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Interactions of Cell-Penetrating Peptides with Membranes 183
39. Scheller, A. et al., Evidence for an amphipathicity independent cellular uptake of
amphipathic cell-penetrating peptides, Eur. J. Biochem., 267, 6043, 2000.
40. Pooga, M. et al., Cell penetration by transportan, FASEB J., 12, 67, 1998.
41. Lindgren, M. et al., Cell-penetrating peptides, TIPS, 21, 99, 2000.
42. Pooga, M. et al., Cellular translocation of proteins by transportan, FASEB J., 15, 1451,
2001.
43. Goldfarb, D.S. et al., Synthetic peptides as nuclear localization signals, Nature, 322,
641, 1986.
44. Briggs, M.S. and Gierasch, L.M., Molecular mechanisms of protein secretion: the
role of the signal sequence, Adv. Prot. Chem., 38, 109, 1986.
45. Slepushkin, V.A. et al., Investigation of human immunodeficiency virus fusion peptides.
Analysis of interrelations between their structure and function, AIDS Res. Hum.
Retroviruses, 8, 9, 1992.
46. Lindberg, M. et al., Secondary structure and position of the cell-penetrating peptide
transportan in SDS micelles as determined by NMR, Biochemistry, 40, 3141, 2001.
47. Chaloin, L. et al., Conformations of primary amphipathic carrier peptides in membrane
mimicking environments, Biochemistry, 36, 11179, 1997.
48. Vidal, P. et al., Conformational analysis of primary amphipathic carrier peptides and
origin of the various cellular localizations, J. Membrane Biol., 162, 259, 1998.
49. Magzoub, M. et al., Interaction and structure induction of cell-penetrating peptides
in the presence of phospholipid vesicles, Biochim. Biophys. Acta, 1512, 77, 2001.
50. Cross, T., Solid-state nuclear magnetic resonance characterization of gramicidin channel
structure, Methods Enzymol., 289, 672, 1997.
51. Yang, J., Gabrys, C.M., and Weliky, D.P., Solid-state nuclera magnetic resonance
evidence for an extended β strand conformation of the membrane-bound HIV-1 fusion
peptide, Biochemistry, 40, 8126, 2001.
52. Wu, Y., Huang, H.W., and Olah, G.A., Method of oriented circular dichroism, Biophys.
J., 57, 797, 1990.
53. Tamm, L.K. and Tatulian, S.A., Infrared spectroscopy of proteins and peptides in
lipid bilayers, Q. Rev. Biophys., 30, 365, 1997.
54. Goormaghtigh, E., Cabiaux, V., and Ruysschaert, J.M., Determination of soluble and
membrane protein structure by Fourier transform infrared spectroscopy. I. Assignments
and model compounds. II. Experimental aspects, side chain structure, and H/D
exchange. III. Secondary structure, in Subcellular Biochemistry, Vol. 23, Physicochemical
Methods in the Study of Biomembranes (ed. H.J. Hilderson and G.B. Ralston),
New York, Plenum Press, 329–450.
55. Goormaghtigh, E., Raussens, V., and Ruysschaert, J.M., Attenuated total reflection
infrared spectroscopy of proteins and lipids in biological membranes, Biochim. Biophys.
Acta, 1422, 105, 1999.
56. Haris, P.I. and Chapman, D., The conformational analysis of peptides using Fourier
transform IR spectroscopy, Biopolymers, 37, 251, 1995.
57. Vié, V. et al., Detection of peptide–lipid interactions in mixed monolayers, using
isotherms, atomic force micoscopy, and Fourier transform infrared analyses, Biophys.
J., 78, 846, 2000.
58. Van Mau, N. et al., Lipid-induced organization of a primary amphipathic peptide: a
coupled AFM-monolayer study, J. Membr. Biol., 167, 241, 1999.
59. Tatulian, S. and Tamm, L., Secondary structure, orientation, oligomerization, and
lipid interactions of the transmembrane domain of influenza hemagglutinin, Biochemistry,
39 496, 2000.