BIBLIOGRAPHY Mishra, V. K., Palgunachari, M. N., Segrest, J. P., and Anantharamaiah, G. M. (1994). <strong>Interaction</strong>s <strong>of</strong> Synthetic Peptide Analogs <strong>of</strong> the Class A Amphipathic Helix With Lipids. Evidence for the Snorkel Hypothesis. J. Biol. Chem. 269: 7185-7191. Monné, M., Nilsson, I., Johansson, M., Elmhed, N., and von Heijne, G. (1998). Positively and Negatively Charged Residues Have Different Effects on the Position in the Membrane <strong>of</strong> a Model Trans<strong>membrane</strong> Helix. J. Mol. Biol. 284: 1177-1183. Morein, S., Killian, J. A., and Sperotto M. (2002). Characterization <strong>of</strong> the Thermotropic Behaviour and Lateral Organization <strong>of</strong> Lipid-Peptide Mixtures by a Combined Experimental and Theoretical Approach: Effects <strong>of</strong> Hydrophobic Mismatch and Role <strong>of</strong> Flanking Residues. Biophys. J. 82: 1405-1417. Mouritsen, O. G., and Bloom, M. (1984). Mattress Model <strong>of</strong> Lipid-Protein <strong>Interaction</strong>s in Membranes. Biophys. J. 46: 141-153. Mouritsen, O. G., and Bloom, M. (1993). Models <strong>of</strong> Lipid-Protein <strong>Interaction</strong>s in Membranes. Annu. Rev. Biophys. Bioeng. 22: 145-171. Mouritsen, O.G. (2005). Life – As a Matter <strong>of</strong> Fat. The Emerging Science <strong>of</strong> Lipidomics. Springer, Heildelberg, Germany. Nadler, G., Morvan, M., Delimoge, I., Belfiore, P., Zocchetti, A., James, I., Zembryki, D., Lee- Rycakzewski, E., Parini, C., Consolandi, E., Gagliardi, S., and Farina, C. (1998). (2Z,4E)-5-(5,6-dichloro- 2-indolyl)-2-methoxy-n-(1,2,2,6,6-pentamethylpiperidin-4-yl)-2,4-pentadienamide, a Novel, Potent and Selective Inhibitor <strong>of</strong> the Osteoclast V-ATPase. Bioorg. Medic. Chem. Lett. 8: 3621-3626. Nagle, J. F., and Tritram-Nagle, S. (2000). Structure <strong>of</strong> Lipid Bilayers. Biochim. Biophys. Acta 1469: 159-195. Neumann, D., Barchan D., Fridkint, M., and Fuchs, S. (1986). Analysis <strong>of</strong> Ligand Binding to the Synthetic Dodecapeptide <strong>of</strong> the Acetylcholine Receptor a Subunit. Proc. Natl. Acad. Sci. USA 83: 9250-9253. Neves, P., Berkane, E., Gameiro, P., Winterhalter, M., and de Castro, B. (2005). <strong>Interaction</strong> Between Quinolones Antibiotics and Bacterial Outer Membrane Porin OmpF. Biophys. Chem. 113: 123-128. Nielsen, C., Goulian, M., and Andersen, O. S. (1998). Energetics <strong>of</strong> Inclusion-Induced Bilayer Deformations. Biophys. J. 74: 1966-1983. Nieva, J. L., Goni, F. M., and Alonso, A. (1993). Phospholipase C-Promoted Membrane Fusion. Retroinhibition by the End-Product Diacylglycerol. Biochemistry 32: 1054-1058. Nikaido, H., Kim, S. H., and Rosenberg, E. Y. (1993). Physical Organization <strong>of</strong> Lipids in the Cell Wall <strong>of</strong> Mycobacterium Chelonae. Mol. Microbiol. 8: 1025-1030. 199
Nikura, K., Takeshita, N., and Takano, M. (2005). A Vacuolar ATPase inhibitor, FR167356 Prevents Bone Resorption in Ovariectomized Rats With High Potency and Specificity: Potential for Clinical Application. J. Bone Miner. Res. 20: 1579-1588. Nishi, T., and Forgac, M. (2002). The Vacuolar (H + ) - ATPases – Nature’s Most Versatile Proton Pumps. Mol. Cell. Biol. 3: 94-103. O´Keeffe, A. H., East, J. M., and Lee, A. G. (2000). Selectivity in Lipid Binding to the Bacterial Outer Membrane Protein OmpF. Biophys. J. 79: 2066-2074. Páli, T., Whyteside, G., Dixon, N., Kee, T. P., Ball, S., Harrison, M. A., Findlay, J. B. C., Finbow, M. E., and Marsh, D. (2004). <strong>Interaction</strong> <strong>of</strong> Inhibitors <strong>of</strong> the Vacuolar H + -ATPase With the Trans<strong>membrane</strong> V o - sector. Biochemistry. 43: 12297-12305. Pap, E. H. W., van Hoek, A., Wirtz, K. W. A., and Visser, A. J: W. G. (1995). Quantitative Analysis <strong>of</strong> Lipid-Lipid and Lipid-Protein <strong>Interaction</strong>s in Membranes by Use <strong>of</strong> Pyrene-Labeled Phosphoinositides. Biochemistry 34: 9118-9125. Papayannopoulos, V., Co, C., Prehoda, K. E., Snapper, S., Taunton, J., and Lim, W. A. (2005). A Polybasic Motif Allows N-WASP to Act as a Sensor <strong>of</strong> PIP 2 Density. Moll. Cell 17: 181-191. Peelen, S. J. C. J., Sanders, J. C., Hemminga, M. A. and Marsh, D. (1992). Stoichiometry, Selectivity and Exchange Dynamics <strong>of</strong> Lipid-Protein <strong>Interaction</strong> <strong>with</strong> Bacteriophage M13 Coat Protein Studied by Spin Label Electron Spin Resonance. Effects <strong>of</strong> Protein Secondary Structure. Biochemistry 31: 2670-2677. Pérez-Gil, J., Cruz, A., and de la Serra, J. B. (2005). Lateral Membrane Structure and Lipid-Protein <strong>Interaction</strong>s. in “Protein-Lipid <strong>Interaction</strong>s: New Approaches and Emerging Concepts.” (Eds. Mateo, C. R., Gómez, J., Villalaín, J., Ros, J. M. G.) Springer-Verlag. Berlin, Germany. Pestova, E., Millichap, J. J., Noskin, G. A., and Peterson, L. R. (2000). Intracellular Targets <strong>of</strong> Moxifloxacin: A Comparison With Other Fluoroquinolones. J. Antimicrob. Chemother. 45: 583-590. Peter, B. J., Kent, H. M., Mills, I.G., Vallis, Y., Butler, P. J. G., Evans, P. R., and McMahon, H. T. (2004). BAR Domains as Sensors <strong>of</strong> Membrane Curvature: the Amphiphysin BAR Structure. Science 303: 495-499. Petrangoline, G., Supino, R., Pratesi, G., Bo, L. D., Tortoreto, M., Croce, A. C., Misiano, P., Belfiore, P., Farina, C., and Zunino, F. (2006). Effect <strong>of</strong> a Novel Vacuolar-H + -ATPase Inhibitor on Cell and Tumor Response to Camptothecins. Chemot. Antib. Gene Ther. 318: 939-946. Pike, L. J., and Miller, J. M. (1998). Cholesterol Depletion Delocalizes Phosphatidylinositol Bisphosphate and Inhibits Hormone-Stimulated Phosphatidylinositol Turnover. J. Biol. Chem. 273: 22298-22304. 200
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UNIVERSIDADE TÉCNICA DE LISBOA INS
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Fernandes, F., Loura, L. M. S., Fed
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Ao Pedro e Hugo, amigos de longa da
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2.2. - Peptides as models 2.3. - Am
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ABBREVIATIONS AND SYMBOL LIST ABBRE
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RESUMO RESUMO As biomembranas são
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SINOPSE SINOPSE Nas últimas duas d
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SINOPSE podem fornecer informação
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SINOPSE aceitantes. Dadores mais pr
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OUTLINE OUTLINE The last two decade
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OUTLINE membranes with a distributi
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OUTLINE BAR domains (tubulation of
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ion diffusion, as the energy requir
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acid. If no more groups are linked
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sphingomyelin, the most abundant sp
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signal for neighbouring cells to ph
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functional role in process such as
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in the L α phase, while lateral di
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1.7. Lateral heterogeneity in lipid
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the vesicle through bilayer deforma
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Figure I.9 - Depiction of the sever
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Figure I.11 - Experimentally obtain
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drying into a film and ressuspensio
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deactivating agents. Zwitterionic d
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amphipatic helices (see Section 2.3
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size corresponding to the hydrophob
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changes abruptly in the interfacial
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thickness of the bilayer (Section 1
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some α-helical membrane proteins a
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The formation of a lipid population
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homogeneous distribution of lipids
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Figure I.20 - Relative binding cons
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2.9. Lipid phase preferential parti
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In Figure I.21, theoretical simulat
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PROTEIN-PROTEIN AND PROTEIN-LIPID I
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PROTEIN-PROTEIN AND PROTEIN-LIPID I
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PROTEIN-PROTEIN AND PROTEIN-LIPID I
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2430 Biophysical Journal Volume 85
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2432 Fernandes et al. Coat protein
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2434 Fernandes et al. leads to an a
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2436 Fernandes et al. FIGURE 4 (A)
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2438 Fernandes et al. section of th
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2440 Fernandes et al. tein oligomer
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QUANTIFICATION OF PROTEIN-LIPID SEL
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FRET Study of Protein-Lipid Selecti
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FRET Study of Protein-Lipid Selecti
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FRET Study of Protein-Lipid Selecti
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FRET Study of Protein-Lipid Selecti
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BINDING OF INHIBITORS TO A PUTATIVE
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BINDING OF INHIBITORS TO A PUTATIVE
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INTERACTION OF THE INDOLE CLASS OF
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5272 Biochemistry, Vol. 45, No. 16,
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5274 Biochemistry, Vol. 45, No. 16,
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5276 Biochemistry, Vol. 45, No. 16,
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5278 Biochemistry, Vol. 45, No. 16,
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BINDING ASSAYS OF INHIBITORS TOWARD
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1778 F. Fernandes et al. / Biochimi
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1780 F. Fernandes et al. / Biochimi
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1782 F. Fernandes et al. / Biochimi
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1784 F. Fernandes et al. / Biochimi
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1786 F. Fernandes et al. / Biochimi
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apparently the most significant as
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110
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Introduction Quinolones are broad-s
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[9-12]. Having this into considerat
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any case, very similar, probably wi
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placement of the protein around the
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⎛ II t ⎛ R ⎞ 0 ρ () t = exp
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APPENDIX - Derivation of the FRET r
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2 2w J ( t) = '2 R − R + w / 1
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[14] L. Plançon, M. Chami, L. Lete
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acceptors) (Eqs. 4-6) (⋅-⋅-⋅)
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FIGURE 1A FIGURE 1B 130
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FIGURE 4A FIGURE 4B 132
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FIGURE 6A FIGURE 6B 134
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136
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dynamin. Soon after, the same group
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140
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142
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Introduction Control of membrane re
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- Page 216 and 217: BIBLIOGRAPHY IX BIBLIOGRAPHY Albert
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- Page 226 and 227: BIBLIOGRAPHY Pluschke, G., Hirota,
- Page 228 and 229: BIBLIOGRAPHY Sperotto, M. M., and M
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