Franck Duong

Summary

Country: France

Publications

  1. pmc Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase
    Franck Duong
    Laboratoire Transports et Signalisations Cellulaires, CNRS UMR 8619, Université de Paris XI, Batiment 430, Orsay 91405, France
    EMBO J 22:4375-84. 2003
  2. pmc The SecYEG preprotein translocation channel is a conformationally dynamic and dimeric structure
    Pascal Bessonneau
    Laboratoire Transports et Signalisations Cellulaires, IBBMC CNRS UMR 8619, Université de Paris XI, Batiment 430, Orsay 91405, France
    EMBO J 21:995-1003. 2002
  3. ncbi Break on through to the other side--the Sec translocon
    Jerry Eichler
    Department of Life Sciences, Ben Gurion University, PO Box 653, Beersheva 84105 Israel
    Trends Biochem Sci 29:221-3. 2004
  4. ncbi The bacterial protein-translocation complex: SecYEG dimers associate with one or two SecA molecules
    Christos Tziatzios
    Institute für Biophysik, JWG Universität, 60590 Frankfurt am Main, Germany
    J Mol Biol 340:513-24. 2004
  5. pmc Investigating the SecY plug movement at the SecYEG translocation channel
    Patrick C K Tam
    Department of Biochemistry and Molecular Biology, Faculty of Medicine, Life Sciences Institute, University of British Columbia, Vancouver, BC, Canada
    EMBO J 24:3380-8. 2005
  6. ncbi Deregulation of the SecYEG translocation channel upon removal of the plug domain
    Antoine P Maillard
    Department of Biochemistry and Molecular Biology, Life Sciences Institute, Faculty of Medicine, University of British Columbia, Vancouver, British Columbia V6T1Z3, Canada
    J Biol Chem 282:1281-7. 2007
  7. pmc Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA
    Meriem Alami
    Department of Biochemistry and Molecular Biology, Life Sciences Institute, Faculty of Medicine, University of British Columbia, British Columbia, Canada
    EMBO J 26:1995-2004. 2007
  8. ncbi Cell biology: fraternal twins
    Franck Duong
    Nature 446:741-3. 2007
  9. ncbi Structure and function of the bacterial Sec translocon
    Vicki A M Gold
    Department of Biochemistry, University of Bristol, Bristol, UK
    Mol Membr Biol 24:387-94. 2007

Collaborators

  • J Eichler
  • Stephen G Sligar
  • Antoine P Maillard
  • Ian Collinson
  • Vicki A M Gold
  • Meriem Alami
  • Patrick C K Tam
  • Christos Tziatzios
  • Pascal Bessonneau
  • Filo Silva
  • Barbara Lelj-Garolla
  • Kush Dalal
  • Dominique Belin
  • Shifana Lalani
  • Kenneth K Y Chan
  • Derya Gundogan
  • Dieter Schubert
  • Heidi Betz
  • Hermann Schagger
  • Winfried Haase
  • Mirko Lotz
  • Véronique Besson

Detail Information

Publications9

  1. pmc Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase
    Franck Duong
    Laboratoire Transports et Signalisations Cellulaires, CNRS UMR 8619, Université de Paris XI, Batiment 430, Orsay 91405, France
    EMBO J 22:4375-84. 2003
    ..The nucleotides and translocation-dependent changes of SecA-SecYEG associations and the SecA dimeric state may reflect important facets of the preprotein translocation reaction...
  2. pmc The SecYEG preprotein translocation channel is a conformationally dynamic and dimeric structure
    Pascal Bessonneau
    Laboratoire Transports et Signalisations Cellulaires, IBBMC CNRS UMR 8619, Université de Paris XI, Batiment 430, Orsay 91405, France
    EMBO J 21:995-1003. 2002
    ..These results provide direct evidence that preproteins cross the bacterial membrane, associated with a translocation channel formed by a dimer of SecYEG...
  3. ncbi Break on through to the other side--the Sec translocon
    Jerry Eichler
    Department of Life Sciences, Ben Gurion University, PO Box 653, Beersheva 84105 Israel
    Trends Biochem Sci 29:221-3. 2004
  4. ncbi The bacterial protein-translocation complex: SecYEG dimers associate with one or two SecA molecules
    Christos Tziatzios
    Institute für Biophysik, JWG Universität, 60590 Frankfurt am Main, Germany
    J Mol Biol 340:513-24. 2004
    ..The observed variability in the stoichiometry of SecYEG and SecA association and its nucleotide modulation may be important and necessary for the protein translocation reaction...
  5. pmc Investigating the SecY plug movement at the SecYEG translocation channel
    Patrick C K Tam
    Department of Biochemistry and Molecular Biology, Faculty of Medicine, Life Sciences Institute, University of British Columbia, Vancouver, BC, Canada
    EMBO J 24:3380-8. 2005
    ..We propose that oligomerization may result in SecYEG cooperative interactions important to prime the translocon function...
  6. ncbi Deregulation of the SecYEG translocation channel upon removal of the plug domain
    Antoine P Maillard
    Department of Biochemistry and Molecular Biology, Life Sciences Institute, Faculty of Medicine, University of British Columbia, Vancouver, British Columbia V6T1Z3, Canada
    J Biol Chem 282:1281-7. 2007
    ..We propose that the plug contributes to the gating mechanism of the channel by maintaining the structure of the SecYEG complex in a compact closed state...
  7. pmc Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA
    Meriem Alami
    Department of Biochemistry and Molecular Biology, Life Sciences Institute, Faculty of Medicine, University of British Columbia, British Columbia, Canada
    EMBO J 26:1995-2004. 2007
    ..Altogether, the results define the fundamental contribution of the SecYEG protomer in the translocation subreactions and illustrate the power of nanoscale lipid bilayers in analyzing the dynamics occurring at the membrane...
  8. ncbi Cell biology: fraternal twins
    Franck Duong
    Nature 446:741-3. 2007
  9. ncbi Structure and function of the bacterial Sec translocon
    Vicki A M Gold
    Department of Biochemistry, University of Bristol, Bristol, UK
    Mol Membr Biol 24:387-94. 2007
    ..This review will draw on genetic, biochemical and structural findings in an account of our current understanding of this mechanism...