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Volumn 7, Issue 3, 2012, Pages 387-396

Screening of cell-penetrating peptides using mRNA display

Author keywords

Cell penetrating peptide; MRNA display; Peptide screening

Indexed keywords

CELL LINES; CELL PENETRATION; CELL-PENETRATING PEPTIDE; CELLULAR UPTAKE; HEK-293; HELA CELL; HUMAN EMBRYONIC KIDNEYS; IN-VITRO; IN-VIVO; MRNA-DISPLAY; PEPTIDE SCREENING; POLYARGININE; SCREENING METHODS; TARGET CELLS;

EID: 84863237869     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.201100220     Document Type: Article
Times cited : (13)

References (27)
  • 1
    • 0024262589 scopus 로고
    • Cellular uptake of the tat protein from human immunodeficiency virus.
    • Frankel, A. D., Pabo, C. O., Cellular uptake of the tat protein from human immunodeficiency virus. Cell 1988, 55, 1189-1193.
    • (1988) Cell , vol.55 , pp. 1189-1193
    • Frankel, A.D.1    Pabo, C.O.2
  • 2
    • 0024209811 scopus 로고
    • Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein.
    • Green, M., Loewenstein, P. M., Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein. Cell 1988, 55, 1179-1188.
    • (1988) Cell , vol.55 , pp. 1179-1188
    • Green, M.1    Loewenstein, P.M.2
  • 3
    • 25444484384 scopus 로고    scopus 로고
    • Protamine as an efficient membrane-translocating peptide.
    • Reynolds, F., Weissleder, R., Josephson, L., Protamine as an efficient membrane-translocating peptide. Bioconjug. Chem. 2005, 16, 1240-1245.
    • (2005) Bioconjug. Chem. , vol.16 , pp. 1240-1245
    • Reynolds, F.1    Weissleder, R.2    Josephson, L.3
  • 4
    • 33646710386 scopus 로고    scopus 로고
    • Cell penetration properties of maurocalcine, a natural venom peptide active on the intracellular ryanodine receptor.
    • Boisseau, S., Mabrouk, K., Ram, N., Garmy, N. et al., Cell penetration properties of maurocalcine, a natural venom peptide active on the intracellular ryanodine receptor. Biochim. Biophys. Acta 2006, 1758, 308-319.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 308-319
    • Boisseau, S.1    Mabrouk, K.2    Ram, N.3    Garmy, N.4
  • 6
    • 34548771163 scopus 로고    scopus 로고
    • A novel cell-penetrating peptide, M918, for efficient delivery of proteins and peptide nucleic acids.
    • Andaloussi, S., Johansson, H. J., Holm, T., Langel, U., A novel cell-penetrating peptide, M918, for efficient delivery of proteins and peptide nucleic acids. Mol. Ther. 2005, 15, 1820-1826.
    • (2005) Mol. Ther. , vol.15 , pp. 1820-1826
    • Andaloussi, S.1    Johansson, H.J.2    Holm, T.3    Langel, U.4
  • 8
    • 45749120326 scopus 로고    scopus 로고
    • Cell-penetrating peptides as delivery vehicles for biology and medicine.
    • Stewart, K. M., Horton, K. L., Kelley, S. O., Cell-penetrating peptides as delivery vehicles for biology and medicine. Org. Biomol. Chem. 2008, 6, 2242-2255.
    • (2008) Org. Biomol. Chem. , vol.6 , pp. 2242-2255
    • Stewart, K.M.1    Horton, K.L.2    Kelley, S.O.3
  • 9
    • 34548183128 scopus 로고    scopus 로고
    • Assessing the delivery efficacy and internalization route of cell-penetrating peptides.
    • Andaloussi, S. E., Guterstam, P., Langel, U., Assessing the delivery efficacy and internalization route of cell-penetrating peptides. Nat. Protoc. 2007, 2, 2043-2047.
    • (2007) Nat. Protoc. , vol.2 , pp. 2043-2047
    • Andaloussi, S.E.1    Guterstam, P.2    Langel, U.3
  • 10
    • 27644561216 scopus 로고    scopus 로고
    • Characterization of cell-penetrating peptide-mediated peptide delivery.
    • Jones, S. W., Christison, R., Bundell, K., Voyce, C. J. et al., Characterization of cell-penetrating peptide-mediated peptide delivery. Br. J. Pharmacol. 2005, 145, 1093-1102.
    • (2005) Br. J. Pharmacol. , vol.145 , pp. 1093-1102
    • Jones, S.W.1    Christison, R.2    Bundell, K.3    Voyce, C.J.4
  • 11
    • 0036976219 scopus 로고    scopus 로고
    • A cell-penetrating peptide from a novel pVII-pIX phage-displayed random peptide library.
    • Gao, C., Mao, S., Ditzel, H. J., Farnases, L. et al., A cell-penetrating peptide from a novel pVII-pIX phage-displayed random peptide library. Bioorg. Med. Chem. 2002, 10, 4057-4065.
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 4057-4065
    • Gao, C.1    Mao, S.2    Ditzel, H.J.3    Farnases, L.4
  • 12
    • 33645737723 scopus 로고    scopus 로고
    • Transdermal protein delivery by a coadministered peptide identified via phage display.
    • Chen, Y., Shen, Y., Guo, X., Zhang, C. et al., Transdermal protein delivery by a coadministered peptide identified via phage display. Nat. Biotechnol. 2006, 24, 455-460.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 455-460
    • Chen, Y.1    Shen, Y.2    Guo, X.3    Zhang, C.4
  • 13
    • 33846991262 scopus 로고    scopus 로고
    • Creation of novel cell-penetrating peptides for intracellular drug delivery using systematic phage display technology originated from Tat transduction domain.
    • Kamada, H., Okamoto, T., Kawamura, M., Shibata, H. et al., Creation of novel cell-penetrating peptides for intracellular drug delivery using systematic phage display technology originated from Tat transduction domain. Biol. Pharm. Bull. 2007, 30, 218-223.
    • (2007) Biol. Pharm. Bull. , vol.30 , pp. 218-223
    • Kamada, H.1    Okamoto, T.2    Kawamura, M.3    Shibata, H.4
  • 14
    • 0030817279 scopus 로고    scopus 로고
    • RNA-peptide fusions for the in vitro selection of peptides and proteins.
    • Roberts, R. W., Szostak, J. W., RNA-peptide fusions for the in vitro selection of peptides and proteins. Proc. Natl. Acad. Sci. USA 1997, 94, 12297-12302.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12297-12302
    • Roberts, R.W.1    Szostak, J.W.2
  • 15
    • 0033643217 scopus 로고    scopus 로고
    • Optimized synthesis of RNA-protein fusions for in vitro protein selection.
    • Liu, R., Barrick, J. E., Szostak, J. W., Roberts, R. W., Optimized synthesis of RNA-protein fusions for in vitro protein selection. Methods Enzymol. 2000, 318, 268-293.
    • (2000) Methods Enzymol. , vol.318 , pp. 268-293
    • Liu, R.1    Barrick, J.E.2    Szostak, J.W.3    Roberts, R.W.4
  • 16
    • 0036298282 scopus 로고    scopus 로고
    • Conjugates of antisense oligonucleotides with the Tat and antennapedia cell-penetrating peptides: effects on cellular uptake, binding to target sequences, and biologic actions.
    • Astriab-Fisher, A., Sergueev, D., Fisher, M., Shaw, B. R. et al., Conjugates of antisense oligonucleotides with the Tat and antennapedia cell-penetrating peptides: effects on cellular uptake, binding to target sequences, and biologic actions. Pharm. Res. 2002, 19, 744-754.
    • (2002) Pharm. Res. , vol.19 , pp. 744-754
    • Astriab-Fisher, A.1    Sergueev, D.2    Fisher, M.3    Shaw, B.R.4
  • 17
    • 0028873081 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides.
    • Muñoz, V., Serrano, L., Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides. J. Mol. Biol. 1994, 245, 275-296.
    • (1994) J. Mol. Biol. , vol.245 , pp. 275-296
    • Muñoz, V.1    Serrano, L.2
  • 18
    • 34548684339 scopus 로고    scopus 로고
    • PEPstr: A de novo method for tertiary structure prediction of small bioactive peptides.
    • Kaur, H., Garg, A., Raghava, G. P. S., PEPstr: A de novo method for tertiary structure prediction of small bioactive peptides. Protein Pept. Lett. 2007, 14, 626-631.
    • (2007) Protein Pept. Lett. , vol.14 , pp. 626-631
    • Kaur, H.1    Garg, A.2    Raghava, G.P.S.3
  • 19
    • 13444263477 scopus 로고    scopus 로고
    • Mammalian transglutaminases. Identification of substrates as a key to physiological function and physiopathological relevance.
    • Esposito, C., Caputo, I., Mammalian transglutaminases. Identification of substrates as a key to physiological function and physiopathological relevance. FEBS J. 2005, 272, 615-631.
    • (2005) FEBS J. , vol.272 , pp. 615-631
    • Esposito, C.1    Caputo, I.2
  • 20
    • 70350040736 scopus 로고    scopus 로고
    • Cell penetrating peptides: How do they do it?
    • Herce, H. D., Garcia, A. E., Cell penetrating peptides: How do they do it? J. Biol. Phys. 2007, 33, 345-356.
    • (2007) J. Biol. Phys. , vol.33 , pp. 345-356
    • Herce, H.D.1    Garcia, A.E.2
  • 21
    • 25144449123 scopus 로고    scopus 로고
    • Internalization of bacterial redox protein azurin in mammalian cells: Entry domain and specificity.
    • Yamada, T., Fialho, A. M., Punj, V., Bratescu, L. et al., Internalization of bacterial redox protein azurin in mammalian cells: Entry domain and specificity. Cell Microbiol. 2005, 7, 1418-1431.
    • (2005) Cell Microbiol. , vol.7 , pp. 1418-1431
    • Yamada, T.1    Fialho, A.M.2    Punj, V.3    Bratescu, L.4
  • 22
    • 58349113855 scopus 로고    scopus 로고
    • Noncationic peptides obtained from azurin preferentially enter cancer cells.
    • Taylor, B. N., Mehta, R. R., Yamada, T., Lekmine, F. et al., Noncationic peptides obtained from azurin preferentially enter cancer cells. Cancer Res. 2009, 69, 537-546.
    • (2009) Cancer Res. , vol.69 , pp. 537-546
    • Taylor, B.N.1    Mehta, R.R.2    Yamada, T.3    Lekmine, F.4
  • 23
    • 70549109798 scopus 로고    scopus 로고
    • Isolation of novel cell-penetrating peptides from a random peptide library using in vitro virus and their modifications.
    • Kamide, K., Nakakubo, H., Uno, S., Fukamizu, A., Isolation of novel cell-penetrating peptides from a random peptide library using in vitro virus and their modifications. Int. J. Mol. Med. 2010, 25, 41-51.
    • (2010) Int. J. Mol. Med. , vol.25 , pp. 41-51
    • Kamide, K.1    Nakakubo, H.2    Uno, S.3    Fukamizu, A.4
  • 24
    • 38049156027 scopus 로고    scopus 로고
    • Molecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranes.
    • Herce, H. D., Garcia, A. E., Molecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranes. Proc. Natl. Acad. Sci. USA 2007, 104, 20805-20810.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 20805-20810
    • Herce, H.D.1    Garcia, A.E.2
  • 25
    • 67149093390 scopus 로고    scopus 로고
    • Efficient siRNA delivery into primary cells by a peptide transduction domain-dsRNA binding domain fusion protein.
    • Eguchi, A., Meade, B. R., Chang, Y-C., Fredrickson, C. T. et al., Efficient siRNA delivery into primary cells by a peptide transduction domain-dsRNA binding domain fusion protein. Nat. Biotechnol. 2009, 27, 567-571.
    • (2009) Nat. Biotechnol. , vol.27 , pp. 567-571
    • Eguchi, A.1    Meade, B.R.2    Chang, Y.-C.3    Fredrickson, C.T.4
  • 26
    • 0042199010 scopus 로고    scopus 로고
    • Cell surface adherence and endocytosis of protein transduction domains.
    • Lundberg, M., Wikstrom, S., Johansson, M., Cell surface adherence and endocytosis of protein transduction domains. Mol. Ther. 2003, 8, 143-150.
    • (2003) Mol. Ther. , vol.8 , pp. 143-150
    • Lundberg, M.1    Wikstrom, S.2    Johansson, M.3
  • 27
    • 77952901022 scopus 로고    scopus 로고
    • Coadministration of a tumor-penetrating peptide enhances the efficacy of cancer drugs.
    • Sugahara, K. N., Teesalu, T., Karmali, P. P., Kotamraju, V. R. et al., Coadministration of a tumor-penetrating peptide enhances the efficacy of cancer drugs. Science 2010, 328, 1031-1035.
    • (2010) Science , vol.328 , pp. 1031-1035
    • Sugahara, K.N.1    Teesalu, T.2    Karmali, P.P.3    Kotamraju, V.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.