Hydrophobic Membrane Translocating Sequence Peptides 135 63. Shou, Y. et al., Cyanide-induced apoptosis involves oxidative-stress-activated NFkappaB in cortical neurons, Toxicol. Appl. Pharmacol., 164, 196, 2000. 64. Mohan, R.R. et al., Modulation of TNF-alpha-induced apoptosis in corneal fibroblasts by transcription factor NF-kappaB, Invest. Ophthalmol. Vis. Sci., 41, 1327, 2000. 65. Pampfer, S. et al., Activation of nuclear factor kappaB and induction of apoptosis by tumor necrosis factor-alpha in the mouse uterine epithelial WEG-1 cell line, Biol. Reprod., 63, 879, 2000. 66. Meja, K.K. et al., p38 MAP kinase and MKK-1 co-operate in the generation of GM- CSF from LPS-stimulated human monocytes by an NF-kappa B-independent mechanism, Br. J. Pharmacol., 131, 1143, 2000. 67. Niwa, M. et al., Nuclear factor-kappaB activates dual inhibition sites in the regulation of tumor necrosis factor-alpha-induced neutrophil apoptosis, Eur. J. Pharmacol., 407, 211, 2000. 68. Xiao, C., Ash, K., and Tsang, B., Nuclear factor-kappaB-mediated X-linked inhibitor of apoptosis protein ex<strong>press</strong>ion prevents rat granulosa cells from tumor necrosis factor alpha-induced apoptosis, Endocrinology, 142, 557, 2001. 69. Han, Y.P. et al., TNF-alpha stimulates activation of pro-MMP2 in human skin through NF-(kappa)B mediated induction of MT1-MMP, J. Cell Sci., 114, 131, 2001. 70. Chae, H.J. et al., The p38 mitogen-activated protein kinase pathway regulates interleukin-6 synthesis in response to tumor necrosis factor in osteoblasts, Bone, 28, 45, 2001. 71. Koulich, E. et al., NF-kappaB is involved in the survival of cerebellar granule neurons: association of Ikappabeta phosphorylation with cell survival, J. Neurochem., 76, 1188, 2001. 72. Ropert, C. et al., Requirement of mitogen-activated protein kinases and I kappa B phosphorylation for induction of proinflammatory cytokines synthesis by macrophages indicates functional similarity of receptors triggered by glycosylphosphatidylinositol anchors from parasitic protozoa and bacterial lipopolysaccharide, J. Immunol., 166, 3423, 2001. 73. Barber, A.J. et al., Insulin rescues retinal neurons from apoptosis by a PI-3 kinase/Aktmediated mechanism that reduces the activation of caspase-3, J. Biol. Chem., 276, 32814, 2001. 74. Komi, A., Suzuki, M., and Imamura, T., Permeable FGF-1 nuclear localization signal peptide stimulates DNA synthesis in various cell types but is cell-density sensitive and unable to support cell proliferation, Exp. Cell Res., 243, 408, 1998. 75. Eason, P.D. and Imperiali, B., A potent oligosaccharyl transferase inhibitor that crosses the intracellular endoplasmic reticulum membrane, Biochemistry, 38, 5430, 1999. 76. Rojas, M. et al., An alternative to phosphotyrosine-containing motifs for binding to an SH2 domain, Biochem. Biophys. Res. Commun., 234, 675, 1997. 77. Chang, M. et al., Dissecting G protein-coupled receptor signaling pathways with membrane-permeable blocking peptides. Endogenous 5-HT(2C) receptors in choroid plexus epithelial cells, J. Biol. Chem., 275, 7021, 2000. 78. Fujihara, S.M. et al., A D-amino acid peptide inhibitor of NF-kappa B nuclear localization is efficacious in models of inflammatory disease, J. Immunol., 165, 1004, 2000. 79. Turkson, J. et al., Phosphotyrosyl peptides block Stat3-mediated DNA-binding activity, gene regulation and cell transformation, J. Biol. Chem., Sep 28 [epub ahead of print], 2001. 80. Croce, K. et al., Inhibition of calpain blocks platelet secretion, aggregation, and spreading, J. Biol. Chem., 274, 36321, 1999.
136 Cell-Penetrating Peptides: Processes and Applications 81. Delli Bovi, P. et al., An oncogene isolated by transfection of Kaposi’s sarcoma DNA encodes a growth factor that is a member of the FGF family, Cell, 50, 729, 1987. 82. Lowenstein, E.J. et al., The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling, Cell, 70, 431, 1992. 83. Zhao, Y. et al., Chemical engineering of cell penetrating antibodies, J. Immunol. Methods, 254, 137, 2001. 84. Jo, D. et al., Epigenetic regulation of gene structure and function with a cell-permeable Cre recombinase, Nat. Biotechnol., 19, 929-33, 2001. 85. Li, A.J. et al., Strong sup<strong>press</strong>ion of feeding by a peptide containing both the nuclear localization sequence of fibroblast growth factor-1 and a cell membrane-permeable sequence, Neurosci. Lett., 255, 41, 1998. 86. Sasaki, K. et al., Effects of fibroblast growth factors and related peptides on food intake by rats, Physiol. Behav., 56, 211, 1994. 87. Li, A.J. et al., Fibroblast growth factor receptor-1 in the lateral hypothalamic area regulates food intake, Exp. Neurol., 137, 318, 1996. 88. Liu, X.Y. et al., Identification of a functionally important sequence in the cytoplasmic tail of integrin beta 3 by using cell-permeable peptide analogs, Proc. Natl. Acad. Sci. U.S.A., 93, 11819, 1996. 89. Fitzgerald, L.A. et al., Protein sequence of endothelial glycoprotein IIIa derived from a cDNA clone. Identity with platelet glycoprotein IIIa and similarity to “integrin,” J. Biol. Chem., 262, 3936, 1987. 90. Hawiger, J., Noninvasive intracellular delivery of functional peptides and proteins, Curr. Opin. Chem. Biol., 3, 89, 1999. 91. Joliot, A.H. et al., Alpha-2,8-Polysialic acid is the neuronal surface receptor of antennapedia homeobox peptide, New Biol., 3, 1121, 1991. 92. Lin, Y.Z. and Du, C., Unpublished results. 93. Briggs, M.S. and Gierasch, L.M., Exploring the conformational roles of signal sequences: synthesis and conformational analysis of lambda receptor protein wildtype and mutant signal peptides, Biochemistry, 23, 3111, 1984. 94. Batenburg, A.M. et al., Characterization of the interfacial behavior and structure of the signal sequence of Escherichia coli outer membrane pore protein PhoE, J. Biol. Chem., 263, 4202, 1998. 95. Batenburg, A.M. et al., Penetration of the signal sequence of Escherichia coli PhoE protein into phospholipid model membranes leads to lipid-specific changes in signal peptide structure and alterations of lipid organization, Biochemistry, 27, 5678, 1988. 96. Yamamoto, Y. et al., Conformational requirement of signal sequences functioning in yeast: circular dichroism and 1H nuclear magnetic resonance studies of synthetic peptides, Biochemistry, 29, 8998, 1990. 97. Rizo, J. et al., Conformational behavior of Escherichia coli OmpA signal peptides in membrane mimetic environments, Biochemistry, 32, 4881, 1993. 98. Chupin, V. et al., PhoE signal peptide inserts into micelles as a dynamic helixbreak-helix structure, which is modulated by the environment. A two-dimensional 1H NMR study, Biochemistry, 34, 11617, 1995. 99. Bruch, M.D. and Gierasch, L.M., Comparison of helix stability in wild-type and mutant LamB signal sequences, J. Biol. Chem., 265, 3851, 1990. 100. McKnight, C.J., Briggs, M.S., and Gierasch, L.M., Functional and nonfunctional LamB signal sequences can be distinguished by their biophysical properties, J. Biol. Chem., 264, 17293, 1989. 101. de Vrije, G.J. et al., Lipid involvement in protein translocation in Escherichia coli, Mol. Microbiol., 4, 143, 1990.
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CELL- PENETRATING PEPTIDES Processe
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Pharmacology and Toxicology: Basic
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Library of Congress Cataloging-in-P
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to the handbook are prominent resea
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REFERENCES 1. Green, M. and Loewens
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Contributors Mats Andersson Microbi
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Erin T. Pelkey Department of Chemis
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Contents Section I Classes of Cell-
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Chapter 16 Cell-Penetrating Peptide
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The Tat-Derived Cell-Penetrating Pe
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The Tat-Derived Cell-Penetrating Pe
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The Tat-Derived Cell-Penetrating Pe
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The Tat-Derived Cell-Penetrating Pe
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The Tat-Derived Cell-Penetrating Pe
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The Tat-Derived Cell-Penetrating Pe
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The Tat-Derived Cell-Penetrating Pe
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The Tat-Derived Cell-Penetrating Pe
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The Tat-Derived Cell-Penetrating Pe
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24 Cell-Penetrating Peptides: Proce
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26 Cell-Penetrating Peptides: Proce
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28 Cell-Penetrating Peptides: Proce
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50 Cell-Penetrating Peptides: Proce
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3 Transportans Margus Pooga, Mattia
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Transportans 55 Indeed, galparan is
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Transportans 57 especially the endo
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Transportans 59 In the penetration
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Transportans 61 A 21-mer antisense
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Transportans 63 Commonly, the prote
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Transportans 65 antibiotin antibodi
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Transportans 67 For cross-linking o
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Transportans 69 and still retain ef
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Model Amphipathic Peptides 73 its D
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Model Amphipathic Peptides 75 pmol/
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TABLE 4.1 Internalization of Peptid
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TABLE 4.2 Internalization of Peptid
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Model Amphipathic Peptides 81 relat
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Model Amphipathic Peptides 83 relat
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Interactions of Cell-Penetrating Pe
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Structure Prediction of CPPs and It
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Structure Prediction of CPPs and It
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Structure Prediction of CPPs and It
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Structure Prediction of CPPs and It
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Structure Prediction of CPPs and It
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Structure Prediction of CPPs and It
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Structure Prediction of CPPs and It
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Structure Prediction of CPPs and It
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Structure Prediction of CPPs and It
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FIGURE 9.7 (Color Figure 9.7 follow
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FIGURE 9.8 The center of the figure
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Structure Prediction of CPPs and It
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Structure Prediction of CPPs and It
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Structure Prediction of CPPs and It
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Structure Prediction of CPPs and It
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Structure Prediction of CPPs and It
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Structure Prediction of CPPs and It
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Biophysical Studies of Cell-Penetra
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Biophysical Studies of Cell-Penetra
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Biophysical Studies of Cell-Penetra
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Biophysical Studies of Cell-Penetra
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Toxicity and Side Effects of Cell-P
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Toxicity and Side Effects of Cell-P
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Kinetics of Uptake of Cell-Penetrat
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Kinetics of Uptake of Cell-Penetrat
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Kinetics of Uptake of Cell-Penetrat
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Cell-Penetrating Peptide Conjugatio
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Cell-Penetrating Peptide Conjugatio
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Cell-Penetrating Peptide Conjugatio
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FIGURE 15.9 (Color Figure 15.9 foll
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Cell-Penetrating Peptide Conjugatio
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Cell-Penetrating Peptides as Vector
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TABLE 16.1 Examples of Transport of
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Cell-Penetrating Peptides as Vector
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CPP 2 Cargo or mRNA CAP Antisense A
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Cell-Penetrating Peptides as Vector
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Microbial Membrane-Permeating Pepti
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Microbial Membrane-Permeating Pepti
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Microbial Membrane-Permeating Pepti
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Microbial Membrane-Permeating Pepti
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Microbial Membrane-Permeating Pepti
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Microbial Membrane-Permeating Pepti
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Microbial Membrane-Permeating Pepti
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Microbial Membrane-Permeating Pepti
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Microbial Membrane-Permeating Pepti
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Index A Abaecin, 129 Abz radiolabel
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Index 399 Diffraction, 168 Disulphi
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Index 401 structure prediction, 187
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Index 403 pRB proteins, Tat-E1A bin
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Index 405 lipid perturbation (secon