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@Article{Plancherel,
  Title                    = {{Contribution à l'étude de la représentation d'une fonction arbitraire par les intégrales définies}},
  Author                   = {Plancherel, Michel and Mittag-Leffler},
  Journal                  = {{Rendiconti del Circolo Matematico di Palermo}},
  Year                     = {{1910}},
  Number                   = {{1}},
  Pages                    = {{289-335}},
  Volume                   = {{30}},
}
@Article{Bai2015,
  Title                    = {{How cryo-EM is revolutionizing structural biology}},
  Author                   = {Bai, Xiao-Chen and McMullan, Greg and Scheres, Sjors H. W.},
  Journal                  = {{Trends in Biochemical Sciences}},
  Year                     = {{2015}},

  Month                    = {{JAN}},
  Number                   = {{1}},
  Pages                    = {{49-57}},
  Volume                   = {{40}},

  Doi                      = {{10.1016/j.tibs.2014.10.005}},
  ISSN                     = {{0968-0004}},
  Unique-id                = {{ISI:000347862900007}}
}

@InCollection{NEwREV-ELad,
  Title                    = {{Cryogenic Electron Microscopy and Single-Particle Analysis}},
  Author                   = {Elmlund, Dominika and Elmlund, Hans},
  Booktitle                = {{Annual Review of Biochemistry, Vol. 84}},
  Year                     = {{2015}},
  Editor                   = {{Kornberg, RD}},
  Pages                    = {{499-517}},
  Series                   = {{Annual Review of Biochemistry}},
  Volume                   = {{84}},

  Doi                      = {{10.1146/annurev-biochem-060614-034226}},
  ISBN                     = {{978-0-8243-0884-1}},
  ISSN                     = {{0066-4154}},
  Orcid-numbers            = {{Elmlund, Hans/0000-0002-6992-0601}},
  Researcherid-numbers     = {{Elmlund, Hans/}},
  Unique-id                = {{ISI:000355765300019}}
}

@article{Penczek_2010,
Author = {Penczek, Pawel A.},
Title = {{Image Restoration in Cryo-Electron Microscopy}},
Journal = {{Methods in Enzymology}},
Year = {{2010}},
Volume = {{482}},
Pages = {{35-72}}
}

@Article{AllegrettiNAT2015,
  Title                    = {{Horizontal membrane-intrinsic alpha-helices in the stator a-subunit of an F-type ATP synthase}},
  Author                   = {Allegretti, Matteo and Klusch, Niklas and Mills, Deryck J. and Vonck, Janet and Kuehlbrandt, Werner and Davies, Karen M.},
  Journal                  = {{Nature}},
  Year                     = {{2015}},

  Month                    = {{MAY 14}},
  Number                   = {{7551}},
  Pages                    = {{237+}},
  Volume                   = {{521}},

  Abstract                 = {{ATP, the universal energy currency of cells, is produced by F-type ATP synthases, which are ancient, membrane-bound nanomachines. F-type ATP synthases use the energy of a transmembrane electrochemical gradient to generate ATP by rotary catalysis. Protons moving across the membrane drive a rotor ring composed of 8-15 c-subunits(1). A central stalk transmits the rotation of the c-ring to the catalytic F-1 head, where a series of conformational changes results in ATP synthesis(2). A key unresolved question in this fundamental process is how protons pass through the membrane to drive ATP production. Mitochondrial ATP synthases form V-shaped homodimers in cristae membranes(3). Here we report the structure of a native and active mitochondrial ATP synthase dimer, determined by single-particle electron cryomicroscopy at 6.2 angstrom resolution. Our structure shows four long, horizontal membrane-intrinsic alpha-helices in the a-subunit, arranged in two hairpins at an angle of approximately 70 degrees relative to the c-ring helices. It has been proposed that a strictly conserved membrane-embedded arginine in the a-subunit couples proton translocation to c-ring rotation(4). A fit of the conserved carboxy-terminal a-subunit sequence places the conserved arginine next to a proton-binding c-subunit glutamate. The map shows a slanting solvent-accessible channel that extends from the mitochondrial matrix to the conserved arginine. Another hydrophilic cavity on the lumenal membrane surface defines a direct route for the protons to an essential histidine-glutamate pair(5). Our results provide unique new insights into the structure and function of rotary ATP synthases and explain how ATP production is coupled to proton translocation.}},
  Address                  = {{MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND}},
  Affiliation              = {{Kuhlbrandt, W (Reprint Author), Max Planck Inst Biophys, Dept Struct Biol, Max von Laue Str 3, D-60438 Frankfurt, Germany. Allegretti, Matteo; Klusch, Niklas; Mills, Deryck J.; Vonck, Janet; Kuehlbrandt, Werner; Davies, Karen M., Max Planck Inst Biophys, Dept Struct Biol, D-60438 Frankfurt, Germany.}},
  Author-email             = {{werner.kuehlbrandt@biophys.mpg.de karen.davies@biophys.mpg.de}},
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  Doc-delivery-number      = {{CH9SY}},
  Doi                      = {{10.1038/nature14185}},
  Eissn                    = {{1476-4687}},
  Funding-acknowledgement  = {{Max Planck Society; Deutsche Forschungsgemeinschaft Cluster of Excellence Frankfurt `Macromolecular Complexes'}},
  Funding-text             = {{We thank T. Meier and J. D. Faraldo-Gomez for discussions and reading the manuscript. O. Yildiz and J. F. Castillo-Hernandez provided computer support. This work was funded by the Max Planck Society (M.A., N.K., D.J.M., J.V., K.M.D., W.K.) and the Deutsche Forschungsgemeinschaft Cluster of Excellence Frankfurt `Macromolecular Complexes' (K.M.D., W.K.).}},
  ISSN                     = {{0028-0836}},
  Journal-iso              = {{Nature}},
  Keywords-plus            = {{ESSENTIAL ARGININE RESIDUE; POLYTOMELLA SP; CROSS-LINKING; C-RING; CHLAMYDOMONAS-REINHARDTII; ELECTRON-MICROSCOPY; F0F1-ATP SYNTHASE; PROTON CHANNEL; CRYO-EM; RESOLUTION}},
  Language                 = {{English}},
  Number-of-cited-references = {{45}},
  Publisher                = {{NATURE PUBLISHING GROUP}},
  Research-areas           = {{Science \& Technology - Other Topics}},
  Times-cited              = {{1}},
  Type                     = {{Article}},
  Unique-id                = {{ISI:000354377800062}},
  Web-of-science-categories = {{Multidisciplinary Sciences}}
}

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