, Willem},
      title        = {{C}lathrin assembly regulated by adaptor proteins in
                      coarse-grained models},
      journal      = {Biophysical journal},
      volume       = {111},
      number       = {1},
      issn         = {0006-3495},
      address      = {Cambridge, Mass.},
      publisher    = {Cell Press},
      reportid     = {FZJ-2016-00257},
      pages        = {222-235},
      year         = {2016},
      abstract     = {The assembly of clathrin triskelia into polyhedral cages
                      during endocytosis is regulated by adaptor proteins (APs).
                      We explore how APs achieve this by developing coarse-grained
                      models for clathrin and AP2, employing a Monte Carlo click
                      interaction, to simulate their collective aggregation
                      behavior. The phase diagrams indicate that a crucial role is
                      played by the mechanical properties of the disordered linker
                      segment of AP. We also present a statistical-mechanical
                      theory for the assembly behavior of clathrin, yielding good
                      agreement with our simulations and experimental data from
                      the literature. Adaptor proteins are found to regulate the
                      formation of clathrin coats under certain conditions, but
                      can also suppress the formation of cages.},
      cin          = {ICS-3},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-3-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000380371400024},
      doi          = {10.1016/j.bpj.2016.06.003},
      url          = {https://juser.fz-juelich.de/record/280487},
}