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@ARTICLE{Najbauer:156026,
      author       = {Najbauer, Eszter E and Becker, Stefan and Giller, Karin and
                      Zweckstetter, Markus and Lange, Adam and Steinem, Claudia
                      and de Groot, Bert L and Griesinger, Christian and Andreas,
                      Loren B},
      title        = {{S}tructure, gating and interactions of the
                      voltage-dependent anion channel.},
      journal      = {European biophysics journal},
      volume       = {50},
      number       = {2},
      issn         = {1432-1017},
      address      = {New York},
      publisher    = {Springer},
      reportid     = {DZNE-2021-01158},
      pages        = {159 - 172},
      year         = {2021},
      abstract     = {The voltage-dependent anion channel (VDAC) is one of the
                      most highly abundant proteins found in the outer
                      mitochondrial membrane, and was one of the earliest
                      discovered. Here we review progress in understanding VDAC
                      function with a focus on its structure, discussing various
                      models proposed for voltage gating as well as potential drug
                      targets to modulate the channel's function. In addition, we
                      explore the sensitivity of VDAC structure to variations in
                      the membrane environment, comparing DMPC-only, DMPC with
                      cholesterol, and near-native lipid compositions, and use
                      magic-angle spinning NMR spectroscopy to locate cholesterol
                      on the outside of the β-barrel. We find that the VDAC
                      protein structure remains unchanged in different membrane
                      compositions, including conditions with cholesterol.},
      keywords     = {Ion Channel Gating / Molecular Dynamics Simulation /
                      Voltage-Dependent Anion Channels: chemistry /
                      Voltage-Dependent Anion Channels: metabolism /
                      Electrophysiology (Other) / Magic-angle spinning (Other) /
                      Membrane protein (Other) / Molecular dynamics simulations
                      (Other) / Solid-state NMR (Other) / Voltage dependent anion
                      channel (Other)},
      cin          = {AG Zweckstetter},
      ddc          = {570},
      cid          = {I:(DE-2719)1410001},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:33782728},
      pmc          = {pmc:PMC8071794},
      doi          = {10.1007/s00249-021-01515-7},
      url          = {https://pub.dzne.de/record/156026},
}