<?xml version="1.0" encoding="ISO-8859-1"?><article xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance">
<front>
<journal-meta>
<journal-id>1405-888X</journal-id>
<journal-title><![CDATA[TIP. Revista especializada en ciencias químico-biológicas]]></journal-title>
<abbrev-journal-title><![CDATA[TIP]]></abbrev-journal-title>
<issn>1405-888X</issn>
<publisher>
<publisher-name><![CDATA[Universidad Nacional Autónoma de México, Facultad de Estudios Superiores Zaragoza]]></publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id>S1405-888X2017000200029</article-id>
<article-id pub-id-type="doi">10.1016/j.recqb.2017.04.004</article-id>
<title-group>
<article-title xml:lang="es"><![CDATA[Topología y función de las subunidades intrínsecas de la membrana de las F 1 F O -ATP sintasa mitocondriales]]></article-title>
<article-title xml:lang="en"><![CDATA[Topology and function of the membrane-embedded proteins of the mitochondrial F 1 F O -ATP synthase]]></article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Sánchez-Vásquez]]></surname>
<given-names><![CDATA[Lorenzo]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[González-Halphen]]></surname>
<given-names><![CDATA[Diego]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
</contrib-group>
<aff id="Af1">
<institution><![CDATA[,Universidad Nacional Autónoma de México Instituto de Fisiología Celular ]]></institution>
<addr-line><![CDATA[Coyoacán Ciudad de México]]></addr-line>
<country>Mexico</country>
</aff>
<pub-date pub-type="pub">
<day>00</day>
<month>12</month>
<year>2017</year>
</pub-date>
<pub-date pub-type="epub">
<day>00</day>
<month>12</month>
<year>2017</year>
</pub-date>
<volume>20</volume>
<numero>2</numero>
<fpage>29</fpage>
<lpage>47</lpage>
<copyright-statement/>
<copyright-year/>
<self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_arttext&amp;pid=S1405-888X2017000200029&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_abstract&amp;pid=S1405-888X2017000200029&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_pdf&amp;pid=S1405-888X2017000200029&amp;lng=en&amp;nrm=iso"></self-uri><abstract abstract-type="short" xml:lang="es"><p><![CDATA[Resumen La F1FO-ATP sintasa es un complejo enzimático que se encuentra ampliamente distribuido en las membranas transductoras de energía. Todas las ATPasas, incluidas las mitocondriales, cloroplastídicas y bacterianas, comparten similitudes estructurales y funcionales. Sin embargo, hay diferencias en su composición que dependen de la especie, siendo más compleja en organismos como Saccharomyces cerevisiae o Bos taurus. Es por ello que una mejor comprensión de la estructura de la F1FO-ATP sintasa contribuirá a un mayor conocimiento a nivel molecular tanto de la función como de la regulación de este complejo enzimático. En la actualidad, se sabe muy poco acerca de la organización estructural de las subunidades de la región FO. Considerando lo anterior, en este trabajo se presenta información concerniente a las proteínas intrínsecas del dominio FO de las ATP sintasas más investigadas a la fecha, así como de algunas otras subunidades de membrana que se encuentran presentes en organismos menos estudiados.]]></p></abstract>
<abstract abstract-type="short" xml:lang="en"><p><![CDATA[Abstract The F1FO-ATP synthase is a complex widely distributed in energy-transducing membranes. All ATPases, including the mitochondrial, chloroplastic and bacterial, share structural and functional similarities. However, there are differences in their composition that depend on the species, being more complex in organisms such as Saccharomyces cerevisiae or Bos taurus. This is why, a better understanding of the F1FO-ATP synthase structure will contribute to a greater knowledge at a molecular level, both of the function, and the regulation of this enzymatic complex. At present, very little is known about the structural organization of the subunits from the FO domain. Considering the former, this paper presents information concerning the intrinsic membrane proteins from the most researched F1FO-ATP synthases to date, as well as some other membrane subunits present in less studied organisms.]]></p></abstract>
<kwd-group>
<kwd lng="es"><![CDATA[algas clorofíceas]]></kwd>
<kwd lng="es"><![CDATA[estructura]]></kwd>
<kwd lng="es"><![CDATA[F1FO-ATP sintasa mitocondrial]]></kwd>
<kwd lng="es"><![CDATA[proteínas membranales]]></kwd>
<kwd lng="es"><![CDATA[subunidades atípicas]]></kwd>
<kwd lng="en"><![CDATA[chlorophycean algae]]></kwd>
<kwd lng="en"><![CDATA[structure]]></kwd>
<kwd lng="en"><![CDATA[mitochondrial F1FO-ATP synthase]]></kwd>
<kwd lng="en"><![CDATA[membrane proteins]]></kwd>
<kwd lng="en"><![CDATA[atypical subunits]]></kwd>
</kwd-group>
</article-meta>
</front><back>
<ref-list>
<ref id="B1">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Abrahams]]></surname>
<given-names><![CDATA[J.P.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Leslie]]></surname>
<given-names><![CDATA[A.G.]]></given-names>
</name>
<name>
<surname><![CDATA[Lutter]]></surname>
<given-names><![CDATA[R.]]></given-names>
</name>
<name>
<surname><![CDATA[Walker]]></surname>
<given-names><![CDATA[J.E.]]></given-names>
</name>
</person-group>
<source><![CDATA[Nature]]></source>
<year>1994</year>
<volume>370</volume>
<numero>6491</numero>
<issue>6491</issue>
<page-range>621-8</page-range></nlm-citation>
</ref>
<ref id="B2">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Allegretti]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Horizontal membrane-intrinsic &#945;-helices in the stator a-subunit of an F-type ATP synthase]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Klusch]]></surname>
<given-names><![CDATA[N.]]></given-names>
</name>
<name>
<surname><![CDATA[Mills]]></surname>
<given-names><![CDATA[D.J.]]></given-names>
</name>
<name>
<surname><![CDATA[Vonck]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Kühlbrandt]]></surname>
<given-names><![CDATA[W.]]></given-names>
</name>
<name>
<surname><![CDATA[Davies]]></surname>
<given-names><![CDATA[K.M.]]></given-names>
</name>
</person-group>
<source><![CDATA[Nature]]></source>
<year>2015</year>
<volume>521</volume>
<numero>7551</numero>
<issue>7551</issue>
<page-range>237-40</page-range></nlm-citation>
</ref>
<ref id="B3">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Altendorf]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Structure and function of the F(O) complex of the ATP synthase from Escherichia coli]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Stalz]]></surname>
<given-names><![CDATA[W.]]></given-names>
</name>
<name>
<surname><![CDATA[Greie]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Deckers-Hebestreit]]></surname>
<given-names><![CDATA[G.]]></given-names>
</name>
</person-group>
<source><![CDATA[J. Exp. Biol.]]></source>
<year>2000</year>
<volume>203</volume>
<numero>Pt 1</numero>
<issue>Pt 1</issue>
<page-range>19-28</page-range></nlm-citation>
</ref>
<ref id="B4">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Amutha]]></surname>
<given-names><![CDATA[B.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[A novel role of Mgm1p, a dynamin-related GTPase, in ATP synthase assembly and cristae formation/maintenance]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Gordon]]></surname>
<given-names><![CDATA[D.M.]]></given-names>
</name>
<name>
<surname><![CDATA[Gu]]></surname>
<given-names><![CDATA[Y.]]></given-names>
</name>
<name>
<surname><![CDATA[Pain]]></surname>
<given-names><![CDATA[D.]]></given-names>
</name>
</person-group>
<source><![CDATA[Biochem. J.]]></source>
<year>2004</year>
<volume>381</volume>
<numero>Pt 1</numero>
<issue>Pt 1</issue>
<page-range>19-23</page-range></nlm-citation>
</ref>
<ref id="B5">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Aris]]></surname>
<given-names><![CDATA[J.P.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The FO subunits of the Escherichia coli F1FO-ATP synthase are sufficient to form a functional proton pore]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Klionsky]]></surname>
<given-names><![CDATA[D.J.]]></given-names>
</name>
<name>
<surname><![CDATA[Simoni]]></surname>
<given-names><![CDATA[R.D.]]></given-names>
</name>
</person-group>
<source><![CDATA[J. Biol. Chem.]]></source>
<year>1985</year>
<volume>260</volume>
<numero>20</numero>
<issue>20</issue>
<page-range>11207-15</page-range></nlm-citation>
</ref>
<ref id="B6">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Arnold]]></surname>
<given-names><![CDATA[I.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Yeast mitochondrial F1FO-ATP synthase exists as a dimer: identification of three dimer-specific subunits]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Pfeiffer]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
<name>
<surname><![CDATA[Neupert]]></surname>
<given-names><![CDATA[W.]]></given-names>
</name>
<name>
<surname><![CDATA[Stuart]]></surname>
<given-names><![CDATA[R.A.]]></given-names>
</name>
<name>
<surname><![CDATA[Schägger]]></surname>
<given-names><![CDATA[H.]]></given-names>
</name>
</person-group>
<source><![CDATA[EMBO J.]]></source>
<year>1998</year>
<volume>17</volume>
<numero>24</numero>
<issue>24</issue>
<page-range>7170-8</page-range></nlm-citation>
</ref>
<ref id="B7">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Arselin]]></surname>
<given-names><![CDATA[G.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The GxxxG motif of the transmembrane domain of subunit e is involved in the dimerization/oligomerization of the yeast ATP synthase complex in the mitochondrial membrane]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Giraud]]></surname>
<given-names><![CDATA[M.F.]]></given-names>
</name>
<name>
<surname><![CDATA[Dautant]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
<name>
<surname><![CDATA[Vaillier]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Brèthes]]></surname>
<given-names><![CDATA[D.]]></given-names>
</name>
<name>
<surname><![CDATA[Coulary-Salin]]></surname>
<given-names><![CDATA[B.]]></given-names>
</name>
<name>
<surname><![CDATA[Schaeffer]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Velours]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
</person-group>
<source><![CDATA[Eur. J. Biochem.]]></source>
<year>2003</year>
<volume>270</volume>
<numero>8</numero>
<issue>8</issue>
<page-range>1875-84</page-range></nlm-citation>
</ref>
<ref id="B8">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Arselin]]></surname>
<given-names><![CDATA[G.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[ATP synthase of yeast mitochondria. Isolation of the subunit h and disruption of the ATP14 gene]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Vaillier]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Graves]]></surname>
<given-names><![CDATA[P.V.]]></given-names>
</name>
<name>
<surname><![CDATA[Velours]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
</person-group>
<source><![CDATA[J. Biol. Chem.]]></source>
<year>1996</year>
<volume>271</volume>
<numero>34</numero>
<issue>34</issue>
<page-range>20284-90</page-range></nlm-citation>
</ref>
<ref id="B9">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Arselin]]></surname>
<given-names><![CDATA[G.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The modulation in subunits e and g amounts of yeast ATP synthase modifies mitochondrial cristae morphology]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Vaillier]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Salin]]></surname>
<given-names><![CDATA[B.]]></given-names>
</name>
<name>
<surname><![CDATA[Schaeffer]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Giraud]]></surname>
<given-names><![CDATA[M.F.]]></given-names>
</name>
<name>
<surname><![CDATA[Dautant]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
<name>
<surname><![CDATA[Brèthes]]></surname>
<given-names><![CDATA[D.]]></given-names>
</name>
<name>
<surname><![CDATA[Velours]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
</person-group>
<source><![CDATA[J. Biol. Chem.]]></source>
<year>2004</year>
<volume>279</volume>
<numero>39</numero>
<issue>39</issue>
<page-range>40392-9</page-range></nlm-citation>
</ref>
<ref id="B10">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Balabaskaran Nina]]></surname>
<given-names><![CDATA[P.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Highly divergent mitochondrial ATP synthase complexes in Tetrahymena thermophila]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Dudkina]]></surname>
<given-names><![CDATA[N.V.]]></given-names>
</name>
<name>
<surname><![CDATA[Kane]]></surname>
<given-names><![CDATA[L.A.]]></given-names>
</name>
<name>
<surname><![CDATA[van Eyk]]></surname>
<given-names><![CDATA[J.E.]]></given-names>
</name>
<name>
<surname><![CDATA[Boekema]]></surname>
<given-names><![CDATA[E.J.]]></given-names>
</name>
<name>
<surname><![CDATA[Mather]]></surname>
<given-names><![CDATA[M.W.]]></given-names>
</name>
<name>
<surname><![CDATA[Vaidya]]></surname>
<given-names><![CDATA[A.B.]]></given-names>
</name>
</person-group>
<source><![CDATA[PLoS Biol.]]></source>
<year>2010</year>
<volume>8</volume>
<numero>7</numero>
<issue>7</issue>
<page-range>e1000418</page-range></nlm-citation>
</ref>
<ref id="B11">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Brunner]]></surname>
<given-names><![CDATA[S.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Su e of the yeast F1FO-ATP synthase forms homodimers]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Everard-Gigot]]></surname>
<given-names><![CDATA[V.]]></given-names>
</name>
<name>
<surname><![CDATA[Stuart]]></surname>
<given-names><![CDATA[R.A.]]></given-names>
</name>
</person-group>
<source><![CDATA[J. Biol. Chem.]]></source>
<year>2002</year>
<volume>277</volume>
<numero>50</numero>
<issue>50</issue>
<page-range>48484-9</page-range></nlm-citation>
</ref>
<ref id="B12">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Bustos]]></surname>
<given-names><![CDATA[D.M.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The modification of the conserved GXXXG motif of the membrane-spanning segment of subunit g destabilizes the supramolecular species of yeast ATP synthase]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Velours]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
</person-group>
<source><![CDATA[J. Biol. Chem.]]></source>
<year>2005</year>
<volume>280</volume>
<numero>32</numero>
<issue>32</issue>
<page-range>29004-10</page-range></nlm-citation>
</ref>
<ref id="B13">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Cano-Estrada]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[F1FO-ATP sintasa y sus diferencias estructurales]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[González-Halphen]]></surname>
<given-names><![CDATA[D.]]></given-names>
</name>
</person-group>
<source><![CDATA[REB]]></source>
<year>2011</year>
<volume>30</volume>
<numero>3</numero>
<issue>3</issue>
<page-range>98-108</page-range></nlm-citation>
</ref>
<ref id="B14">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Cingolani]]></surname>
<given-names><![CDATA[G.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Structure of the ATP synthase catalytic complex (F1) from Escherichia coli in an auto inhibited conformation]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Duncan]]></surname>
<given-names><![CDATA[T.M.]]></given-names>
</name>
</person-group>
<source><![CDATA[Nat. Struct. Mol. Biol.]]></source>
<year>2011</year>
<volume>18</volume>
<numero>6</numero>
<issue>6</issue>
<page-range>701-7</page-range></nlm-citation>
</ref>
<ref id="B15">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Claggett]]></surname>
<given-names><![CDATA[S.B.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Functional incorporation of chimeric b subunits into F1Fo ATP synthase]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Grabar]]></surname>
<given-names><![CDATA[T.B.]]></given-names>
</name>
<name>
<surname><![CDATA[Dunn]]></surname>
<given-names><![CDATA[S.D.]]></given-names>
</name>
<name>
<surname><![CDATA[Cain]]></surname>
<given-names><![CDATA[B.D.]]></given-names>
</name>
</person-group>
<source><![CDATA[J. Bacteriol.]]></source>
<year>2007</year>
<volume>189</volume>
<numero>15</numero>
<issue>15</issue>
<page-range>5463-71</page-range></nlm-citation>
</ref>
<ref id="B16">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Collinson]]></surname>
<given-names><![CDATA[I.R.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[FO membrane domain of ATP synthase from bovine heart mitochondria: purification, subunit composition, and reconstitution with F1-ATPase]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Runswick]]></surname>
<given-names><![CDATA[M.J.]]></given-names>
</name>
<name>
<surname><![CDATA[Buchanan]]></surname>
<given-names><![CDATA[S.K.]]></given-names>
</name>
<name>
<surname><![CDATA[Fearnley]]></surname>
<given-names><![CDATA[I.M.]]></given-names>
</name>
<name>
<surname><![CDATA[Skehel]]></surname>
<given-names><![CDATA[J.M.]]></given-names>
</name>
<name>
<surname><![CDATA[van Raaij]]></surname>
<given-names><![CDATA[M.J.]]></given-names>
</name>
<name>
<surname><![CDATA[Griffiths]]></surname>
<given-names><![CDATA[D.E.]]></given-names>
</name>
<name>
<surname><![CDATA[Walker]]></surname>
<given-names><![CDATA[J.E.]]></given-names>
</name>
</person-group>
<source><![CDATA[Biochemistry]]></source>
<year>1994</year>
<volume>33</volume>
<numero>25</numero>
<issue>25</issue>
<page-range>7971-8</page-range></nlm-citation>
</ref>
<ref id="B17">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Couoh-Cardel]]></surname>
<given-names><![CDATA[S.J.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Structure of dimeric F1FO-ATP synthase]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Uribe-Carvajal]]></surname>
<given-names><![CDATA[S.]]></given-names>
</name>
<name>
<surname><![CDATA[Wilkens]]></surname>
<given-names><![CDATA[S.]]></given-names>
</name>
<name>
<surname><![CDATA[García-Trejo]]></surname>
<given-names><![CDATA[J.J.]]></given-names>
</name>
</person-group>
<source><![CDATA[J. Biol. Chem.]]></source>
<year>2010</year>
<volume>285</volume>
<numero>47</numero>
<issue>47</issue>
<page-range>36447-55</page-range></nlm-citation>
</ref>
<ref id="B18">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Deckers-Hebestreit]]></surname>
<given-names><![CDATA[G.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The FO complex of the proton-translocating F-type ATPase of Escherichia coli]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Altendorf]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
</person-group>
<source><![CDATA[J. Exp. Biol.]]></source>
<year>1992</year>
<volume>172</volume>
<page-range>451-9</page-range></nlm-citation>
</ref>
<ref id="B19">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Deckers-Hebestreit]]></surname>
<given-names><![CDATA[G.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The F0F1-type ATP synthases of bacteria: structure and function of the F0 complex]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Altendorf]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
</person-group>
<source><![CDATA[Annu. Rev. Microbiol.]]></source>
<year>1996</year>
<volume>50</volume>
<page-range>791-824</page-range></nlm-citation>
</ref>
<ref id="B20">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Devenish]]></surname>
<given-names><![CDATA[R.J.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Structure/function analysis of yeast mitochondrial ATP synthase subunit 8]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Papakonstantinou]]></surname>
<given-names><![CDATA[T.]]></given-names>
</name>
<name>
<surname><![CDATA[Galanis]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
<name>
<surname><![CDATA[Law]]></surname>
<given-names><![CDATA[R.H.]]></given-names>
</name>
<name>
<surname><![CDATA[Linnane]]></surname>
<given-names><![CDATA[A.W.]]></given-names>
</name>
<name>
<surname><![CDATA[Nagley]]></surname>
<given-names><![CDATA[P.]]></given-names>
</name>
</person-group>
<source><![CDATA[Ann. NY Acad. Sci.]]></source>
<year>1992</year>
<volume>671</volume>
<page-range>403-14</page-range></nlm-citation>
</ref>
<ref id="B21">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Dickson]]></surname>
<given-names><![CDATA[V.K.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[On the structure of the stator of the mitochondrial ATP synthase]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Silvester]]></surname>
<given-names><![CDATA[J.A.]]></given-names>
</name>
<name>
<surname><![CDATA[Fearnley]]></surname>
<given-names><![CDATA[I.M.]]></given-names>
</name>
<name>
<surname><![CDATA[Leslie]]></surname>
<given-names><![CDATA[A.G.]]></given-names>
</name>
<name>
<surname><![CDATA[Walker]]></surname>
<given-names><![CDATA[J.E.]]></given-names>
</name>
</person-group>
<source><![CDATA[EMBO J.]]></source>
<year>2006</year>
<volume>25</volume>
<page-range>2911-8</page-range></nlm-citation>
</ref>
<ref id="B22">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Dmitriev]]></surname>
<given-names><![CDATA[O.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Structure of the membrane domain of subunit b of the Escherichia coli FOF1 ATP synthase]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Jones]]></surname>
<given-names><![CDATA[P.C.]]></given-names>
</name>
<name>
<surname><![CDATA[Jiang]]></surname>
<given-names><![CDATA[W.]]></given-names>
</name>
<name>
<surname><![CDATA[Fillingame]]></surname>
<given-names><![CDATA[R.H.]]></given-names>
</name>
</person-group>
<source><![CDATA[J. Biol. Chem.]]></source>
<year>1999</year>
<volume>274</volume>
<numero>22</numero>
<issue>22</issue>
<page-range>15598-604</page-range></nlm-citation>
</ref>
<ref id="B23">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Domínguez-Ramírez]]></surname>
<given-names><![CDATA[L.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Virtudes y pecados de una enzima: La FOF1 ATP sintasa]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Tuena de Gómez-Poyou]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
</person-group>
<source><![CDATA[Mensaje Bioquímico]]></source>
<year>2003</year>
<volume>27</volume>
<page-range>25-44</page-range></nlm-citation>
</ref>
<ref id="B24">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Dudkina]]></surname>
<given-names><![CDATA[N.V.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Characterization of dimeric ATP synthase and cristae membrane ultrastructure from Saccharomyces and Polytomella mitochondria]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Sunderhaus]]></surname>
<given-names><![CDATA[S.]]></given-names>
</name>
<name>
<surname><![CDATA[Braun]]></surname>
<given-names><![CDATA[H.P.]]></given-names>
</name>
<name>
<surname><![CDATA[Boekema]]></surname>
<given-names><![CDATA[E.J.]]></given-names>
</name>
</person-group>
<source><![CDATA[FEBS Lett.]]></source>
<year>2006</year>
<volume>580</volume>
<numero>14</numero>
<issue>14</issue>
<page-range>3427-32</page-range></nlm-citation>
</ref>
<ref id="B25">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Everard-Gigot]]></surname>
<given-names><![CDATA[V.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Functional analysis of subunit e of the F1FO-ATP synthase of the yeast Saccharomyces cerevisiae: importance of the N-terminal membrane anchor region]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Dunn]]></surname>
<given-names><![CDATA[C.D.]]></given-names>
</name>
<name>
<surname><![CDATA[Dolan]]></surname>
<given-names><![CDATA[B.M.]]></given-names>
</name>
<name>
<surname><![CDATA[Brunner]]></surname>
<given-names><![CDATA[S.]]></given-names>
</name>
<name>
<surname><![CDATA[Jensen]]></surname>
<given-names><![CDATA[R.E.]]></given-names>
</name>
<name>
<surname><![CDATA[Stuart]]></surname>
<given-names><![CDATA[R.A.]]></given-names>
</name>
</person-group>
<source><![CDATA[Eukaryot. Cell.]]></source>
<year>2005</year>
<volume>4</volume>
<numero>2</numero>
<issue>2</issue>
<page-range>346-55</page-range></nlm-citation>
</ref>
<ref id="B26">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Fillingame]]></surname>
<given-names><![CDATA[R.H.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Structural model of the transmembrane FO rotary sector of H+-transporting ATP synthase derived by solution NMR and intersubunit cross-linking in situ]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Dmitriev]]></surname>
<given-names><![CDATA[O.]]></given-names>
</name>
</person-group>
<source><![CDATA[Biochim. Biophys. Acta]]></source>
<year>2002</year>
<volume>1565</volume>
<numero>2</numero>
<issue>2</issue>
<page-range>232-45</page-range></nlm-citation>
</ref>
<ref id="B27">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Foster]]></surname>
<given-names><![CDATA[D.L.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Stoichiometry of subunits in the H+-ATP synthase complex of Escherichia coli]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Fillingame]]></surname>
<given-names><![CDATA[R.H.]]></given-names>
</name>
</person-group>
<source><![CDATA[J. Biol. Chem.]]></source>
<year>1982</year>
<volume>257</volume>
<page-range>2009-15</page-range></nlm-citation>
</ref>
<ref id="B28">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Fronzes]]></surname>
<given-names><![CDATA[R.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The peripheral stalk participates in the yeast ATP synthase dimerization independently of e and g subunits]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Weimann]]></surname>
<given-names><![CDATA[T.]]></given-names>
</name>
<name>
<surname><![CDATA[Vaillier]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Velours]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Brèthes]]></surname>
<given-names><![CDATA[D.]]></given-names>
</name>
</person-group>
<source><![CDATA[Biochemistry]]></source>
<year>2006</year>
<volume>45</volume>
<numero>21</numero>
<issue>21</issue>
<page-range>6715-23</page-range></nlm-citation>
</ref>
<ref id="B29">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[García-Trejo]]></surname>
<given-names><![CDATA[J.J.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Estructura y mecanismo de la nueva subunidad inhibitoria &#950; del nanomotor F1FO ATP sintasa de las &#945;-proteobacterias en Paracoccus denitrificans]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Zarco Zavala]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
<name>
<surname><![CDATA[Morales Ríos]]></surname>
<given-names><![CDATA[E.]]></given-names>
</name>
</person-group>
<source><![CDATA[Mensaje Bioquímico]]></source>
<year>2012</year>
<volume>36</volume>
<page-range>106-26</page-range></nlm-citation>
</ref>
<ref id="B30">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Girvin]]></surname>
<given-names><![CDATA[M.E.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Rastogi]]></surname>
<given-names><![CDATA[V.K.]]></given-names>
</name>
<name>
<surname><![CDATA[Abildgaard]]></surname>
<given-names><![CDATA[F.]]></given-names>
</name>
<name>
<surname><![CDATA[Markley]]></surname>
<given-names><![CDATA[J.L.]]></given-names>
</name>
<name>
<surname><![CDATA[Fillingame]]></surname>
<given-names><![CDATA[R.H.]]></given-names>
</name>
</person-group>
<source><![CDATA[Biochemistry]]></source>
<year>1998</year>
<volume>37</volume>
<numero>25</numero>
<issue>25</issue>
<page-range>8817-24</page-range></nlm-citation>
</ref>
<ref id="B31">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Godinot]]></surname>
<given-names><![CDATA[C.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Structure and function of the ATPase-ATP synthase complex of mitochondria as compared to chloroplasts and bacteria]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Di Pietro]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
</person-group>
<source><![CDATA[Biochimie]]></source>
<year>1986</year>
<volume>68</volume>
<numero>3</numero>
<issue>3</issue>
<page-range>367-74</page-range></nlm-citation>
</ref>
<ref id="B32">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Grasso]]></surname>
<given-names><![CDATA[D.G.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The C-terminal positively charged region of subunit 8 of yeast mitochondrial ATP synthase is required for efficient assembly of this subunit into the membrane FO sector]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Nero]]></surname>
<given-names><![CDATA[D.]]></given-names>
</name>
<name>
<surname><![CDATA[Law]]></surname>
<given-names><![CDATA[R.H.]]></given-names>
</name>
<name>
<surname><![CDATA[Devenish]]></surname>
<given-names><![CDATA[R.J.]]></given-names>
</name>
<name>
<surname><![CDATA[Nagley]]></surname>
<given-names><![CDATA[P.]]></given-names>
</name>
</person-group>
<source><![CDATA[Eur. J. Biochem.]]></source>
<year>1991</year>
<volume>199</volume>
<numero>1</numero>
<issue>1</issue>
<page-range>203-9</page-range></nlm-citation>
</ref>
<ref id="B33">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Habersetzer]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[ATP synthase oligomerization: from the enzyme models to the mitochondrial morphology]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Ziani]]></surname>
<given-names><![CDATA[W.]]></given-names>
</name>
<name>
<surname><![CDATA[Larrieu]]></surname>
<given-names><![CDATA[I.]]></given-names>
</name>
<name>
<surname><![CDATA[Stines-Chaumeil]]></surname>
<given-names><![CDATA[C.]]></given-names>
</name>
<name>
<surname><![CDATA[Giraud]]></surname>
<given-names><![CDATA[M.F.]]></given-names>
</name>
<name>
<surname><![CDATA[Brèthes]]></surname>
<given-names><![CDATA[D.]]></given-names>
</name>
<name>
<surname><![CDATA[Dautant]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
<name>
<surname><![CDATA[Paumard]]></surname>
<given-names><![CDATA[P.]]></given-names>
</name>
</person-group>
<source><![CDATA[Int. J. Biochem. Cell. Biol.]]></source>
<year>2013</year>
<volume>45</volume>
<numero>1</numero>
<issue>1</issue>
<page-range>99-105</page-range></nlm-citation>
</ref>
<ref id="B34">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Hahn]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of Inner Mitochondrial Membrane Morphology]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Parey]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
<name>
<surname><![CDATA[Bublitz]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
<name>
<surname><![CDATA[Mills]]></surname>
<given-names><![CDATA[D.J.]]></given-names>
</name>
<name>
<surname><![CDATA[Zickermann]]></surname>
<given-names><![CDATA[V.]]></given-names>
</name>
<name>
<surname><![CDATA[Vonck]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Kühlbrandt]]></surname>
<given-names><![CDATA[W.]]></given-names>
</name>
<name>
<surname><![CDATA[Meier]]></surname>
<given-names><![CDATA[T.]]></given-names>
</name>
</person-group>
<source><![CDATA[Mol. Cell]]></source>
<year>2016</year>
<volume>63</volume>
<numero>3</numero>
<issue>3</issue>
<page-range>445-56</page-range></nlm-citation>
</ref>
<ref id="B35">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Heazlewood]]></surname>
<given-names><![CDATA[J.L.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The products of the mitochondrial orf25 and orfB genes are FO components in the plant F1FO ATP synthase]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Whelan]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Millar]]></surname>
<given-names><![CDATA[A.H.]]></given-names>
</name>
</person-group>
<source><![CDATA[FEBS Lett.]]></source>
<year>2003</year>
<volume>540</volume>
<numero>1-3</numero>
<issue>1-3</issue>
<page-range>201-5</page-range></nlm-citation>
</ref>
<ref id="B36">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Itoh]]></surname>
<given-names><![CDATA[H.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Mechanically driven ATP synthase by F1-ATPase]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Takahashi]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
<name>
<surname><![CDATA[Adachi]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
<name>
<surname><![CDATA[Noji]]></surname>
<given-names><![CDATA[H.]]></given-names>
</name>
<name>
<surname><![CDATA[Yasuda]]></surname>
<given-names><![CDATA[R.]]></given-names>
</name>
<name>
<surname><![CDATA[Yoshida]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
<name>
<surname><![CDATA[Kinosita]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
</person-group>
<source><![CDATA[Nature]]></source>
<year>2004</year>
<volume>427</volume>
<page-range>465-8</page-range></nlm-citation>
</ref>
<ref id="B37">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Jiko]]></surname>
<given-names><![CDATA[C.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Bovine F1FO ATP synthase monomers bend the lipid bilayer in 2D membrane crystals]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Davies]]></surname>
<given-names><![CDATA[K.M.]]></given-names>
</name>
<name>
<surname><![CDATA[Shinzawa-Itoh]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
<name>
<surname><![CDATA[Tani]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
<name>
<surname><![CDATA[Maeda]]></surname>
<given-names><![CDATA[S.]]></given-names>
</name>
<name>
<surname><![CDATA[Mills]]></surname>
<given-names><![CDATA[D.J.]]></given-names>
</name>
<name>
<surname><![CDATA[Tsukihara]]></surname>
<given-names><![CDATA[T.]]></given-names>
</name>
<name>
<surname><![CDATA[Fujiyoshi]]></surname>
<given-names><![CDATA[Y.]]></given-names>
</name>
<name>
<surname><![CDATA[Kühlbrandt]]></surname>
<given-names><![CDATA[W.]]></given-names>
</name>
<name>
<surname><![CDATA[Gerle]]></surname>
<given-names><![CDATA[C.]]></given-names>
</name>
</person-group>
<source><![CDATA[Elife]]></source>
<year>2015</year>
<volume>27</volume>
<numero>4</numero>
<issue>4</issue>
<page-range>e06119</page-range></nlm-citation>
</ref>
<ref id="B38">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Jonckheere]]></surname>
<given-names><![CDATA[A.I.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Mitochondrial ATP synthase: architecture, function and pathology]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Smeitink]]></surname>
<given-names><![CDATA[J.A.]]></given-names>
</name>
<name>
<surname><![CDATA[Rodenburg]]></surname>
<given-names><![CDATA[R.J.]]></given-names>
</name>
</person-group>
<source><![CDATA[J. Inherit. Metab. Dis.]]></source>
<year>2012</year>
<volume>35</volume>
<numero>2</numero>
<issue>2</issue>
<page-range>211-25</page-range></nlm-citation>
</ref>
<ref id="B39">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Kühlbrandt]]></surname>
<given-names><![CDATA[W.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Rotary ATPases: A New Twist to an Ancient Machine]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Davies]]></surname>
<given-names><![CDATA[K.M.]]></given-names>
</name>
</person-group>
<source><![CDATA[Trends Biochem. Sci.]]></source>
<year>2016</year>
<volume>41</volume>
<numero>1</numero>
<issue>1</issue>
<page-range>106-16</page-range></nlm-citation>
</ref>
<ref id="B40">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Lee]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Organization of Subunits in the Membrane Domain of the Bovine F-ATPase Revealed by Covalent Cross-linking]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Ding]]></surname>
<given-names><![CDATA[S.]]></given-names>
</name>
<name>
<surname><![CDATA[Walpole]]></surname>
<given-names><![CDATA[T.B.]]></given-names>
</name>
<name>
<surname><![CDATA[Holding]]></surname>
<given-names><![CDATA[A.N.]]></given-names>
</name>
<name>
<surname><![CDATA[Montgomery]]></surname>
<given-names><![CDATA[M.G.]]></given-names>
</name>
<name>
<surname><![CDATA[Fearnley]]></surname>
<given-names><![CDATA[I.M.]]></given-names>
</name>
<name>
<surname><![CDATA[Walker]]></surname>
<given-names><![CDATA[J.E.]]></given-names>
</name>
</person-group>
<source><![CDATA[J. Biol. Chem.]]></source>
<year>2015</year>
<volume>290</volume>
<numero>21</numero>
<issue>21</issue>
<page-range>13308-20</page-range></nlm-citation>
</ref>
<ref id="B41">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Leyva]]></surname>
<given-names><![CDATA[J.A.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Understanding ATP synthesis: structure and mechanism of the F1-ATPase]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Bianchet]]></surname>
<given-names><![CDATA[M.A.]]></given-names>
</name>
<name>
<surname><![CDATA[Mario Amzel]]></surname>
<given-names><![CDATA[L.]]></given-names>
</name>
</person-group>
<source><![CDATA[Mol. Memb. Biol.]]></source>
<year>2003</year>
<volume>20</volume>
<numero>1</numero>
<issue>1</issue>
<page-range>27-33</page-range></nlm-citation>
</ref>
<ref id="B42">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Liu]]></surname>
<given-names><![CDATA[S.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The purification and characterization of ATP synthase complexes from the mitochondria of four fungal species]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Charlesworth]]></surname>
<given-names><![CDATA[T.J.]]></given-names>
</name>
<name>
<surname><![CDATA[Bason]]></surname>
<given-names><![CDATA[J.V.]]></given-names>
</name>
<name>
<surname><![CDATA[Montgomery]]></surname>
<given-names><![CDATA[M.G.]]></given-names>
</name>
<name>
<surname><![CDATA[Harbour]]></surname>
<given-names><![CDATA[M.E.]]></given-names>
</name>
<name>
<surname><![CDATA[Fearnley]]></surname>
<given-names><![CDATA[I.M.]]></given-names>
</name>
<name>
<surname><![CDATA[Walker]]></surname>
<given-names><![CDATA[J.E.]]></given-names>
</name>
</person-group>
<source><![CDATA[Biochem. J.]]></source>
<year>2015</year>
<volume>468</volume>
<numero>1</numero>
<issue>1</issue>
<page-range>167-75</page-range></nlm-citation>
</ref>
<ref id="B43">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Martin]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[FO-driven Rotation in the ATP Synthase Direction against the Force of F1 ATPase in the FOF1 ATP Synthase]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Hudson]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Hornung]]></surname>
<given-names><![CDATA[T.]]></given-names>
</name>
<name>
<surname><![CDATA[Frasch]]></surname>
<given-names><![CDATA[W.D.]]></given-names>
</name>
</person-group>
<source><![CDATA[J. Biol. Chem.]]></source>
<year>2015</year>
<volume>290</volume>
<numero>17</numero>
<issue>17</issue>
<page-range>10717-28</page-range></nlm-citation>
</ref>
<ref id="B44">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Martin]]></surname>
<given-names><![CDATA[J.L.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Anatomy of F1-ATPase powered rotation]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Ishmukhametov]]></surname>
<given-names><![CDATA[R.]]></given-names>
</name>
<name>
<surname><![CDATA[Hornung]]></surname>
<given-names><![CDATA[T.]]></given-names>
</name>
<name>
<surname><![CDATA[Ahmad]]></surname>
<given-names><![CDATA[Z.]]></given-names>
</name>
<name>
<surname><![CDATA[Frasch]]></surname>
<given-names><![CDATA[W.D.]]></given-names>
</name>
</person-group>
<source><![CDATA[Proc. Natl. Acad. Sci. U S A.]]></source>
<year>2014</year>
<volume>111</volume>
<numero>10</numero>
<issue>10</issue>
<page-range>3715-20</page-range></nlm-citation>
</ref>
<ref id="B45">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Meyer]]></surname>
<given-names><![CDATA[B.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Identification of two proteins associated with mammalian ATP synthase]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Wittig]]></surname>
<given-names><![CDATA[I.]]></given-names>
</name>
<name>
<surname><![CDATA[Trifilieff]]></surname>
<given-names><![CDATA[E.]]></given-names>
</name>
<name>
<surname><![CDATA[Karas]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
<name>
<surname><![CDATA[Schägger]]></surname>
<given-names><![CDATA[H.]]></given-names>
</name>
</person-group>
<source><![CDATA[Mol. Cell . Proteomics]]></source>
<year>2007</year>
<volume>6</volume>
<numero>10</numero>
<issue>10</issue>
<page-range>1690-9</page-range></nlm-citation>
</ref>
<ref id="B46">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Morales-Ríos]]></surname>
<given-names><![CDATA[E.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Structure of ATP synthase from Paracoccus denitrificans determined by X-ray crystallography at 4.0 Å resolution]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Montgomery]]></surname>
<given-names><![CDATA[M.G.]]></given-names>
</name>
<name>
<surname><![CDATA[Leslie]]></surname>
<given-names><![CDATA[A.G.]]></given-names>
</name>
<name>
<surname><![CDATA[Walker]]></surname>
<given-names><![CDATA[J.E.]]></given-names>
</name>
</person-group>
<source><![CDATA[Proc. Natl. Acad. Sci. U S A.]]></source>
<year>2015</year>
<volume>112</volume>
<numero>43</numero>
<issue>43</issue>
<page-range>13231-6</page-range></nlm-citation>
</ref>
<ref id="B47">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Nesci]]></surname>
<given-names><![CDATA[S.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Opposite rotation directions in the synthesis and hydrolysis of ATP by the ATP synthase: hints from a subunit asymmetry]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Trombetti]]></surname>
<given-names><![CDATA[F.]]></given-names>
</name>
<name>
<surname><![CDATA[Ventrella]]></surname>
<given-names><![CDATA[V.]]></given-names>
</name>
<name>
<surname><![CDATA[Pagliarani]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
</person-group>
<source><![CDATA[J. Membr. Biol.]]></source>
<year>2015</year>
<volume>248</volume>
<numero>2</numero>
<issue>2</issue>
<page-range>163-9</page-range></nlm-citation>
</ref>
<ref id="B48">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Nesci]]></surname>
<given-names><![CDATA[S.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The c-Ring of the F1FO-ATP Synthase: Facts and Perspectives]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Trombetti]]></surname>
<given-names><![CDATA[F.]]></given-names>
</name>
<name>
<surname><![CDATA[Ventrella]]></surname>
<given-names><![CDATA[V.]]></given-names>
</name>
<name>
<surname><![CDATA[Pagliarani]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
</person-group>
<source><![CDATA[J. Membr. Biol.]]></source>
<year>2016</year>
<volume>249</volume>
<numero>1-2</numero>
<issue>1-2</issue>
<page-range>11-21</page-range></nlm-citation>
</ref>
<ref id="B49">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Paul]]></surname>
<given-names><![CDATA[M.F.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The role of subunit 4, a nuclear-encoded protein of the FO sector of yeast mitochondrial ATP synthase, in the assembly of the whole complex]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Velours]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Arselin de Chateaubodeau]]></surname>
<given-names><![CDATA[G.]]></given-names>
</name>
<name>
<surname><![CDATA[Aigle]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
<name>
<surname><![CDATA[Guerin]]></surname>
<given-names><![CDATA[B.]]></given-names>
</name>
</person-group>
<source><![CDATA[Eur. J. Biochem.]]></source>
<year>1989</year>
<volume>85</volume>
<numero>1</numero>
<issue>1</issue>
<page-range>163-71</page-range></nlm-citation>
</ref>
<ref id="B50">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Paumard]]></surname>
<given-names><![CDATA[P.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Two ATP synthases can be linked through subunits i in the inner mitochondrial membrane of Saccharomyces cerevisiae]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Arselin]]></surname>
<given-names><![CDATA[G.]]></given-names>
</name>
<name>
<surname><![CDATA[Vaillier]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Chaignepain]]></surname>
<given-names><![CDATA[S.]]></given-names>
</name>
<name>
<surname><![CDATA[Bathany]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
<name>
<surname><![CDATA[Schmitter]]></surname>
<given-names><![CDATA[J.M.]]></given-names>
</name>
<name>
<surname><![CDATA[Brèthes]]></surname>
<given-names><![CDATA[D.]]></given-names>
</name>
<name>
<surname><![CDATA[Velours]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
</person-group>
<source><![CDATA[Biochemistry]]></source>
<year>2002</year>
<volume>1</volume>
<numero>33</numero>
<issue>33</issue>
<page-range>10390-6</page-range></nlm-citation>
</ref>
<ref id="B51">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Paumard]]></surname>
<given-names><![CDATA[P.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The ATP synthase is involved in generating mitochondrial cristae morphology]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Vaillier]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Coulary]]></surname>
<given-names><![CDATA[B.]]></given-names>
</name>
<name>
<surname><![CDATA[Schaeffer]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Soubannier]]></surname>
<given-names><![CDATA[V.]]></given-names>
</name>
<name>
<surname><![CDATA[Mueller]]></surname>
<given-names><![CDATA[D.M.]]></given-names>
</name>
<name>
<surname><![CDATA[Brèthes]]></surname>
<given-names><![CDATA[D.]]></given-names>
</name>
<name>
<surname><![CDATA[di Rago]]></surname>
<given-names><![CDATA[J.P.]]></given-names>
</name>
<name>
<surname><![CDATA[Velours]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
</person-group>
<source><![CDATA[EMBO J.]]></source>
<year>2002</year>
<volume>21</volume>
<numero>3</numero>
<issue>3</issue>
<page-range>221-30</page-range></nlm-citation>
</ref>
<ref id="B52">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Paumard]]></surname>
<given-names><![CDATA[P.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Environmental study of subunit i, a F(O) component of the yeast ATP synthase]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Vaillier]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Napias]]></surname>
<given-names><![CDATA[C.]]></given-names>
</name>
<name>
<surname><![CDATA[Arselin]]></surname>
<given-names><![CDATA[G.]]></given-names>
</name>
<name>
<surname><![CDATA[Brèthes]]></surname>
<given-names><![CDATA[D.]]></given-names>
</name>
<name>
<surname><![CDATA[Graves]]></surname>
<given-names><![CDATA[P.V.]]></given-names>
</name>
<name>
<surname><![CDATA[Velours]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
</person-group>
<source><![CDATA[Biochemistry]]></source>
<year>2000</year>
<volume>39</volume>
<numero>14</numero>
<issue>14</issue>
<page-range>4199-205</page-range></nlm-citation>
</ref>
<ref id="B53">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Rees]]></surname>
<given-names><![CDATA[D.M.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The structure of the membrane extrinsic region of bovine ATP synthase]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Leslie]]></surname>
<given-names><![CDATA[A.G.]]></given-names>
</name>
<name>
<surname><![CDATA[Walker]]></surname>
<given-names><![CDATA[J.E.]]></given-names>
</name>
</person-group>
<source><![CDATA[Proc. Natl. Acad. Sci. U S A.]]></source>
<year>2009</year>
<volume>106</volume>
<page-range>21597-601</page-range></nlm-citation>
</ref>
<ref id="B54">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Roudeau]]></surname>
<given-names><![CDATA[S.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Subunit f of the yeast mitochondrial ATP synthase: topological and functional studies]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Spannagel]]></surname>
<given-names><![CDATA[C.]]></given-names>
</name>
<name>
<surname><![CDATA[Vaillier]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Arselin]]></surname>
<given-names><![CDATA[G.]]></given-names>
</name>
<name>
<surname><![CDATA[Graves]]></surname>
<given-names><![CDATA[P.V.]]></given-names>
</name>
<name>
<surname><![CDATA[Velours]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
</person-group>
<source><![CDATA[J. Bioenerg. Biomembr.]]></source>
<year>1999</year>
<volume>31</volume>
<numero>2</numero>
<issue>2</issue>
<page-range>85-94</page-range></nlm-citation>
</ref>
<ref id="B55">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Roy]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Improved crystallization of Escherichia coli ATP synthase catalytic complex (F1) by introducing a phosphomimetic mutation in subunit &#949;]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Hutcheon]]></surname>
<given-names><![CDATA[M.L.]]></given-names>
</name>
<name>
<surname><![CDATA[Duncan]]></surname>
<given-names><![CDATA[T.M.]]></given-names>
</name>
<name>
<surname><![CDATA[Cingolani]]></surname>
<given-names><![CDATA[G.]]></given-names>
</name>
</person-group>
<source><![CDATA[Acta Crystallogr. Sect. F. Struct. Biol. Cryst. Commun.]]></source>
<year>2012</year>
<volume>68</volume>
<numero>Pt 10</numero>
<issue>Pt 10</issue>
<page-range>1229-33</page-range></nlm-citation>
</ref>
<ref id="B56">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Saddar]]></surname>
<given-names><![CDATA[S.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The yeast F(1)F(0)-ATP synthase: analysis of the molecular organization of subunit g and the importance of a conserved GXXXG motif]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Stuart]]></surname>
<given-names><![CDATA[R.A.]]></given-names>
</name>
</person-group>
<source><![CDATA[J. Biol. Chem.]]></source>
<year>2005</year>
<volume>280</volume>
<numero>26</numero>
<issue>26</issue>
<page-range>24435-42</page-range></nlm-citation>
</ref>
<ref id="B57">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Shirakihara]]></surname>
<given-names><![CDATA[Y.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Structure of a thermophilic F1-ATPase inhibited by an &#949;-subunit: deeper insight into the &#949;-inhibition mechanism]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Shiratori]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
<name>
<surname><![CDATA[Tanikawa]]></surname>
<given-names><![CDATA[H.]]></given-names>
</name>
<name>
<surname><![CDATA[Nakasako]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
<name>
<surname><![CDATA[Yoshida]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
<name>
<surname><![CDATA[Suzuki]]></surname>
<given-names><![CDATA[T.]]></given-names>
</name>
</person-group>
<source><![CDATA[FEBS J]]></source>
<year>2015</year>
<volume>282</volume>
<numero>15</numero>
<issue>15</issue>
<page-range>2895-913</page-range></nlm-citation>
</ref>
<ref id="B58">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Soubannier]]></surname>
<given-names><![CDATA[V.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The second stalk of the yeast ATP synthase complex: identification of subunits showing cross-links with known positions of subunit 4 (subunit b)]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Rusconi]]></surname>
<given-names><![CDATA[F.]]></given-names>
</name>
<name>
<surname><![CDATA[Vaillier]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Arselin]]></surname>
<given-names><![CDATA[G.]]></given-names>
</name>
<name>
<surname><![CDATA[Chaignepain]]></surname>
<given-names><![CDATA[S.]]></given-names>
</name>
<name>
<surname><![CDATA[Graves]]></surname>
<given-names><![CDATA[P.V.]]></given-names>
</name>
<name>
<surname><![CDATA[Schmitter]]></surname>
<given-names><![CDATA[J.M.]]></given-names>
</name>
<name>
<surname><![CDATA[Zhang]]></surname>
<given-names><![CDATA[J.L.]]></given-names>
</name>
<name>
<surname><![CDATA[Mueller]]></surname>
<given-names><![CDATA[D.]]></given-names>
</name>
<name>
<surname><![CDATA[Velours]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
</person-group>
<source><![CDATA[Biochemistry]]></source>
<year>1999</year>
<volume>38</volume>
<numero>45</numero>
<issue>45</issue>
<page-range>15017-24</page-range></nlm-citation>
</ref>
<ref id="B59">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Soubannier]]></surname>
<given-names><![CDATA[V.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[In the absence of the first membrane-spanning segment of subunit 4(b), the yeast ATP synthase is functional but does not dimerize or oligomerize]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Vaillier]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Paumard]]></surname>
<given-names><![CDATA[P.]]></given-names>
</name>
<name>
<surname><![CDATA[Coulary]]></surname>
<given-names><![CDATA[B.]]></given-names>
</name>
<name>
<surname><![CDATA[Schaeffer]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Velours]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
</person-group>
<source><![CDATA[J. Biol. Chem.]]></source>
<year>2002</year>
<volume>277</volume>
<numero>12</numero>
<issue>12</issue>
<page-range>10739-45</page-range></nlm-citation>
</ref>
<ref id="B60">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Spannagel]]></surname>
<given-names><![CDATA[C.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The subunit f of mitochondrial yeast ATP-synthase: characterization of the protein and disruption of the structural gene ATP17]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Vaillier]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Arselin]]></surname>
<given-names><![CDATA[G.]]></given-names>
</name>
<name>
<surname><![CDATA[Graves]]></surname>
<given-names><![CDATA[P.V.]]></given-names>
</name>
<name>
<surname><![CDATA[Velours]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
</person-group>
<source><![CDATA[Eur. J. Biochem.]]></source>
<year>1997</year>
<volume>247</volume>
<numero>3</numero>
<issue>3</issue>
<page-range>1111-7</page-range></nlm-citation>
</ref>
<ref id="B61">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Stewart]]></surname>
<given-names><![CDATA[A.G.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Rotatory ATPases: Models, machine elements and technical specifications]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Sobti]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
<name>
<surname><![CDATA[Harvey]]></surname>
<given-names><![CDATA[R.P.]]></given-names>
</name>
<name>
<surname><![CDATA[Stock]]></surname>
<given-names><![CDATA[D.]]></given-names>
</name>
</person-group>
<source><![CDATA[BioArchitecture]]></source>
<year>2013</year>
<volume>3</volume>
<numero>1</numero>
<issue>1</issue>
<page-range>2-12</page-range></nlm-citation>
</ref>
<ref id="B62">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Stock]]></surname>
<given-names><![CDATA[D.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Molecular architecture of the rotary motor in ATP synthase]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Leslie]]></surname>
<given-names><![CDATA[A.G.]]></given-names>
</name>
<name>
<surname><![CDATA[Walker]]></surname>
<given-names><![CDATA[J.E.]]></given-names>
</name>
</person-group>
<source><![CDATA[Science]]></source>
<year>1999</year>
<volume>286</volume>
<page-range>1700-5</page-range></nlm-citation>
</ref>
<ref id="B63">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Stocker]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The structural basis for unidirectional rotation of thermo alkaliphilic F1-ATPase]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Keis]]></surname>
<given-names><![CDATA[S.]]></given-names>
</name>
<name>
<surname><![CDATA[Vonck]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Cook]]></surname>
<given-names><![CDATA[G.M.]]></given-names>
</name>
<name>
<surname><![CDATA[Dimroth]]></surname>
<given-names><![CDATA[P.]]></given-names>
</name>
</person-group>
<source><![CDATA[Structure]]></source>
<year>2007</year>
<volume>15</volume>
<numero>8</numero>
<issue>8</issue>
<page-range>904-14</page-range></nlm-citation>
</ref>
<ref id="B64">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Vázquez-Acevedo]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The mitochondrial ATP synthase of chlorophycean algae contains eight subunits of unknown origin involved in the formation of an atypical stator-stalk and in the dimerization of the complex]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Cardol]]></surname>
<given-names><![CDATA[P.]]></given-names>
</name>
<name>
<surname><![CDATA[Cano-Estrada]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
<name>
<surname><![CDATA[Lapaille]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
<name>
<surname><![CDATA[Remacle]]></surname>
<given-names><![CDATA[C.]]></given-names>
</name>
<name>
<surname><![CDATA[González-Halphen]]></surname>
<given-names><![CDATA[D.]]></given-names>
</name>
</person-group>
<source><![CDATA[J. Bioenerg. Biomembr.]]></source>
<year>2006</year>
<volume>38</volume>
<numero>5-6</numero>
<issue>5-6</issue>
<page-range>271-82</page-range></nlm-citation>
</ref>
<ref id="B65">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Vázquez-Acevedo]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Dissecting the peripheral stalk of the mitochondrial ATP synthase of chlorophycean algae]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Vega-de Luna]]></surname>
<given-names><![CDATA[F.]]></given-names>
</name>
<name>
<surname><![CDATA[Sánchez-Vásquez]]></surname>
<given-names><![CDATA[L.]]></given-names>
</name>
<name>
<surname><![CDATA[Colina-Tenorio]]></surname>
<given-names><![CDATA[L.]]></given-names>
</name>
<name>
<surname><![CDATA[Remacle]]></surname>
<given-names><![CDATA[C.]]></given-names>
</name>
<name>
<surname><![CDATA[Cardol]]></surname>
<given-names><![CDATA[P.]]></given-names>
</name>
<name>
<surname><![CDATA[Miranda-Astudillo]]></surname>
<given-names><![CDATA[H.]]></given-names>
</name>
<name>
<surname><![CDATA[González-Halphen]]></surname>
<given-names><![CDATA[D.]]></given-names>
</name>
</person-group>
<source><![CDATA[Biochim. Biophys. Acta]]></source>
<year>2016</year>
<volume>S0005-2728</volume>
<numero>16</numero>
<issue>16</issue>
<page-range>30022-6</page-range></nlm-citation>
</ref>
<ref id="B66">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Velours]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Organisation of the yeast ATP synthase F(0): a study based on cysteine mutants, thiol modification and cross-linking reagents]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Paumard]]></surname>
<given-names><![CDATA[P.]]></given-names>
</name>
<name>
<surname><![CDATA[Soubannier]]></surname>
<given-names><![CDATA[V.]]></given-names>
</name>
<name>
<surname><![CDATA[Spannagel]]></surname>
<given-names><![CDATA[C.]]></given-names>
</name>
<name>
<surname><![CDATA[Vaillier]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Arselin]]></surname>
<given-names><![CDATA[G.]]></given-names>
</name>
<name>
<surname><![CDATA[Graves]]></surname>
<given-names><![CDATA[P.V.]]></given-names>
</name>
</person-group>
<source><![CDATA[Biochim. Biophys. Acta]]></source>
<year>2000</year>
<volume>1458</volume>
<numero>2-3</numero>
<issue>2-3</issue>
<page-range>443-56</page-range></nlm-citation>
</ref>
<ref id="B67">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Vik]]></surname>
<given-names><![CDATA[S.B.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Structure and function of subunit a of the ATP synthase of Escherichia coli]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Ishmukhametov]]></surname>
<given-names><![CDATA[R.R.]]></given-names>
</name>
</person-group>
<source><![CDATA[J. Bioenerg. Biomembr.]]></source>
<year>2005</year>
<volume>37</volume>
<numero>6</numero>
<issue>6</issue>
<page-range>445-9</page-range></nlm-citation>
</ref>
<ref id="B68">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Wagner]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Stepwise assembly of dimeric F(1)F(o)-ATP synthase in mitochondria involves the small F(o)-subunits k and i]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Perschil]]></surname>
<given-names><![CDATA[I.]]></given-names>
</name>
<name>
<surname><![CDATA[Fichter]]></surname>
<given-names><![CDATA[C.D.]]></given-names>
</name>
<name>
<surname><![CDATA[van der Laan]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
</person-group>
<source><![CDATA[Mol. Biol. Cell.]]></source>
<year>2010</year>
<volume>21</volume>
<numero>9</numero>
<issue>9</issue>
<page-range>1494-504</page-range></nlm-citation>
</ref>
<ref id="B69">
<nlm-citation citation-type="journal">
<article-title xml:lang=""><![CDATA[The ATP synthase: the understood, the uncertain and the unknown]]></article-title>
<person-group person-group-type="author">
<name>
<surname><![CDATA[Walker]]></surname>
<given-names><![CDATA[J.E.]]></given-names>
</name>
</person-group>
<source><![CDATA[Biochem. Soc. Trans.]]></source>
<year>2013</year>
<volume>41</volume>
<page-range>1-16</page-range></nlm-citation>
</ref>
<ref id="B70">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Welch]]></surname>
<given-names><![CDATA[A.K.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The b (arg36) contributes to efficient coupling in F(1)F(o) ATP synthase in Escherichia coli]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Claggett]]></surname>
<given-names><![CDATA[S.B.]]></given-names>
</name>
<name>
<surname><![CDATA[Cain]]></surname>
<given-names><![CDATA[B.D.]]></given-names>
</name>
</person-group>
<source><![CDATA[J. Bioenerg. Biomembr.]]></source>
<year>2008</year>
<volume>40</volume>
<numero>1</numero>
<issue>1</issue>
<page-range>1-8</page-range></nlm-citation>
</ref>
<ref id="B71">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Wittig]]></surname>
<given-names><![CDATA[I.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Structural organization of mitochondrial ATP synthase]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Schägger]]></surname>
<given-names><![CDATA[H.]]></given-names>
</name>
</person-group>
<source><![CDATA[Biochim. Biophys. Acta]]></source>
<year>2008</year>
<volume>1777</volume>
<numero>7-8</numero>
<issue>7-8</issue>
<page-range>592-8</page-range></nlm-citation>
</ref>
<ref id="B72">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Yoshida]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[ATP synthase-a marvellous rotary engine of the cell]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Muneyuki]]></surname>
<given-names><![CDATA[E.]]></given-names>
</name>
<name>
<surname><![CDATA[Hisabori]]></surname>
<given-names><![CDATA[T.]]></given-names>
</name>
</person-group>
<source><![CDATA[Nat. Rev. Mol. Cell . Biol.]]></source>
<year>2001</year>
<volume>2</volume>
<numero>9</numero>
<issue>9</issue>
<page-range>669-77</page-range></nlm-citation>
</ref>
<ref id="B73">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Zhou]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Rohou]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
<name>
<surname><![CDATA[Scheo]]></surname>
<given-names><![CDATA[D.G.]]></given-names>
</name>
<name>
<surname><![CDATA[Bason]]></surname>
<given-names><![CDATA[J.V.]]></given-names>
</name>
<name>
<surname><![CDATA[Montgomery]]></surname>
<given-names><![CDATA[M.G.]]></given-names>
</name>
<name>
<surname><![CDATA[Walker]]></surname>
<given-names><![CDATA[J.E.]]></given-names>
</name>
<name>
<surname><![CDATA[Grigorieff]]></surname>
<given-names><![CDATA[N.]]></given-names>
</name>
<name>
<surname><![CDATA[Rubinstein]]></surname>
<given-names><![CDATA[J.L.]]></given-names>
</name>
</person-group>
<source><![CDATA[eLife]]></source>
<year>2015</year>
<volume>4</volume>
<page-range>e10180</page-range></nlm-citation>
</ref>
<ref id="B74">
<nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Zíková]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The F(o)F(1)-ATP synthase complex contains novel subunits and is essential for procyclic Trypanosoma brucei]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Schnaufer]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
<name>
<surname><![CDATA[Dalley]]></surname>
<given-names><![CDATA[R.A.]]></given-names>
</name>
<name>
<surname><![CDATA[Panigrahi]]></surname>
<given-names><![CDATA[A.K.]]></given-names>
</name>
<name>
<surname><![CDATA[Stuart]]></surname>
<given-names><![CDATA[K.D.]]></given-names>
</name>
</person-group>
<source><![CDATA[PLoSPathog.]]></source>
<year>2009</year>
<volume>5</volume>
<numero>5</numero>
<issue>5</issue>
<page-range>e1000436</page-range></nlm-citation>
</ref>
</ref-list>
</back>
</article>
