(en) Andrei L. Lomize, Irina D. Pogozheva et Henry I. Mosberg, « Anisotropic Solvent Model of the Lipid Bilayer. 1. Parameterization of Long-Range Electrostatics and First Solvation Shell Effects », Journal of Chemical Information and Modeling, vol. 51, no 4, , p. 918-929 (PMID21438609, PMCID3089899, DOI10.1021/ci2000192, lire en ligne)
(en) Andrei L. Lomize, Irina D. Pogozheva et Henry I. Mosberg, « Anisotropic Solvent Model of the Lipid Bilayer. 2. Energetics of Insertion of Small Molecules, Peptides, and Proteins in Membranes », Journal of Chemical Information and Modeling, vol. 51, no 4, , p. 930-946 (PMID21438606, PMCID3091260, DOI10.1021/ci200020k, lire en ligne)
(en) Brian Lathrop, Martha Gadd, Rodney L. Biltonen et Gordon S. Rule, « Changes in Ca2+ Affinity upon Activation of Agkistrodon piscivorus piscivorus Phospholipase A2 », Biochemistry, vol. 40, no 11, , p. 3264-3272 (PMID11258945, DOI10.1021/bi001901n, lire en ligne)
annualreviews.org
(en) Nathan J. Malmberg et Joseph J. Falke, « Use of EPR Power Saturation to Analyze the Membrane-Docking Geometries of Peripheral Proteins: Applications to C2 Domains », Annual Review of Biophysics and Biomolecular Structure, vol. 34, , p. 71-90 (PMID15869384, PMCID3637887, DOI10.1146/annurev.biophys.34.040204.144534, lire en ligne)
biomedcentral.com
bmcstructbiol.biomedcentral.com
(en) Andrei L. Lomize, Irina D. Pogozheva, Mikhail A. Lomize et Henry I. Mosberg, « The role of hydrophobic interactions in positioning of peripheral proteins in membranes », BMC Structural Biology, vol. 7, , p. 44 (PMID17603894, PMCID1934363, DOI10.1186/1472-6807-7-44, lire en ligne)
cell.com
(en) Derek Marsh, Micha Jost, Cristina Peggion et Claudio Toniolo, « TOAC Spin Labels in the Backbone of Alamethicin: EPR Studies in Lipid Membranes », Biophysical Journal, vol. 92, no 2, , p. 473-481 (PMID17056731, PMCID1751395, DOI10.1529/biophysj.106.092775, lire en ligne)
doi.org
dx.doi.org
(en) Mikhail A. Lomize, Andrei L. Lomize, Irina D. Pogozheva et Henry I. Mosberg, « OPM: orientations of proteins in membranes database », Bioinformatics, vol. 22, no 5, , p. 623-625 (PMID16397007, DOI10.1093/bioinformatics/btk023)
(en) Andrei L. Lomize, Irina D. Pogozheva, Mikhail A. Lomize et Henry I. Mosberg, « Positioning of proteins in membranes: A computational approach », Protein Science, vol. 15, no 6, , p. 1318-1333 (PMID16731967, PMCID2242528, DOI10.1110/ps.062126106, lire en ligne)
(en) Andrei L. Lomize, Irina D. Pogozheva, Mikhail A. Lomize et Henry I. Mosberg, « The role of hydrophobic interactions in positioning of peripheral proteins in membranes », BMC Structural Biology, vol. 7, , p. 44 (PMID17603894, PMCID1934363, DOI10.1186/1472-6807-7-44, lire en ligne)
(en) Andrei L. Lomize, Irina D. Pogozheva et Henry I. Mosberg, « Anisotropic Solvent Model of the Lipid Bilayer. 1. Parameterization of Long-Range Electrostatics and First Solvation Shell Effects », Journal of Chemical Information and Modeling, vol. 51, no 4, , p. 918-929 (PMID21438609, PMCID3089899, DOI10.1021/ci2000192, lire en ligne)
(en) Andrei L. Lomize, Irina D. Pogozheva et Henry I. Mosberg, « Anisotropic Solvent Model of the Lipid Bilayer. 2. Energetics of Insertion of Small Molecules, Peptides, and Proteins in Membranes », Journal of Chemical Information and Modeling, vol. 51, no 4, , p. 930-946 (PMID21438606, PMCID3091260, DOI10.1021/ci200020k, lire en ligne)
(en) Nathan J. Malmberg et Joseph J. Falke, « Use of EPR Power Saturation to Analyze the Membrane-Docking Geometries of Peripheral Proteins: Applications to C2 Domains », Annual Review of Biophysics and Biomolecular Structure, vol. 34, , p. 71-90 (PMID15869384, PMCID3637887, DOI10.1146/annurev.biophys.34.040204.144534, lire en ligne)
(en) Andrew G. Spencer, Elizabeth Thuresson, James C. Otto, Inseok Song, Tim Smith, David L. DeWitt, R. Michael Garavito et William L. Smith, « The membrane binding domains of prostaglandin endoperoxide H synthases 1 and 2. Peptide mapping and mutational analysis », Journal of Biological Chemistry, vol. 274, no 46, , p. 32936-32942 (PMID10551860, DOI10.1074/jbc.274.46.32936, lire en ligne)
(en) Brian Lathrop, Martha Gadd, Rodney L. Biltonen et Gordon S. Rule, « Changes in Ca2+ Affinity upon Activation of Agkistrodon piscivorus piscivorus Phospholipase A2 », Biochemistry, vol. 40, no 11, , p. 3264-3272 (PMID11258945, DOI10.1021/bi001901n, lire en ligne)
(en) Suren A. Tatulian, Shan Qin, Abhay H. Pande, Xiaomei He, « Positioning Membrane Proteins by Novel Protein Engineering and Biophysical Approaches », Journal of Molecular Biology, vol. 351, no 5, , p. 939-947 (PMID16055150, DOI10.1016/j.jmb.2005.06.080, lire en ligne)
(en) Kalina Hristova, William C. Wimley, Vinod K. Mishra, G. M. Anantharamiah, Jere P. Segrest, Stephen H. White, « An amphipathic α-helix at a membrane interface: a structural study using a novel X-ray diffraction method », Journal of Molecular Biology, vol. 290, no 1, , p. 99-117 (PMID10388560, DOI10.1006/jmbi.1999.2840, lire en ligne)
(en) Yungki Park et Volkhard Helms, « On the derivation of propensity scales for predicting exposed transmembrane residues of helical membrane proteins », Bioinformatics, vol. 23, no 6, , p. 701-708 (PMID17237049, DOI10.1093/bioinformatics/btl653, lire en ligne)
(en) Derek Marsh, Micha Jost, Cristina Peggion et Claudio Toniolo, « TOAC Spin Labels in the Backbone of Alamethicin: EPR Studies in Lipid Membranes », Biophysical Journal, vol. 92, no 2, , p. 473-481 (PMID17056731, PMCID1751395, DOI10.1529/biophysj.106.092775, lire en ligne)
(en) V. Cherezov, E. Yamashita, W. Liu, M. Zhalnina, W. A. Cramer et M. Caffrey, « In Meso Structure of the Cobalamin Transporter, BtuB, at 1.95 Å Resolution », Journal of Molecular Biology, vol. 364, no 4, , p. 716-734 (PMID17028020, PMCID1808586, DOI10.1016/j.jmb.2006.09.022, lire en ligne)
(en) Tibor Páli, Denys Bashtovyy et Derek Marsh, « Stoichiometry of lipid interactions with transmembrane proteins—Deduced from the 3D structures », Protein Science, vol. 15, no 5, , p. 1153-1161 (PMID16641489, PMCID2242517, DOI10.1110/ps.052021406, lire en ligne)
jbc.org
(en) Andrew G. Spencer, Elizabeth Thuresson, James C. Otto, Inseok Song, Tim Smith, David L. DeWitt, R. Michael Garavito et William L. Smith, « The membrane binding domains of prostaglandin endoperoxide H synthases 1 and 2. Peptide mapping and mutational analysis », Journal of Biological Chemistry, vol. 274, no 46, , p. 32936-32942 (PMID10551860, DOI10.1074/jbc.274.46.32936, lire en ligne)
nih.gov
ncbi.nlm.nih.gov
(en) Mikhail A. Lomize, Andrei L. Lomize, Irina D. Pogozheva et Henry I. Mosberg, « OPM: orientations of proteins in membranes database », Bioinformatics, vol. 22, no 5, , p. 623-625 (PMID16397007, DOI10.1093/bioinformatics/btk023)
(en) Andrei L. Lomize, Irina D. Pogozheva, Mikhail A. Lomize et Henry I. Mosberg, « Positioning of proteins in membranes: A computational approach », Protein Science, vol. 15, no 6, , p. 1318-1333 (PMID16731967, PMCID2242528, DOI10.1110/ps.062126106, lire en ligne)
(en) Andrei L. Lomize, Irina D. Pogozheva, Mikhail A. Lomize et Henry I. Mosberg, « The role of hydrophobic interactions in positioning of peripheral proteins in membranes », BMC Structural Biology, vol. 7, , p. 44 (PMID17603894, PMCID1934363, DOI10.1186/1472-6807-7-44, lire en ligne)
(en) Andrei L. Lomize, Irina D. Pogozheva et Henry I. Mosberg, « Anisotropic Solvent Model of the Lipid Bilayer. 1. Parameterization of Long-Range Electrostatics and First Solvation Shell Effects », Journal of Chemical Information and Modeling, vol. 51, no 4, , p. 918-929 (PMID21438609, PMCID3089899, DOI10.1021/ci2000192, lire en ligne)
(en) Andrei L. Lomize, Irina D. Pogozheva et Henry I. Mosberg, « Anisotropic Solvent Model of the Lipid Bilayer. 2. Energetics of Insertion of Small Molecules, Peptides, and Proteins in Membranes », Journal of Chemical Information and Modeling, vol. 51, no 4, , p. 930-946 (PMID21438606, PMCID3091260, DOI10.1021/ci200020k, lire en ligne)
(en) Nathan J. Malmberg et Joseph J. Falke, « Use of EPR Power Saturation to Analyze the Membrane-Docking Geometries of Peripheral Proteins: Applications to C2 Domains », Annual Review of Biophysics and Biomolecular Structure, vol. 34, , p. 71-90 (PMID15869384, PMCID3637887, DOI10.1146/annurev.biophys.34.040204.144534, lire en ligne)
(en) Andrew G. Spencer, Elizabeth Thuresson, James C. Otto, Inseok Song, Tim Smith, David L. DeWitt, R. Michael Garavito et William L. Smith, « The membrane binding domains of prostaglandin endoperoxide H synthases 1 and 2. Peptide mapping and mutational analysis », Journal of Biological Chemistry, vol. 274, no 46, , p. 32936-32942 (PMID10551860, DOI10.1074/jbc.274.46.32936, lire en ligne)
(en) Brian Lathrop, Martha Gadd, Rodney L. Biltonen et Gordon S. Rule, « Changes in Ca2+ Affinity upon Activation of Agkistrodon piscivorus piscivorus Phospholipase A2 », Biochemistry, vol. 40, no 11, , p. 3264-3272 (PMID11258945, DOI10.1021/bi001901n, lire en ligne)
(en) Suren A. Tatulian, Shan Qin, Abhay H. Pande, Xiaomei He, « Positioning Membrane Proteins by Novel Protein Engineering and Biophysical Approaches », Journal of Molecular Biology, vol. 351, no 5, , p. 939-947 (PMID16055150, DOI10.1016/j.jmb.2005.06.080, lire en ligne)
(en) Kalina Hristova, William C. Wimley, Vinod K. Mishra, G. M. Anantharamiah, Jere P. Segrest, Stephen H. White, « An amphipathic α-helix at a membrane interface: a structural study using a novel X-ray diffraction method », Journal of Molecular Biology, vol. 290, no 1, , p. 99-117 (PMID10388560, DOI10.1006/jmbi.1999.2840, lire en ligne)
(en) Yungki Park et Volkhard Helms, « On the derivation of propensity scales for predicting exposed transmembrane residues of helical membrane proteins », Bioinformatics, vol. 23, no 6, , p. 701-708 (PMID17237049, DOI10.1093/bioinformatics/btl653, lire en ligne)
(en) Derek Marsh, Micha Jost, Cristina Peggion et Claudio Toniolo, « TOAC Spin Labels in the Backbone of Alamethicin: EPR Studies in Lipid Membranes », Biophysical Journal, vol. 92, no 2, , p. 473-481 (PMID17056731, PMCID1751395, DOI10.1529/biophysj.106.092775, lire en ligne)
(en) V. Cherezov, E. Yamashita, W. Liu, M. Zhalnina, W. A. Cramer et M. Caffrey, « In Meso Structure of the Cobalamin Transporter, BtuB, at 1.95 Å Resolution », Journal of Molecular Biology, vol. 364, no 4, , p. 716-734 (PMID17028020, PMCID1808586, DOI10.1016/j.jmb.2006.09.022, lire en ligne)
(en) Tibor Páli, Denys Bashtovyy et Derek Marsh, « Stoichiometry of lipid interactions with transmembrane proteins—Deduced from the 3D structures », Protein Science, vol. 15, no 5, , p. 1153-1161 (PMID16641489, PMCID2242517, DOI10.1110/ps.052021406, lire en ligne)
oxfordjournals.org
bioinformatics.oxfordjournals.org
(en) Yungki Park et Volkhard Helms, « On the derivation of propensity scales for predicting exposed transmembrane residues of helical membrane proteins », Bioinformatics, vol. 23, no 6, , p. 701-708 (PMID17237049, DOI10.1093/bioinformatics/btl653, lire en ligne)
sciencedirect.com
(en) Suren A. Tatulian, Shan Qin, Abhay H. Pande, Xiaomei He, « Positioning Membrane Proteins by Novel Protein Engineering and Biophysical Approaches », Journal of Molecular Biology, vol. 351, no 5, , p. 939-947 (PMID16055150, DOI10.1016/j.jmb.2005.06.080, lire en ligne)
(en) Kalina Hristova, William C. Wimley, Vinod K. Mishra, G. M. Anantharamiah, Jere P. Segrest, Stephen H. White, « An amphipathic α-helix at a membrane interface: a structural study using a novel X-ray diffraction method », Journal of Molecular Biology, vol. 290, no 1, , p. 99-117 (PMID10388560, DOI10.1006/jmbi.1999.2840, lire en ligne)
(en) V. Cherezov, E. Yamashita, W. Liu, M. Zhalnina, W. A. Cramer et M. Caffrey, « In Meso Structure of the Cobalamin Transporter, BtuB, at 1.95 Å Resolution », Journal of Molecular Biology, vol. 364, no 4, , p. 716-734 (PMID17028020, PMCID1808586, DOI10.1016/j.jmb.2006.09.022, lire en ligne)
(en) Andrei L. Lomize, Irina D. Pogozheva, Mikhail A. Lomize et Henry I. Mosberg, « Positioning of proteins in membranes: A computational approach », Protein Science, vol. 15, no 6, , p. 1318-1333 (PMID16731967, PMCID2242528, DOI10.1110/ps.062126106, lire en ligne)
(en) Tibor Páli, Denys Bashtovyy et Derek Marsh, « Stoichiometry of lipid interactions with transmembrane proteins—Deduced from the 3D structures », Protein Science, vol. 15, no 5, , p. 1153-1161 (PMID16641489, PMCID2242517, DOI10.1110/ps.052021406, lire en ligne)