Urea denaturation of α‐hemolysin pore inserted in planar lipid bilayer detected by single nanopore recording: Loss of structural asymmetry
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J. Betton | L. Auvray | J. Pelta | J. Mathé | G. Oukhaled | Jean-Michel Betton | Manuela Pastoriza-Gallego | Bénédicte Thiebot | Loïc Auvray | Juan Pelta | Jérôme Mathé | B. Thiébot | Ghani Oukhaled | Manuela Pastoriza-Gallego
[1] Sergey M. Bezrukov,et al. Dynamics and Free Energy of Polymers Partitioning into a Nanoscale Pore , 1996 .
[2] H. Bayley,et al. Temperature-responsive protein pores. , 2006, Journal of the American Chemical Society.
[3] S H White,et al. Hydrophobic interactions of peptides with membrane interfaces. , 1998, Biochimica et biophysica acta.
[4] Yi-Tao Long,et al. Transport of R-Helical Peptides through R-Hemolysin and Aerolysin Pores † , 2006 .
[5] M Montal,et al. Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties. , 1972, Proceedings of the National Academy of Sciences of the United States of America.
[6] E. Gouaux. α-Hemolysin fromStaphylococcus aureus:An Archetype of β-Barrel, Channel-Forming Toxins , 1998 .
[7] Helen R Saibil,et al. The mechanism of pore formation by bacterial toxins. , 2006, Current opinion in structural biology.
[8] Gianfranco Menestrina,et al. Ionic channels formed byStaphylococcus aureus alpha-toxin: Voltage-dependent inhibition by divalent and trivalent cations , 2005, The Journal of Membrane Biology.
[9] V. Picciarelli,et al. Effect of Sterols on β-Amyloid Peptide (AβP 1–40) Channel Formation and their Properties in Planar Lipid Membranes , 2004 .
[10] G. Viero,et al. Ion channels and bacterial infection: the case of β‐barrel pore‐forming protein toxins of Staphylococcus aureus , 2003, FEBS letters.
[11] M. Misakian,et al. Electrostatic Influence on Ion Transport through the αHL Channel , 2003, The Journal of Membrane Biology.
[12] M Misakian,et al. Driven DNA transport into an asymmetric nanometer-scale pore. , 2000, Physical review letters.
[13] Li-Qun Gu,et al. Single protein pores containing molecular adapters at high temperatures. , 2005, Angewandte Chemie.
[14] E. Gouaux. alpha-Hemolysin from Staphylococcus aureus: an archetype of beta-barrel, channel-forming toxins. , 1998, Journal of structural biology.
[15] S. Bezrukov,et al. The charge state of an ion channel controls neutral polymer entry into its pore , 1997, European Biophysics Journal.
[16] M. Parker,et al. Pore-forming protein toxins: from structure to function. , 2005, Progress in biophysics and molecular biology.
[17] A. Meller,et al. Nanopore unzipping of individual DNA hairpin molecules. , 2004, Biophysical journal.
[18] D. Branton,et al. Characterization of individual polynucleotide molecules using a membrane channel. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[19] M. Colombini,et al. Self-catalyzed Insertion of Proteins into Phospholipid Membranes* , 1996, The Journal of Biological Chemistry.
[20] R. Lal,et al. Amyloid β protein forms ion channels: implications for Alzheimer's disease pathophysiology , 2001, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[21] K. Banerjee,et al. Unfolding of Vibrio cholerae Hemolysin Induces Oligomerization of the Toxin Monomer* , 2003, Journal of Biological Chemistry.
[22] J. Gouaux,et al. Structure of Staphylococcal α-Hemolysin, a Heptameric Transmembrane Pore , 1996, Science.
[23] D. Branton,et al. Microsecond time-scale discrimination among polycytidylic acid, polyadenylic acid, and polyuridylic acid as homopolymers or as segments within single RNA molecules. , 1999, Biophysical journal.
[24] Michelle Montoya,et al. Beta-barrel membrane protein folding and structure viewed through the lens of alpha-hemolysin. , 2003, Biochimica et biophysica acta.
[25] D. Branton,et al. Unzipping kinetics of double-stranded DNA in a nanopore. , 2002, Physical review letters.
[26] S. Ferreira,et al. Formation of Soluble Oligomers and Amyloid Fibrils with Physical Properties of the Scrapie Isoform of the Prion Protein from the C-terminal Domain of Recombinant Murine Prion Protein mPrP-(121–231)* , 2006, Journal of Biological Chemistry.
[27] V. Picciarelli,et al. Effect of sterols on beta-amyloid peptide (AbetaP 1-40) channel formation and their properties in planar lipid membranes. , 2004, Biophysical journal.
[28] Stanley B. Prusiner,et al. Nobel Lecture: Prions , 1998 .
[29] K. Schulten,et al. Imaging alpha-hemolysin with molecular dynamics: ionic conductance, osmotic permeability, and the electrostatic potential map. , 2005, Biophysical journal.
[30] Michelle Montoya,et al. β-Barrel membrane protein folding and structure viewed through the lens of α-hemolysin , 2003 .
[31] R. Ward,et al. A stability transition at mildly acidic pH in the alpha‐hemolysin (alpha‐toxin) from Staphylococcus aureus , 1999, FEBS letters.
[32] H. Bayley,et al. Stochastic sensors inspired by biology , 2001, Nature.
[33] D. P. Remeta,et al. Energetics of membrane protein folding and stability. , 2006, Archives of biochemistry and biophysics.
[34] J. M. Scholtz,et al. Interactions of peptides with a protein pore. , 2005, Biophysical journal.
[35] P. Lansbury,et al. Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins? , 2006, Quarterly Reviews of Biophysics.
[36] C. Lesieur,et al. Increased Stability upon Heptamerization of the Pore-forming Toxin Aerolysin* , 1999, The Journal of Biological Chemistry.
[37] J. Betton,et al. Unfolding of proteins and long transient conformations detected by single nanopore recording. , 2007, Physical review letters.
[38] Yi-Tao Long,et al. Transport of alpha-helical peptides through alpha-hemolysin and aerolysin pores. , 2006, Biochemistry.
[39] Rushana Azimova,et al. Amyloid Peptide Channels , 2004, The Journal of Membrane Biology.