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Volumn 1808, Issue 7, 2011, Pages 1860-1867

Binding of cell-penetrating penetratin peptides to plasma membrane vesicles correlates directly with cellular uptake

Author keywords

Arginine; Cell penetrating peptide; Lysine; Membrane affinity; Penetratin; Plasma membrane vesicles

Indexed keywords

ARGININE; HEPARIN; LYSINE; PENETRATIN; PROTEOGLYCAN;

EID: 79955814107     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2011.03.011     Document Type: Article
Times cited : (35)

References (65)
  • 2
    • 70349456654 scopus 로고    scopus 로고
    • Recent advances in the use of cell-penetrating peptides for medical and biological applications
    • S.B. Fonseca, M.P. Pereira, and S.O. Kelley Recent advances in the use of cell-penetrating peptides for medical and biological applications Adv. Drug Deliv. Rev. 61 2009 953 964
    • (2009) Adv. Drug Deliv. Rev. , vol.61 , pp. 953-964
    • Fonseca, S.B.1    Pereira, M.P.2    Kelley, S.O.3
  • 3
    • 0024262589 scopus 로고
    • Cellular uptake of the tat protein from human immunodeficiency virus
    • DOI 10.1016/0092-8674(88)90263-2
    • A.D. Frankel, and C.O. Pabo Cellular uptake of the tat protein from human immunodeficiency virus Cell 55 1988 1189 1193 (Pubitemid 19020071)
    • (1988) Cell , vol.55 , Issue.6 , pp. 1189-1193
    • Frankel, A.D.1    Pabo, C.O.2
  • 4
    • 0024209811 scopus 로고
    • Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein
    • DOI 10.1016/0092-8674(88)90262-0
    • M. Green, and P.M. Loewenstein Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein Cell 55 1988 1179 1188 (Pubitemid 19020070)
    • (1988) Cell , vol.55 , Issue.6 , pp. 1179-1188
    • Green, M.1    Loewenstein, P.M.2
  • 6
    • 0034613057 scopus 로고    scopus 로고
    • The antennapedia peptide penetratin translocates across lipid bilayers-the first direct observation
    • P.E. Thorén, D. Persson, M. Karlsson, and B. Nordén The antennapedia peptide penetratin translocates across lipid bilayers-the first direct observation FEBS Lett. 482 2000 265 268
    • (2000) FEBS Lett. , vol.482 , pp. 265-268
    • Thorén, P.E.1    Persson, D.2    Karlsson, M.3    Nordén, B.4
  • 8
    • 25844466684 scopus 로고    scopus 로고
    • A critical reassessment of penetratin translocation across lipid membranes
    • DOI 10.1529/biophysj.105.067694
    • E. Barany-Wallje, S. Keller, S. Serowy, S. Geibel, P. Pohl, M. Bienert, and M. Dathe A critical reassessment of penetratin translocation across lipid membranes Biophys. J. 89 2005 2513 2521 (Pubitemid 41401039)
    • (2005) Biophysical Journal , vol.89 , Issue.4 , pp. 2513-2521
    • Barany-Wallje, E.1    Keller, S.2    Serowy, S.3    Geibel, S.4    Pohl, P.5    Bienert, M.6    Dathe, M.7
  • 9
    • 1642304434 scopus 로고    scopus 로고
    • Membrane Binding and Translocation of Cell-Penetrating Peptides
    • DOI 10.1021/bi0360049
    • P.E. Thorén, D. Persson, E.K. Esbjörner, M. Goksör, P. Lincoln, and B. Nordén Membrane binding and translocation of cell-penetrating peptides Biochemistry 43 2004 3471 3489 (Pubitemid 38391703)
    • (2004) Biochemistry , vol.43 , Issue.12 , pp. 3471-3489
    • Thoren, P.E.G.1    Persson, D.2    Esbjorner, E.K.3    Goksor, M.4    Lincoln, P.5    Norden, B.6
  • 10
    • 33746853554 scopus 로고    scopus 로고
    • Real-time transmembrane translocation of penetratin driven by light-generated proton pumping
    • J. Björklund, H. Biverståhl, A. Gräslund, L. Mäler, and P. Brzezinski Real-time transmembrane translocation of penetratin driven by light-generated proton pumping Biophys. J. 91 2006 L29 L31
    • (2006) Biophys. J. , vol.91
    • Björklund, J.1    Biverståhl, H.2    Gräslund, A.3    Mäler, L.4    Brzezinski, P.5
  • 11
    • 0345275894 scopus 로고    scopus 로고
    • Penetratin and Related Cell-Penetrating Cationic Peptides Can Translocate Across Lipid Bilayers in the Presence of a Transbilayer Potential
    • DOI 10.1021/bi035293y
    • D. Terrone, S.L. Sang, L. Roudaia, and J.R. Silvius Penetratin and related cell-penetrating cationic peptides can translocate across lipid bilayers in the presence of a transbilayer potential Biochemistry 42 2003 13787 13799 (Pubitemid 37466604)
    • (2003) Biochemistry , vol.42 , Issue.47 , pp. 13787-13799
    • Terrone, D.1    Sang, S.L.W.2    Roudaia, L.3    Silvius, J.R.4
  • 12
    • 34250835903 scopus 로고    scopus 로고
    • A comprehensive model for the cellular uptake of cationic cell-penetrating peptides
    • DOI 10.1111/j.1600-0854.2007.00572.x
    • F. Duchardt, M. Fotin-Mleczek, H. Schwarz, R. Fischer, and R. Brock A comprehensive model for the cellular uptake of cationic cell-penetrating peptides Traffic 8 2007 848 866 (Pubitemid 46971632)
    • (2007) Traffic , vol.8 , Issue.7 , pp. 848-866
    • Duchardt, F.1    Fotin-Mleczek, M.2    Schwarz, H.3    Fischer, R.4    Brock, R.5
  • 13
    • 0033794501 scopus 로고    scopus 로고
    • Polyarginine enters cells more efficiently than other polycationic homopolymers
    • D.J. Mitchell, D.T. Kim, L. Steinman, C.G. Fathman, and J.B. Rothbard Polyarginine enters cells more efficiently than other polycationic homopolymers J. Pept. Res. 56 2000 318 325
    • (2000) J. Pept. Res. , vol.56 , pp. 318-325
    • Mitchell, D.J.1    Kim, D.T.2    Steinman, L.3    Fathman, C.G.4    Rothbard, J.B.5
  • 15
    • 27744528180 scopus 로고    scopus 로고
    • Endocytosis and cationic cell-penetrating peptides - A merger of concepts and methods
    • DOI 10.2174/138161205774580778
    • M. Fotin-Mleczek, R. Fischer, and R. Brock Endocytosis and cationic cell-penetrating peptides-a merger of concepts and methods Curr. Pharm. Des. 11 2005 3613 3628 (Pubitemid 41630988)
    • (2005) Current Pharmaceutical Design , vol.11 , Issue.28 , pp. 3613-3628
    • Fotin-Mleczek, M.1    Fischer, R.2    Brock, R.3
  • 17
    • 56049093057 scopus 로고    scopus 로고
    • Cell-penetrating and cell-targeting peptides in drug delivery
    • E. Vives, J. Schmidt, and A. Pelegrin Cell-penetrating and cell-targeting peptides in drug delivery Biochim. Biophys. Acta 1786 2008 126 138
    • (2008) Biochim. Biophys. Acta , vol.1786 , pp. 126-138
    • Vives, E.1    Schmidt, J.2    Pelegrin, A.3
  • 18
    • 33645640345 scopus 로고    scopus 로고
    • High density of octaarginine stimulates macropinocytosis leading to efficient intracellular trafficking for gene expression
    • DOI 10.1074/jbc.M503202200
    • I.A. Khalil, K. Kogure, S. Futaki, and H. Harashima High density of octaarginine stimulates macropinocytosis leading to efficient intracellular trafficking for gene expression J. Biol. Chem. 281 2006 3544 3551 (Pubitemid 43845971)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.6 , pp. 3544-3551
    • Khalil, I.A.1    Kogure, K.2    Futaki, S.3    Harashima, H.4
  • 19
    • 2342595835 scopus 로고    scopus 로고
    • Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis
    • DOI 10.1038/nm996
    • J.S. Wadia, R.V. Stan, and S.F. Dowdy Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis Nat. Med. 10 2004 310 315 (Pubitemid 38667624)
    • (2004) Nature Medicine , vol.10 , Issue.3 , pp. 310-315
    • Wadia, J.S.1    Stan, R.V.2    Dowdy, S.F.3
  • 20
    • 11844268027 scopus 로고    scopus 로고
    • Cationic TAT peptide transduction domain enters cells by macropinocytosis
    • DOI 10.1016/j.jconrel.2004.10.018, PII S0168365904004766
    • I.M. Kaplan, J.S. Wadia, and S.F. Dowdy Cationic TAT peptide transduction domain enters cells by macropinocytosis J. Control. Release 102 2005 247 253 (Pubitemid 40093789)
    • (2005) Journal of Controlled Release , vol.102 , Issue.1 , pp. 247-253
    • Kaplan, I.M.1    Wadia, J.S.2    Dowdy, S.F.3
  • 22
    • 0029982569 scopus 로고    scopus 로고
    • Cell internalization of the third helix of the antennapedia homeodomain is receptor-independent
    • DOI 10.1074/jbc.271.30.18188
    • D. Derossi, S. Calvet, A. Trembleau, A. Brunissen, G. Chassaing, and A. Prochiantz Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent J. Biol. Chem. 271 1996 18188 18193 (Pubitemid 26250811)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.30 , pp. 18188-18193
    • Derossi, D.1    Calvet, S.2    Trembleau, A.3    Brunissen, A.4    Chassaing, G.5    Prochiantz, A.6
  • 23
    • 0035937124 scopus 로고    scopus 로고
    • Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery
    • S. Futaki, T. Suzuki, W. Ohashi, T. Yagami, S. Tanaka, K. Ueda, and Y. Sugiura Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery J. Biol. Chem. 276 2001 5836 5840
    • (2001) J. Biol. Chem. , vol.276 , pp. 5836-5840
    • Futaki, S.1    Suzuki, T.2    Ohashi, W.3    Yagami, T.4    Tanaka, S.5    Ueda, K.6    Sugiura, Y.7
  • 24
    • 0041816277 scopus 로고    scopus 로고
    • Antennapedia and HIV transactivator of transcription (TAT) "protein transduction domains" promote endocytosis of high molecular weight cargo upon binding to cell surface glycosaminoglycans
    • DOI 10.1074/jbc.M301726200
    • S. Console, C. Marty, C. Garcia-Echeverria, R. Schwendener, and K. Ballmer-Hofer Antennapedia and HIV transactivator of transcription (TAT) "protein transduction domains" promote endocytosis of high molecular weight cargo upon binding to cell surface glycosaminoglycans J. Biol. Chem. 278 2003 35109 35114 (Pubitemid 37102274)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.37 , pp. 35109-35114
    • Console, S.1    Marty, C.2    Garcia-Echeverria, C.3    Schwendener, R.4    Ballmer-Hofer, K.5
  • 25
    • 33846223900 scopus 로고    scopus 로고
    • Interaction of arginine-rich peptides with membrane-associated proteoglycans is crucial for induction of actin organization and macropinocytosis
    • DOI 10.1021/bi0612824
    • I. Nakase, A. Tadokoro, N. Kawabata, T. Takeuchi, H. Katoh, K. Hiramoto, M. Negishi, M. Nomizu, Y. Sugiura, and S. Futaki Interaction of arginine-rich peptides with membrane-associated proteoglycans is crucial for induction of actin organization and macropinocytosis Biochemistry 46 2007 492 501 (Pubitemid 46105438)
    • (2007) Biochemistry , vol.46 , Issue.2 , pp. 492-501
    • Nakase, I.1    Tadokoro, A.2    Kawabata, N.3    Takeuchi, T.4    Katoh, H.5    Hiramoto, K.6    Negishi, M.7    Nomizu, M.8    Sugiura, Y.9    Futaki, S.10
  • 26
    • 17644386231 scopus 로고    scopus 로고
    • Cellular uptake of unconjugated TAT peptide involves clathrin-dependent endocytosis and heparan sulfate receptors
    • DOI 10.1074/jbc.M401604200
    • J.P. Richard, K. Melikov, H. Brooks, P. Prevot, B. Lebleu, and L.V. Chernomordik Cellular uptake of unconjugated TAT peptide involves clathrin-dependent endocytosis and heparan sulfate receptors J. Biol. Chem. 280 2005 15300 15306 (Pubitemid 40562886)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.15 , pp. 15300-15306
    • Richard, J.P.1    Melikov, K.2    Brooks, H.3    Prevot, P.4    Lebleu, B.5    Chernomordik, L.V.6
  • 27
    • 0035793619 scopus 로고    scopus 로고
    • Internalization of HIV-1 tat requires cell surface heparan sulfate proteoglycans
    • M. Tyagi, M. Rusnati, M. Presta, and M. Giacca Internalization of HIV-1 tat requires cell surface heparan sulfate proteoglycans J. Biol. Chem. 276 2001 3254 3261
    • (2001) J. Biol. Chem. , vol.276 , pp. 3254-3261
    • Tyagi, M.1    Rusnati, M.2    Presta, M.3    Giacca, M.4
  • 28
    • 0037333830 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycan as a plasma membrane carrier
    • DOI 10.1016/S0968-0004(03)00031-8
    • M. Belting Heparan sulfate proteoglycan as a plasma membrane carrier Trends Biochem. Sci. 28 2003 145 151 (Pubitemid 36293852)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.3 , pp. 145-151
    • Belting, M.1
  • 29
    • 34548162679 scopus 로고    scopus 로고
    • Cell-surface proteoglycans as molecular portals for cationic peptide and polymer entry into cells
    • G.M. Poon, and J. Gariepy Cell-surface proteoglycans as molecular portals for cationic peptide and polymer entry into cells Biochem. Soc. Trans. 35 2007 788 793 (Pubitemid 47310369)
    • (2007) Biochemical Society Transactions , vol.35 , Issue.4 , pp. 788-793
    • Poon, G.M.K.1    Gariepy, J.2
  • 31
    • 70450225343 scopus 로고    scopus 로고
    • ScFv antibody-induced translocation of cell-surface heparan sulfate proteoglycan to endocytic vesicles: Evidence for heparan sulfate epitope specificity and role of both syndecan and glypican
    • A. Wittrup, S.H. Zhang, G.B. ten Dam, T.H. van Kuppevelt, P. Bengtson, M. Johansson, J. Welch, M. Morgelin, and M. Belting ScFv antibody-induced translocation of cell-surface heparan sulfate proteoglycan to endocytic vesicles: evidence for heparan sulfate epitope specificity and role of both syndecan and glypican J. Biol. Chem. 284 2009 32959 32967
    • (2009) J. Biol. Chem. , vol.284 , pp. 32959-32967
    • Wittrup, A.1    Zhang, S.H.2    Ten Dam, G.B.3    Van Kuppevelt, T.H.4    Bengtson, P.5    Johansson, M.6    Welch, J.7    Morgelin, M.8    Belting, M.9
  • 32
    • 3543051871 scopus 로고    scopus 로고
    • Role of membrane potential and hydrogen bonding in the mechanism of translocation of guanidinium-rich peptides into cells
    • DOI 10.1021/ja0482536
    • J.B. Rothbard, T.C. Jessop, R.S. Lewis, B.A. Murray, and P.A. Wender Role of membrane potential and hydrogen bonding in the mechanism of translocation of guanidinium-rich peptides into cells J. Am. Chem. Soc. 126 2004 9506 9507 (Pubitemid 39031015)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.31 , pp. 9506-9507
    • Rothbard, J.B.1    Jessop, T.C.2    Lewis, R.S.3    Murray, B.A.4    Wender, P.A.5
  • 33
    • 0344012169 scopus 로고    scopus 로고
    • Anion-Mediated Transfer of Polyarginine across Liquid and Bilayer Membranes
    • DOI 10.1021/ja037601l
    • N. Sakai, and S. Matile Anion-mediated transfer of polyarginine across liquid and bilayer membranes J. Am. Chem. Soc. 125 2003 14348 14356 (Pubitemid 37452373)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.47 , pp. 14348-14356
    • Sakai, N.1    Matile, S.2
  • 34
    • 12344275753 scopus 로고    scopus 로고
    • Direct observation of anion-mediated translocation of fluorescent oligoarginine carriers into and across bulk liquid and anionic bilayer membranes
    • DOI 10.1002/cbic.200400256
    • N. Sakai, T. Takeuchi, S. Futaki, and S. Matile Direct observation of anion-mediated translocation of fluorescent oligoarginine carriers into and across bulk liquid and anionic bilayer membranes Chembiochem 6 2005 114 122 (Pubitemid 40128644)
    • (2005) ChemBioChem , vol.6 , Issue.1 , pp. 114-122
    • Sakai, N.1    Takeuchi, T.2    Futaki, S.3    Matile, S.4
  • 36
    • 33745151952 scopus 로고    scopus 로고
    • Membrane interactions of cell-penetrating peptides probed by tryptophan fluorescence and dichroism techniques: Correlations of structure to cellular uptake
    • DOI 10.1021/bi052095t
    • C.E. Caesar, E.K. Esbjörner, P. Lincoln, and B. Nordén Membrane interactions of cell-penetrating peptides probed by tryptophan fluorescence and dichroism techniques: correlations of structure to cellular uptake Biochemistry 45 2006 7682 7692 (Pubitemid 43894958)
    • (2006) Biochemistry , vol.45 , Issue.24 , pp. 7682-7692
    • Caesar, C.E.B.1    Esbjorner, E.K.2    Lincoln, P.3    Norden, B.4
  • 37
    • 34249102563 scopus 로고    scopus 로고
    • Counterion-mediated membrane penetration: Cationic cell-penetrating peptides overcome Born energy barrier by ion-pairing with phospholipids
    • DOI 10.1016/j.bbamem.2007.03.004, PII S0005273607000764
    • E.K. Esbjörner, P. Lincoln, and B. Nordén Counterion-mediated membrane penetration: cationic cell-penetrating peptides overcome Born energy barrier by ion-pairing with phospholipids Biochim. Biophys. Acta 1768 2007 1550 1558 (Pubitemid 46782707)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.6 , pp. 1550-1558
    • Esbjorner, E.K.1    Lincoln, P.2    Norden, B.3
  • 38
    • 4644224822 scopus 로고    scopus 로고
    • Vesicle membrane interactions of penetratin analogues
    • DOI 10.1021/bi036054d
    • D. Persson, P.E. Thorén, P. Lincoln, and B. Nordén Vesicle membrane interactions of penetratin analogues Biochemistry 43 2004 11045 11055 (Pubitemid 39433693)
    • (2004) Biochemistry , vol.43 , Issue.34 , pp. 11045-11055
    • Persson, D.1    Thoren, P.E.G.2    Lincoln, P.3    Norden, B.4
  • 39
    • 17144373997 scopus 로고    scopus 로고
    • Membrane destabilizing properties of cell-penetrating peptides
    • DOI 10.1016/j.bpc.2004.11.016
    • P.E. Thorén, D. Persson, P. Lincoln, and B. Nordén Membrane destabilizing properties of cell-penetrating peptides Biophys. Chem. 114 2005 169 179 (Pubitemid 40521515)
    • (2005) Biophysical Chemistry , vol.114 , Issue.2-3 , pp. 169-179
    • Thoren, P.E.G.1    Persson, D.2    Lincoln, P.3    Norden, B.4
  • 40
    • 0028832566 scopus 로고
    • Differences in the interaction of heparin with arginine and lysine and the importance of these basic amino acids in the binding of heparin to acidic fibroblast growth factor
    • J.R. Fromm, R.E. Hileman, E.E. Caldwell, J.M. Weiler, and R.J. Linhardt Differences in the interaction of heparin with arginine and lysine and the importance of these basic amino acids in the binding of heparin to acidic fibroblast growth factor Arch. Biochem. Biophys. 323 1995 279 287
    • (1995) Arch. Biochem. Biophys. , vol.323 , pp. 279-287
    • Fromm, J.R.1    Hileman, R.E.2    Caldwell, E.E.3    Weiler, J.M.4    Linhardt, R.J.5
  • 41
    • 0017139396 scopus 로고
    • Plasma membrane vesiculation: A new technique for isolation of plasma membranes
    • R.E. Scott Plasma membrane vesiculation: a new technique for isolation of plasma membranes Science (New York, N.Y) 194 1976 743 745
    • (1976) Science (New York, N.Y) , vol.194 , pp. 743-745
    • Scott, R.E.1
  • 42
    • 0018331203 scopus 로고
    • Plasma membrane vesiculation in 3T3 and SV3T3 cells. II. Factors affecting the process of vesiculation
    • R.E. Scott, and P.B. Maercklein Plasma membrane vesiculation in 3T3 and SV3T3 cells. II. Factors affecting the process of vesiculation J. Cell Sci. 35 1979 245 252 (Pubitemid 9092083)
    • (1979) Journal of Cell Science , vol.35 , pp. 245-252
    • Scott, R.E.1    Maercklein, P.B.2
  • 43
    • 0018331202 scopus 로고
    • Plasma membrane vesiculation in 3T3 and SV3T3 cells. I. Morphological and biochemical characterization
    • R.E. Scott, R.G. Perkins, M.A. Zschunke, B.J. Hoerl, and P.B. Maercklein Plasma membrane vesiculation in 3T3 and SV3T3 cells. I. Morphological and biochemical characterization J. Cell Sci. 35 1979 229 243 (Pubitemid 9092082)
    • (1979) Journal of Cell Science , vol.35 , pp. 229-243
    • Scott, R.E.1    Perkins, R.G.2    Zschunke, M.A.3
  • 44
    • 70450173690 scopus 로고    scopus 로고
    • Cholesterol-dependent phase separation in cell-derived giant plasma-membrane vesicles
    • I. Levental, F.J. Byfield, P. Chowdhury, F. Gai, T. Baumgart, and P.A. Janmey Cholesterol-dependent phase separation in cell-derived giant plasma-membrane vesicles Biochem. J. 424 2009 163 167
    • (2009) Biochem. J. , vol.424 , pp. 163-167
    • Levental, I.1    Byfield, F.J.2    Chowdhury, P.3    Gai, F.4    Baumgart, T.5    Janmey, P.A.6
  • 47
    • 33751437206 scopus 로고    scopus 로고
    • Direct reconstitution of plasma membrane lipids and proteins in nanotube-vesicle networks
    • DOI 10.1021/la060828k
    • B. Bauer, M. Davidson, and O. Orwar Direct reconstitution of plasma membrane lipids and proteins in nanotube-vesicle networks Langmuir 22 2006 9329 9332 (Pubitemid 44818525)
    • (2006) Langmuir , vol.22 , Issue.22 , pp. 9329-9332
    • Bauer, B.1    Davidson, M.2    Orwar, O.3
  • 49
    • 0042232110 scopus 로고    scopus 로고
    • Studies on the internalization mechanism of cationic cell-penetrating peptides
    • DOI 10.1074/jbc.M303938200
    • G. Drin, S. Cottin, E. Blanc, A.R. Rees, and J. Temsamani Studies on the internalization mechanism of cationic cell-penetrating peptides J. Biol. Chem. 278 2003 31192 31201 (Pubitemid 36994635)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.33 , pp. 31192-31201
    • Drin, G.1    Cottin, S.2    Blanc, E.3    Rees, A.R.4    Temsamani, J.5
  • 50
    • 22144453931 scopus 로고    scopus 로고
    • Quantification of the cellular uptake of cell-penetrating peptides by MALDI-TOF mass spectrometry
    • DOI 10.1002/anie.200500477
    • F. Burlina, S. Sagan, G. Bolbach, and G. Chassaing Quantification of the cellular uptake of cell-penetrating peptides by MALDI-TOF mass spectrometry Angew. Chem. Int. Ed. Engl. 44 2005 4244 4247 (Pubitemid 40968506)
    • (2005) Angewandte Chemie - International Edition , vol.44 , Issue.27 , pp. 4244-4247
    • Burlina, F.1    Sagan, S.2    Bolbach, G.3    Chassaing, G.4
  • 52
    • 0037457905 scopus 로고    scopus 로고
    • Application of a novel analysis to measure the binding of the membrane-translocating peptide penetratin to negatively charged liposomes
    • DOI 10.1021/bi026453t
    • D. Persson, P.E. Thorén, M. Herner, P. Lincoln, and B. Nordén Application of a novel analysis to measure the binding of the membrane-translocating peptide penetratin to negatively charged liposomes Biochemistry 42 2003 421 429 (Pubitemid 36105760)
    • (2003) Biochemistry , vol.42 , Issue.2 , pp. 421-429
    • Persson, D.1    Thoren, P.E.G.2    Herner, M.3    Lincoln, P.4    Norden, B.5
  • 53
    • 0030176423 scopus 로고    scopus 로고
    • Imaging exocytosis and endocytosis
    • DOI 10.1016/S0959-4388(96)80121-8
    • W.J. Betz, F. Mao, and C.B. Smith Imaging exocytosis and endocytosis Curr. Opin. Neurobiol. 6 1996 365 371 (Pubitemid 26235686)
    • (1996) Current Opinion in Neurobiology , vol.6 , Issue.3 , pp. 365-371
    • Betz, W.J.1    Mao, F.2    Smith, C.B.3
  • 54
    • 27744493266 scopus 로고    scopus 로고
    • Modeling the endosomal escape of cell-penetrating peptides: Transmembrane pH gradient driven translocation across phospholipid bilayers
    • DOI 10.1021/bi051356w
    • M. Magzoub, A. Pramanik, and A. Graslund Modeling the endosomal escape of cell-penetrating peptides: transmembrane pH gradient driven translocation across phospholipid bilayers Biochemistry 44 2005 14890 14897 (Pubitemid 41612268)
    • (2005) Biochemistry , vol.44 , Issue.45 , pp. 14890-14897
    • Magzoub, M.1    Pramanik, A.2    Graslund, A.3
  • 55
    • 71749110589 scopus 로고    scopus 로고
    • Analysis of in vitro toxicity of five cell-penetrating peptides by metabolic profiling
    • K. Kilk, R. Mahlapuu, U. Soomets, and Ü. Langel Analysis of in vitro toxicity of five cell-penetrating peptides by metabolic profiling Toxicology 265 2009 87 95
    • (2009) Toxicology , vol.265 , pp. 87-95
    • Kilk, K.1    Mahlapuu, R.2    Soomets, U.3    Langel, Ü.4
  • 57
    • 14044270161 scopus 로고    scopus 로고
    • Binding of oligoarginine to membrane lipids and heparan sulfate: Structural and thermodynamic characterization of a cell-penetrating peptide
    • DOI 10.1021/bi048046i
    • E. Goncalves, E. Kitas, and J. Seelig Binding of oligoarginine to membrane lipids and heparan sulfate: structural and thermodynamic characterization of a cell-penetrating peptide Biochemistry 44 2005 2692 2702 (Pubitemid 40279574)
    • (2005) Biochemistry , vol.44 , Issue.7 , pp. 2692-2702
    • Goncalves, E.1    Kitas, E.2    Seelig, J.3
  • 59
    • 38949118666 scopus 로고    scopus 로고
    • DNA condensation by PAMAM dendrimers: Self-assembly characteristics and effect on transcription
    • DOI 10.1021/bi7017199
    • K. Fant, E.K. Esbjörner, P. Lincoln, and B. Nordén DNA condensation by PAMAM dendrimers: self-assembly characteristics and effect on transcription Biochemistry 47 2008 1732 1740 (Pubitemid 351231222)
    • (2008) Biochemistry , vol.47 , Issue.6 , pp. 1732-1740
    • Fant, K.1    Esbjorner, E.K.2    Lincoln, P.3    Norden, B.4
  • 61
    • 44049095595 scopus 로고    scopus 로고
    • Binding and clustering of glycosaminoglycans: A common property of mono- and multivalent cell-penetrating compounds
    • A. Ziegler, and J. Seelig Binding and clustering of glycosaminoglycans: a common property of mono- and multivalent cell-penetrating compounds Biophys. J. 94 2008 2142 2149
    • (2008) Biophys. J. , vol.94 , pp. 2142-2149
    • Ziegler, A.1    Seelig, J.2
  • 62
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • DOI 10.1038/nsb1096-842
    • W.C. Wimley, and S.H. White Experimentally determined hydrophobicity scale for proteins at membrane interfaces Nat. Struct. Biol. 3 1996 842 848 (Pubitemid 26330634)
    • (1996) Nature Structural Biology , vol.3 , Issue.10 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 63
    • 0037466075 scopus 로고    scopus 로고
    • Comparison of the interaction, positioning, structure induction and membrane perturbation of cell-penetrating peptides and non-translocating variants with phospholipid vesicles
    • DOI 10.1016/S0301-4622(02)00321-6, PII S0301462202003216
    • M. Magzoub, L.E. Eriksson, and A. Gräslund Comparison of the interaction, positioning, structure induction and membrane perturbation of cell-penetrating peptides and non-translocating variants with phospholipid vesicles Biophys. Chem. 103 2003 271 288 (Pubitemid 36506473)
    • (2003) Biophysical Chemistry , vol.103 , Issue.3 , pp. 271-288
    • Magzoub, M.1    Eriksson, L.E.G.2    Graslund, A.3
  • 64
    • 0028335262 scopus 로고
    • Phospholipid asymmetry in plasma membrane vesicles derived from BHK cells
    • DOI 10.1016/0005-2736(94)90146-5
    • J.L. Whatmore, and D. Allan Phospholipid asymmetry in plasma membrane vesicles derived from BHK cells Biochim. Biophys. Acta 1192 1994 88 94 (Pubitemid 24171545)
    • (1994) Biochimica et Biophysica Acta - Biomembranes , vol.1192 , Issue.1 , pp. 88-94
    • Whatmore, J.L.1    Allan, D.2
  • 65
    • 74049160383 scopus 로고    scopus 로고
    • Revised role of glycosaminoglycans in TAT protein transduction domain-mediated cellular transduction
    • J.M. Gump, R.K. June, and S.F. Dowdy Revised role of glycosaminoglycans in TAT protein transduction domain-mediated cellular transduction J. Biol. Chem. 285 2010 1500 1507
    • (2010) J. Biol. Chem. , vol.285 , pp. 1500-1507
    • Gump, J.M.1    June, R.K.2    Dowdy, S.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.