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@ARTICLE{Vlasov:907887,
      author       = {Vlasov, Alexey V. and Osipov, Stepan D. and Bondarev,
                      Nikolay A. and Uversky, Vladimir N. and Borshchevskiy,
                      Valentin and Yanyushin, Mikhail F. and Manukhov, Ilya V. and
                      Rogachev, Andrey V. and Vlasova, Anastasiia D. and Ilyinsky,
                      Nikolay S. and Kuklin, Alexandr I. and Dencher, Norbert A.
                      and Gordeliy, Valentin I.},
      title        = {{ATP} synthase {FOF}1 structure, function, and
                      structure-based drug design},
      journal      = {Cellular and molecular life sciences},
      volume       = {79},
      number       = {3},
      issn         = {0014-4754},
      address      = {Cham (ZG)},
      publisher    = {Springer International Publishing AG},
      reportid     = {FZJ-2022-02267},
      pages        = {179},
      year         = {2022},
      abstract     = {ATP synthases are unique rotatory molecular machines that
                      supply biochemical reactions with adenosine triphosphate
                      (ATP)—the universal “currency”, which cells use for
                      synthesis of vital molecules and sustaining life. ATP
                      synthases of F-type (FOF1) are found embedded in bacterial
                      cellular membrane, in thylakoid membranes of chloroplasts,
                      and in mitochondrial inner membranes in eukaryotes. The main
                      functions of ATP synthases are control of the ATP synthesis
                      and transmembrane potential. Although the key subunits of
                      the enzyme remain highly conserved, subunit composition and
                      structural organization of ATP synthases and their
                      assemblies are significantly different. In addition, there
                      are hypotheses that the enzyme might be involved in the
                      formation of the mitochondrial permeability transition pore
                      and play a role in regulation of the cell death processes.
                      Dysfunctions of this enzyme lead to numerous severe
                      disorders with high fatality levels. In our review, we focus
                      on FOF1-structure-based approach towards development of new
                      therapies by using FOF1 structural features inherited by the
                      representatives of this enzyme family from different
                      taxonomy groups. We analyzed and systematized the most
                      relevant information about the structural organization of
                      FOF1 to discuss how this approach might help in the
                      development of new therapies targeting ATP synthases and
                      design tools for cellular bioenergetics control.},
      cin          = {IBI-7},
      ddc          = {610},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:35253091},
      UT           = {WOS:000765169100001},
      doi          = {10.1007/s00018-022-04153-0},
      url          = {https://juser.fz-juelich.de/record/907887},
}