Signal Peptides 321 151. Martoglio, B. and Dobberstein, B., Signal sequences: more than just greedy peptides, Trends Cell Biol., 8, 410, 1998. 152. von Heijne, G., Signal sequences. The limits of variation, J. Mol. Biol., 184, 99, 1985. 153. von Heijne, G., How signal sequences maintain cleavage specific, J. Mol. Biol., 173, 243, 1984. 154. Jain, R.G., Rusch, S.L., and Kendall, D.A., Signal peptide cleavage regions. Functional limits on length and topological implications, J. Biol. Chem., 269, 16305, 1994. 155. Simonen, M. and Palva, I., Protein secretion in Bacillus species, Microbiol. Rev., 57, 109, 1993. 156. Nagarajan, V., Protein secretion, in Bacillus subtilis and Other Gram-Positive Bacteria: Biochemistry, Physiology, and Molecular Genetics, Sonenshein, A.L., Hoch, J.A., and Losick, R., Eds., American Soc. Microbiol., 713, 1993. 157. Nakai, K., Refinement of the prediction methods of signal peptides for the genome analyses of Saccharomyces cerevisiae and Bacillus subtilis, in Genome Informatics 1996, Universal Academy Press, Inc., Tokyo, Japan, 1996, 72. 158. Tjalsma, H. et al., Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome, Microbiol. Mol. Biol. Rev., 64, 515, 2000. 159. Karel, H.M. et al., Translocation of proteins across the cell envelope of Gram-positive bacteria, FEMS Microbiol. Rev., 25, 437, 2001. 160. Cao, G. and Dalbey, R.E., Translocation of N-terminal tails across the plasma membrane, EMBO J., 13, 4662, 1994. 161. Dalbey, R.E., Kuhn, A., and von Heijne, G, Directionality in protein translocation across membranes: the N-tail phenomenon, Trends Cell Biol., 5, 380, 1995. 162. Monné, M. et al., N-tail translocation in a eukaryotic polytopic membrane protein. Synergy between neighboring transmembrane segments, Eur. J. Biochem., 263, 264, 1999. 163. Nilsson, I. et al., Distant downstream sequence determinants can control N-tail translocation during protein insertion into the endoplasmic reticulum membrane, J. Biol. Chem., 275, 6207, 2000. 164. McMurry, J.L. and Kendall, D.A., An artificial transmembrane segment directs SecA, SecB, and electrochemical potential-dependent translocation of a long amino-terminal tail, J. Biol. Chem., 274, 6776, 1999. 165. Ouzzine, M. et al., An internal signal sequence mediates the targeting and retention of the human UDP-glucuronosyltransferase 1A6 to the endoplasmic reticulum, J. Biol. Chem., 274, 31401, 1999. 166. Hölscher, C., Bach, U.C., and Dobberstein, B., Prion protein contains a second endoplasmic reticulum targeting sequence located at its C terminus, J. Biol. Chem., 276, 13388, 2001. 167. Bhagwat, S.V. et al., Dual targeting property of the N-terminal signal sequence of P450A1. Targeting of heterologous proteins to endoplasmic reticulum and mitochondria, J. Biol. Chem., 274, 24014, 1999. 168. Paetzel, M., Dalbey, R.E., and Strynadka, N.C., The structure and mechanism of bacterial type I signal peptidases. A novel antibiotic target, Pharmacol. Ther., 87, 27, 2000. 169. Dalbey, R.E. et al., The chemistry and enzymology of the type I signal peptidases, Protein Sci., 6, 1129, 1997. 170. Tjalsma, H. et al., Functional analysis of the secretory precursor processing machinery of Bacillus subtilis: identification of a eubacterial homolog of archaeal and eukaryotic signal peptidases, Genes Dev., 12, 2318, 1998.
322 Cell-Penetrating Peptides: Processes and Applications 171. van Roosmalen, M.L. et al., Distinction between major and minor Bacillus signal peptidases based on phylogenetic and structural criteria, J. Biol. Chem., 276, 25230, 2001. 172. Howe, C.J. and Wallace, T.P., Prediction of leader peptide cleavage sites for polypeptides of the thylakoid lumen, Nucl. Acids Res., 18, 3417. 1990. 173. Nielsen, H. et al., Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites, Protein Eng., 10, 1, 1997. 174. Sakaguchi, M. et al., Functions of signal and signal-anchor sequences are determined by the balance between the hydrophobic segment, Prot. Natl Acad. Sci. U.S.A., 89, 16, 1992. 175. Nilsson, I., Whitley, P., and von Heijne, G., The COOH-terminal ends of internal signal and signal-anchor sequences are positioned differently in the ER translocase, J. Cell Biol., 126, 1127, 1994. 176. Paetzel, M., Dalbey, R.E., and Strynadka, N.C., Crystal structure of a bacterial signal peptidase in complex with a β-lactam inhibitor, Nature, 396, 186, 1998. 177. von Heijne, G., Life and death of a signal peptide, Nature, 396, 111, 1998. 178. Carlos, J.L. et al., The role of the membrane-spanning domain of type I signal peptidases in substrate cleavage site selection, J. Biol. Chem., 275, 38813, 2000. 179. Roy, P. et al., Transformation of the signal peptide/membrane anchor domain of a type II transmembrane protein into a cleavable signal peptide, J. Biol. Chem., 268, 2699, 1993. 180. Rehm, A. et al., Signal peptide cleavage of a type I membrane protein, HCMV US11, is dependent on its membrane anchor, EMBO J., 20, 1573, 2001. 181. Klein, P., Somorjai, R.L., and Lau, P.C.K., Distinctive properties of signal sequences from bacterial lipoproteins, Protein Eng., 2, 15, 1988. 182. von Heijne, G., The structure of signal peptides from bacterial lipoproteins, Protein Eng., 2, 531, 1989. 183. Tjalsma, H. et al., The role of lipoprotein processing by signal peptidase II in the Gram-positive eubacterium Bacillus subtilis, J. Biol. Chem., 274, 1698, 1999. 184. Strom, M.S., Nunn, D.N., and Lory, S., Posttranslational processing of type IV prepilin and homologs by PilD of Pseudomonas aeruginosa, Methods Enzymol., 235, 527, 1994. 185. Lory, S. and Strom, M.S., Structure-function relationship of type-IV prepilin peptidase of Pseudomonas aeruginosa — a review, Gene, 192, 117, 1997. 186. Fernandez, L.A. and Berenguer, J., Secretion and assembly of regular surface structures in Gram-negative bacteria, FEMS Microbiol. Rev., 24, 21, 2000. 187. Nunn, D., Bacterial type II protein export and pilus biogenesis: more than just homologies? Trends Cell Biol., 9, 402, 1999. 188. Nakai, K., Protein sorting signals and prediction of subcellular localization, Adv. Protein Chem., 54, 277, 2000. 189. Sjöström, M. et al., Signal peptide amino acid sequences in Eschericha coli contain information related to final protein localization. A multivariate data analysis, EMBO J., 6, 823, 1987. 190. Edman, M. et al., Different sequence patterns in signal peptides from Mycoplasmas, other Gram-positive bacteria, and Escherichia coli: a multivariate data analysis, Proteins, Struct. Funct. Genet., 35, 195, 1999. 191. Tommassen, J., van Tol, H., and Lugtenberg, B., The ultimate localization of an outer membrane protein of Escherichia coli K-12 is not determined by the signal sequence, EMBO J., 2, 1275, 1983.
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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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Model Amphipathic Peptides 85 relat
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Model Amphipathic Peptides 87 A cat
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Model Amphipathic Peptides 89 At th
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Model Amphipathic Peptides 91 16. H
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Signal Sequence-Based Cell-Penetrat
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Signal Sequence-Based Cell-Penetrat
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Signal Sequence-Based Cell-Penetrat
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Signal Sequence-Based Cell-Penetrat
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Signal Sequence-Based Cell-Penetrat
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Signal Sequence-Based Cell-Penetrat
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Signal Sequence-Based Cell-Penetrat
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Signal Sequence-Based Cell-Penetrat
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Signal Sequence-Based Cell-Penetrat
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Signal Sequence-Based Cell-Penetrat
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116 Cell-Penetrating Peptides: Proc
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124 Cell-Penetrating Peptides: Proc
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Interactions of Cell-Penetrating Pe
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Interactions of Cell-Penetrating Pe
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Interactions of Cell-Penetrating Pe
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Interactions of Cell-Penetrating Pe
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Interactions of Cell-Penetrating Pe
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Interactions of Cell-Penetrating Pe
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Interactions of Cell-Penetrating Pe
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Interactions of Cell-Penetrating Pe
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Interactions of Cell-Penetrating Pe
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Interactions of Cell-Penetrating Pe
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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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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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Toxicity and Side Effects of Cell-P
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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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Toxicity and Side Effects of Cell-P
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Toxicity and Side Effects of Cell-P
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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