AMPHIPOLS: References

  • References 1-18

  • References 19-36

  1. Popot, J.-L., Berry, E. A., Charvolin, D., Creuzenet, C., Ebel, C., Engelman, D.M., Flötenmeyer, M., Giusti, F., Gohon, Y., Hervé, P., Hong, Q., Lakey, J.H., Leonard, K., Shuman, H.A., Timmins, P., Warschawski, D.E., Zito, F., Zoonens, M., Pucci, B. & Tribet, C. (2003). Amphipols: polymeric surfactants for membrane biology research. Cell. Mol. Life Sci.60, 1559-1574.

  2. Gohon, Y. & Popot, J.-L. (2003). Membrane protein-surfactant complexes. Curr. Opin. Col­loid Interface Sci.8, 15-22.

  3. Sanders, C.R., Hoffmann, A.K., Gray, D.N., Keyes, M.H. & Ellis, C.D. (2004). French swimwear for membrane proteins. ChemBioChem 5, 423-426.
  4. Breyton, C., Pucci, B. & Popot, J.-L. (2010). Amphipols and fluorinated surfactants: two alternatives to detergents for studying membrane proteins in vitro In Heterologous expression of membrane proteins: Methods and protocols (Mus-Veteau, I., ed.), Vol. 601, pp. 219-245. The Humana Press, Totowa, New Jersey, USA.

  5. Popot, J.-L. (2010). Amphipols, nanodiscs, and fluorinated surfactants: three non-conventional approaches to studying membrane proteins in aqueous solutions. Annu. Rev. Biochem. 79, 737-775.

  6. Tribet, C., Audebert, R. & Popot, J.-L. (1996). Amphipols: polymers that keep membrane proteins soluble in aqueous solutions. Proc. Natl. Acad. Sci. USA 93, 15047-15050.

  7. Gohon, Y., Pavlov, G., Timmins, P., Tribet, C., Popot, J.-L. & Ebel, C. (2004). Partial specific volume and solvent interactions of amphipol A8-35. Anal. Biochem. 334, 318-334.

  8. Gohon, Y., Giusti, F., Prata, C., Charvolin, D., Timmins, P., Ebel, C., Tribet, C. & Popot, J.-L. (2006). Well-defined nanoparticles formed by hydrophobic assembly of a short and polydisperse random terpolymer, amphipol A8-35. Langmuir 22, 1281-1290.

  9. Gohon, Y., Dahmane, T., Ruigrok, R., Schuck,P., Charvolin,D., Rappaport, F., Timmins, P., Engelman, D.M., Tribet, C., Popot, J.-L. & Ebel, C. (2008). Bacteriorhodopsin/amphipol complexes: structural and functional properties. Biophys. J. 94, 3523-3537.

  10. Picard, M., Dahmane, T., Garrigos, M., Gauron, C., Giusti, F., le Maire, M., Popot, J.-L. & Champeil, P. (2006). Protective and inhibitory effects of various types of amphipols on the Ca2+-ATPase from sarcoplasmic reticulum: a comparative study. Biochemistry 45, 1861-1869.

  11. Diab, C., Tribet, C., Gohon, Y., Popot, J.-L. & Winnik, F.M. (2007). Complexation of integral membrane proteins by phosphorylcholine-based amphipols. Biochim. Biophys. Acta 1768, 2737-2747.

  12. Zoonens, M., Giusti, F., Zito, F. & Popot, J.-L. (2007). Dynamics of membrane protein/amphipol association studied by Förster resonance energy transfer. Implications for in vitro studies of amphipol-stabilized membrane proteins. Biochemistry 46, 10392-10404.

  13. Tribet, C., Diab, C., Dahmane, T., Zoonens, M., Popot, J.-L. & Winnik, F. M. (2009). Thermodynamic characterization of the exchange of detergents and amphipols at the surfaces of integral membrane proteins. Langmuir 25, 12623-12634.

  14. Zoonens, M., Catoire, L. J., Giusti, F. & Popot, J.-L. (2005). NMR study of a membrane protein in detergent-free aqueous solution. Proc. Natl. Acad. Sci. USA 102, 8893-8898.

  15. Charvolin, D., Picard, M., Huang, L.-S., Courant, J.-C., Berry, E. A. & Popot, J.-L. (2010). Solution behavior and crystallization of cytochrome bc1 in the presence of amphipols. In preparation.

  16. Charvolin, D., Perez, J.-B., Rouvière, F., Giusti, F., Bazzacco, P., Abdine, A., Rappaport, F., Martinez, K.L. & Popot, J.-L. (2009). The use of amphipols as universal molecular adapters to immobilize membrane proteins onto solid supports. Proc. Natl. Acad. Sci. USA 106, 405-410.

  17. Pocanschi, C.L., Dahmane, T., Gohon, Y., Rappaport, F., Apell, H.-J., Kleinschmidt, J.H. & Popot, J.-L. (2006). Amphipathic polymers: tools to fold integral membrane proteins to their active form. Biochemistry 45, 13954-13961.

  18. Dahmane, T., Damian, M., Mary, S., Popot, J.-L. & Banères, J.-L. (2009). Amphipol-assisted in vitro folding of G protein-coupled receptors. Biochemistry 48, 6516-6521.

  1. Catoire, L. J., Zoonens, M., van Heijenoort, C., Giusti, F., Popot, J.-L. & Guittet, E. (2009). Inter- and intramolecular contacts in a membrane protein/surfactant complex observed by heteronuclear dipole-to-dipole cross-relaxation. J. Magn. Res. 197, 91-95.

  2. Champeil, P., Menguy, T., Tribet, C., Popot, J.-L. & le Maire, M. (2000). Interaction of amphipols with the sarcoplasmic reticulum Ca2+-ATPase. J. Biol. Chem. 275, 18623-18637.

  3. Martinez, K.L., Gohon, Y., Corringer, P.-J., Tribet, C., Mérola, F., Changeux, J.-P. & Popot, J.-L. (2002). Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: molecular interactions vs. physical constraints. FEBS Lett. 528, 251-256.

  4. Gorzelle, B. M., Hoffman, A. K., Keyes, M. H., Gray, D. N., Ray, D. G. & Sanders II, C. R. (2002). Amphipols can support the activity of a membrane enzyme. J. Am. Chem. Soc. 124, 11594-11595.

  5. Bazzacco, P. (2009). Non-ionic amphipols: new tools for in vitro studies of membrane proteins. Validation and development of biochemical and biophysical applications. Thèse de Doctorat, Université Paris-7.

  6. Tribet, C., Audebert, R. & Popot, J.-L. (1997). Stabilisation of hydrophobic colloidal dispersions in water with amphiphilic polymers: application to integral membrane proteins. Langmuir 13, 5570-5576.

  7. Tribet, C., Mills, D., Haider, M. & Popot, J.-L. (1998). Scanning transmission electron microscopy study of the molecular mass of amphipol/cytochrome b6 f complexes. Biochimie 80, 475-482.
  8. Flötenmeyer, M., Weiss, H., Tribet, C., Popot, J.-L. & Leonard, K. (2007). The use of amphipathic polymers for cryo-electron microscopy of NADH:ubiquinone oxidoreductase (Complex I). J. Microsc. 227, 229-235.

  9. Nagy, J.K., Kuhn Hoffmann, A., Keyes, M.H., Gray, D.N., Oxenoid, K. & Sanders, C.R. (2001). Use of amphipathic polymers to deliver a membrane protein to lipid bilayers. FEBS Lett. 501, 115-120.
  10. Catoire, L. J., Zoonens, M., van Heijenoort, C., Giusti, F., Guittet, E. & Popot, J.-L. (2010). Solution NMR mapping of water-accessible residues in the transmembrane b-barrel of OmpX. Eur. Biophys. J. 39, 623-630.

  11. Banères, J.-L., Martin, A., Hullot, P., Girard, J.-P., Rossi, J.-C. & Parello, J. (2003). Structure-based analysis of GPCR function. Conformational adaptation of both agonist and receptor upon leukotriene B4 binding to recombinant BLT1. J. Mol. Biol. 329, 801-814.

  12. Popot, J.-L., Gerchman, S.-E. & Engelman, D.M. (1987). Refolding of bacteriorhodopsin in lipid bilayers: a thermodynamically controlled two-stage process. J. Mol. Biol. 198, 655-676.

  13. Diab, C., Winnik, F.M. & Tribet, C. (2007). Enthalpy of interaction and binding isotherms of non-ionic surfactants onto micellar amphiphilic polymers (amphipols). Langmuir 23, 3025-3035.

  14. Dahmane, T., Giusti, F., Catoire, L.J. & Popot, J.-L. (2010). Sulfonated amphipols: synthesis, properties and applications. In preparation.

  15. Prata, C., Giusti, F., Gohon, Y., Pucci, B., Popot, J.-L. & Tribet, C. (2001). Non-ionic amphiphilic polymers derived from tris(hydroxymethyl)-acrylamidomethane keep membrane proteins soluble and native in the absence of detergent. Biopolymers 56, 77-84.

  16. Sharma, K.S., Durand, G., Giusti, F., Olivier, B., Fabiano, A.-S., Bazzacco, P., Dahmane, T., Ebel, C., Popot, J.-L. & Pucci, B. (2008). Glucose-based amphiphilic telomers designed to keep membrane proteins soluble in aqueous solutions: synthesis and physicochemical characterization. Langmuir 24, 13581-13590.

  17. Bazzacco, P., Sharma, K.S., Durand, G., Giusti, F., Ebel, C., Popot, J.-L. & Pucci, B. (2009). Grafted glucose-based amphipols: Synthesis, solution behavior, and biochemical properties. Submitted for publication.

  18. Catoire, L. J., Damian, M., Giusti, F., Martin, A., van Heijenoort, C., Popot, J.-L., Guittet, E. & Banères, J.-L. (2010). Structure of a GPCR ligand in its receptor-bound state: leukotriene B4 adopts a highly constrained conformation when associated to human BLT2. J. Am. Chem. Soc. 132, 9049-9057.