% 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:119256,
      author       = {J. D. Unsay$^*$ and K. Cosentino and K. Sporbeck and A. J.
                      García-Sáez},
      title        = {{P}ro-apoptotic c{B}id and {B}ax exhibit distinct membrane
                      remodeling activities: {A}n {AFM} study.},
      journal      = {Biochimica et biophysica acta / Biomembranes},
      volume       = {1859},
      number       = {1},
      issn         = {0005-2736},
      address      = {Amsterdam},
      publisher    = {Elsevier},
      reportid     = {DKFZ-2017-00042},
      pages        = {17 - 27},
      year         = {2017},
      abstract     = {Bcl-2 proteins are key regulators of the mitochondrial
                      outer membrane (MOM) permeabilization that mediates
                      apoptosis. During apoptosis, Bid is cleaved (cBid) and
                      translocates to the MOM, where it activates Bax. Bax then
                      oligomerizes and induces MOM permeabilization. However,
                      little is known about how these proteins affect membrane
                      organization aside from pore formation. In previous studies,
                      we have shown that both cBid and Bax are able to remodel
                      membranes and stabilize curvature. Here, we dissected the
                      independent effects of Bax and cBid on supported lipid
                      structures mimicking the mitochondrial composition by means
                      of atomic force spectroscopy. We show that cBid did not
                      permeabilize the membrane but lowered the membrane
                      breakthrough force. On the other hand, Bax effects were
                      dependent on its oligomeric state. Monomeric Bax did not
                      affect the membrane properties. In contrast, oligomeric Bax
                      lowered the breakthrough force of the membrane, which in the
                      context of pore formation, implies a lowering of the line
                      tension at the edge of the pore.},
      cin          = {B160},
      ddc          = {570},
      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:27755971},
      doi          = {10.1016/j.bbamem.2016.10.007},
      url          = {https://inrepo02.dkfz.de/record/119256},
}