david poger's homepage
publications
peer-reviewed articles
  1. Poger D. & Mark A. E. (2015) Effect of ring size in ω-alicyclic fatty acids on the structural and dynamical properties associated with fluidity in lipid bilayers. Langmuir 31 (42), 11574–11582
    doi: 10.1021/acs.langmuir.5b02635
  2. Poger D. & Mark A. E. (2015) A ring to rule them all: the effect of cyclopropane fatty acids on the fluidity of lipid bilayers. J. Phys. Chem. B 119 (17), 5487–5495
    doi: 10.1021/acs.jpcb.5b00958
  3. Poger D., Caron, B. & Mark A. E. (2014) Effect of methyl-branched fatty acids on the structure of lipid bilayers. J. Phys. Chem. B 118 (48), 13838–13848
    doi: 10.1021/jp503910r
  4. Caron, B., Mark A. E. & Poger D. (2014) Some like it hot: the effect of sterols and hopanoids on lipid ordering at high temperature. J. Phys. Chem. Lett. 5 (22), 3953–3957
    doi: 10.1021/jz5020778
  5. Poger D. & Mark A. E. (2014) Activation of the epidermal growth factor receptor: a series of twists and turns. Biochemistry 53 (16), 2710–2721
    doi: 10.1021/bi401632z
  6. Xue, Y., He, L., Middelberg, A. P. J., Mark, A. E. & Poger D. (2014) Determining the structure of interfacial peptide films: comparing neutron reflectometry and molecular dynamics simulations. Langmuir 30 (33), 10080–10089
    doi: 10.1021/la501715h
  7. Poger D. & Mark A. E. (2013) The relative effect of sterols and hopanoids on lipid bilayers: when comparable is not identical. J. Phys. Chem. B 117 (50), 16129–16140
    doi: 10.1021/jp409748d
  8. Poger D. & Mark A. E. (2012) Lipid bilayers: the effect of force field on ordering and dynamics. J. Chem. Theory Comput. 8 (11), 4807–4817
    doi: 10.1021/ct300675z
  9. Malde, A. K., Zuo, L., Breeze, M., Stroet, M., Poger D., Nair, P. C., Oostenbrink, C. & Mark, A. E. (2011) An Automated force field Topology Builder (ATB) and repository: version 1.0. J. Chem. Theory Comput. 7 (12), 4026–4037
    doi: 10.1021/ct200196m
  10. Chen, R., Poger D. & Mark A. E. (2011) Effect of high pressure on fully hydrated DPPC and POPC bilayers. J. Phys. Chem. B 115 (5), 1038–1044
    doi: 10.1021/jp110002q
  11. Groothuizen, F. S., Poger D. & Mark A. E. (2010) Activating the prolactin receptor: effect of the ligand on the conformation of the extracellular domain. J. Chem. Theory Comput. 6 (10), 3274–3283
    doi: 10.1021/ct1003934
  12. Poger D. & Mark A. E. (2010) On the validation of molecular dynamics simulations of saturated and cis-monounsaturated phosphatidylcholine lipid bilayers: a comparison with experiment. J. Chem. Theory Comput. 6 (1), 325–336
    doi: 10.1021/ct900487a
  13. Poger D. & Mark A. E. (2010) Turning the growth hormone receptor on: evidence that hormone binding induces subunit rotation. Proteins 78 (5), 1163–1174
    doi: 10.1002/prot.22636
  14. Poger D., van Gunsteren W. F. & Mark A. E. (2010) A new force field for simulating phosphatidylcholine bilayers. J. Comput. Chem. 31 (6), 1117–1125
    doi: 10.1002/jcc.21396
  15. Poger D., Fillaux C., Miras R., Crouzy S., Delangle P., Mintz E., Den Auwer C. & Ferrand M. (2008) Interplay between glutathione, Atx1 and copper: X-ray absorption spectroscopy determination of Cu(I) environment in an Atx1 dimer. J. Biol. Inorg. Chem. 13 (8), 1239–1248
    doi: 10.1007/s00775-008-0408-1
  16. Fuchs J.-F., Nedev H., Poger D., Ferrand M., Brenner V., Dognon J.-P. & Crouzy S. (2006) New model potentials for sulfur–copper(I) and sulfur–mercury(II) interactions in proteins: from ab initio to molecular dynamics. J. Comput. Chem. 27 (7), 837–856
    doi: 10.1002/jcc.20392
  17. Poger D., Fuchs J.-F., Nedev H., Ferrand M. & Crouzy S. (2005) Molecular dynamics study of the metallochaperone Hah1 in its apo and Cu(I)-loaded states: role of the conserved residue M10. FEBS Lett. 579 (24), 5287–5292
    doi: 10.1016/j.febslet.2005.08.052
book chapters
  1. Poger D. & Mark, A. E. (2013) Study of proteins and peptides at interfaces by molecular dynamics simulation techniques. In J. M. Ruso & Á. Piñeiro (Eds), Proteins in solution and at interfaces: Methods and applications in biotechnology and materials science (first edition) (pp. 291–313). Hoboken, NJ, USA, John Wiley & Sons.
    doi: 10.1002/9781118523063.ch14
poster communications
  1. Poger D. & Mark, A. E. (2010) Activation of the epidermal growth factor receptor: a twisted story.
    OzBio2010, Melbourne (Australia)
  2. Poger D. & Mark, A. E. (2009) The human growth hormone receptor turned on.
    34th Lorne Conference on Protein Structure and Dynamics, Lorne (Australia)
  3. Poger D. & Mark, A. E. (2008) Early steps of the formation of a pore by Equinatoxin II.
    33rd Lorne Conference on Protein Structure and Dynamics, Lorne (Australia)
  4. Poger D. & Mark, A. E. (2007) When Equinatoxin II binds to membranes.
    Eur. Biophys. J. (2007), 36 (Suppl. 1), S100
    6th EBSA European Biophysics Congress, London (UK)
  5. Poger D. & Mark, A. E. (2007) Interaction of Equinatoxin II with a POPC membrane
    32nd Lorne Conference on Protein Structure and Dynamics, Lorne (Australia)
  6. Poger D., Fuchs J.-F., Nedev H., Ferrand M. & Crouzy S. (2005) Molecular dynamics study of the metallochaperone Hah1 – What role for the conserved residue M10?
    Eur. Biophys. J. (2005), 34 (6), 743
    Joint 15th IUPAB/5th EBSA International Biophysics Congress, Montpellier (France)
  7. Poger D., Fuchs J.-F., Ferrand M. & Crouzy S. (2003) Complexation of Cu(I) by the metallochaperone Atx1
    Eur. Biophys. J. (2007), 32 (3), 212
    4th EBSA European Biophysics Congress, Alicante (Spain)
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