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@ARTICLE{Hudina:1049088,
      author       = {Hudina, Esther and Junglas, Benedikt and Sachse, Carsten},
      title        = {{P}lastizität bakterieller {ESCRT}-{III}-{S}trukturen bei
                      der {M}embranremodellierung},
      journal      = {Biospektrum},
      volume       = {31},
      number       = {7},
      issn         = {0947-0867},
      address      = {Heidelberg},
      publisher    = {Springer Nature},
      reportid     = {FZJ-2025-05180},
      pages        = {723 - 726},
      year         = {2025},
      abstract     = {Bacterial ESCRT-III proteins protect and maintain the
                      structural integrity of prokaryotic membranes. Cryo-electron
                      microscopy studies of ESCRT-III family members PspA and
                      Vipp1 revealed the structural basis of helical rod, ring and
                      stacked ring assembly formation. Although the basic
                      ESCRT-III fold remained conserved in the observed
                      structures, monomers adopted a remarkable degree of
                      structural plasticity. Minor conformational changes resulted
                      in major shifts in assembly architectures and are important
                      for the ability to remodel membranes.},
      cin          = {ER-C-3},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ER-C-3-20170113},
      pnm          = {5352 - Understanding the Functionality of Soft Matter and
                      Biomolecular Systems (POF4-535) / 5241 - Molecular
                      Information Processing in Cellular Systems (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5352 / G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1007/s12268-025-2597-3},
      url          = {https://juser.fz-juelich.de/record/1049088},
}