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Volumn 17, Issue 1, 2006, Pages 90-100

Intracellular traffic and fate of protein transduction domains HIV-1 TAT peptide and octaarginine. Implications for their utilization as drug delivery vectors

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOPHAGES; CELL CULTURE; CELL MEMBRANES; CONTROLLED DRUG DELIVERY; DISEASES; TARGETED DRUG DELIVERY;

EID: 31544479580     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc050274h     Document Type: Article
Times cited : (101)

References (59)
  • 1
    • 1542609485 scopus 로고    scopus 로고
    • Transduction peptides: From technology to physiology
    • Joliot, A., and Prochiantz, A. (2004) Transduction peptides: from technology to physiology. Nat. Cell Biol. 6, 189-96.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 189-196
    • Joliot, A.1    Prochiantz, A.2
  • 2
    • 1542721107 scopus 로고    scopus 로고
    • Cell penetrating peptides in drug delivery
    • Snyder, E. L., and Dowdy, S. F. (2004) Cell penetrating peptides in drug delivery. Pharm. Res. 21, 389-93.
    • (2004) Pharm. Res. , vol.21 , pp. 389-393
    • Snyder, E.L.1    Dowdy, S.F.2
  • 3
    • 23944483437 scopus 로고    scopus 로고
    • Cell-penetrating peptides: Tools for intracellular delivery of therapeutics
    • Deshayes, S., Morris, M. C., Divita, G., and Heitz, F. (2005) Cell-penetrating peptides: tools for intracellular delivery of therapeutics. Cell. Mol. Life Sci. 62, 1839-49.
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 1839-1849
    • Deshayes, S.1    Morris, M.C.2    Divita, G.3    Heitz, F.4
  • 4
    • 31544438701 scopus 로고    scopus 로고
    • Break on through to the Other Side-Biophysics and Cell Biology Shed Light on Cell-Penetrating Peptides
    • in press
    • Fischer, R., Fotin-Mleczek, M., Hufnagel, H., and Brock, R. (2005) Break on through to the Other Side-Biophysics and Cell Biology Shed Light on Cell-Penetrating Peptides. Chembiochem, in press.
    • (2005) Chembiochem
    • Fischer, R.1    Fotin-Mleczek, M.2    Hufnagel, H.3    Brock, R.4
  • 5
    • 3242811587 scopus 로고    scopus 로고
    • Protein transduction domains and their utility in gene therapy
    • Beerens, A. M., Al Hadithy, A. F., Rots, M. G., and Haisma, H. J. (2003) Protein transduction domains and their utility in gene therapy. Curr. Gene Ther. 3, 486-94.
    • (2003) Curr. Gene Ther. , vol.3 , pp. 486-494
    • Beerens, A.M.1    Al Hadithy, A.F.2    Rots, M.G.3    Haisma, H.J.4
  • 6
    • 0038048992 scopus 로고    scopus 로고
    • Modulation of cellular function by TAT mediated transduction of full length proteins
    • Wadia, J. S., and Dowdy, S. F. (2003) Modulation of cellular function by TAT mediated transduction of full length proteins. Curr. Protein Pept. Sci. 4, 97-104.
    • (2003) Curr. Protein Pept. Sci. , vol.4 , pp. 97-104
    • Wadia, J.S.1    Dowdy, S.F.2
  • 7
    • 13844256697 scopus 로고    scopus 로고
    • Transmembrane delivery of protein and peptide drugs by TAT-mediated transduction in the treatment of cancer
    • Wadia, J. S., and Dowdy, S. F. (2005) Transmembrane delivery of protein and peptide drugs by TAT-mediated transduction in the treatment of cancer. Adv. Drug Delivery Rev. 57, 579-96.
    • (2005) Adv. Drug Delivery Rev. , vol.57 , pp. 579-596
    • Wadia, J.S.1    Dowdy, S.F.2
  • 9
    • 20344401001 scopus 로고    scopus 로고
    • Application of novel solid lipid nanoparticle (SLN)-gene vector formulations based on a dimeric HIV-1 TAT-peptide in vitro and in vivo
    • Rudolph, C., Schillinger, U., Ortiz, A., Tabatt, K., Plank, C., Muller, R. H., and Rosenecker, J. (2004) Application of novel solid lipid nanoparticle (SLN)-gene vector formulations based on a dimeric HIV-1 TAT-peptide in vitro and in vivo. Pharm. Res. 21, 1662-9.
    • (2004) Pharm. Res. , vol.21 , pp. 1662-1669
    • Rudolph, C.1    Schillinger, U.2    Ortiz, A.3    Tabatt, K.4    Plank, C.5    Muller, R.H.6    Rosenecker, J.7
  • 12
    • 0042199010 scopus 로고    scopus 로고
    • Cell surface adherence and endocytosis of protein transduction domains
    • Lundberg, M., Wikstrom, S., and Johansson, M. (2003) Cell surface adherence and endocytosis of protein transduction domains. Mol. Ther. 8, 143-50.
    • (2003) Mol. Ther. , vol.8 , pp. 143-150
    • Lundberg, M.1    Wikstrom, S.2    Johansson, M.3
  • 13
    • 0042355293 scopus 로고    scopus 로고
    • Caveolae-mediated internalization of extracellular HIV-1 tat fusion proteins visualized in real time
    • Ferrari, A., Pellegrini, V., Arcangeli, C., Fittipaldi, A., Giacca, M., and Beltram, F. (2003) Caveolae-mediated internalization of extracellular HIV-1 tat fusion proteins visualized in real time. Mol. Ther. 8, 284-94.
    • (2003) Mol. Ther. , vol.8 , pp. 284-294
    • Ferrari, A.1    Pellegrini, V.2    Arcangeli, C.3    Fittipaldi, A.4    Giacca, M.5    Beltram, F.6
  • 14
    • 1842529513 scopus 로고    scopus 로고
    • A stepwise dissection of the intracellular fate of cationic cell-penetrating peptides
    • Fischer, R., Kohler, K., Fotin-Mleczek, M., and Brock, R. (2004) A stepwise dissection of the intracellular fate of cationic cell-penetrating peptides. J. Biol. Chem. 279, 12625-35.
    • (2004) J. Biol. Chem. , vol.279 , pp. 12625-12635
    • Fischer, R.1    Kohler, K.2    Fotin-Mleczek, M.3    Brock, R.4
  • 15
    • 2442660623 scopus 로고    scopus 로고
    • Cellular trajectories of Peptide-modified gold particle complexes: Comparison of nuclear localization signals and Peptide transduction domains
    • Tkachenko, A. G., Xie, H., Liu, Y., Coleman, D., Ryan, J., Glomm, W. R., Shipton, M. K., Franzen, S., and Feldheim, D. L. (2004) Cellular trajectories of Peptide-modified gold particle complexes: comparison of nuclear localization signals and Peptide transduction domains. Bioconjugate Chem. 15, 482-90.
    • (2004) Bioconjugate Chem. , vol.15 , pp. 482-490
    • Tkachenko, A.G.1    Xie, H.2    Liu, Y.3    Coleman, D.4    Ryan, J.5    Glomm, W.R.6    Shipton, M.K.7    Franzen, S.8    Feldheim, D.L.9
  • 16
    • 2342595835 scopus 로고    scopus 로고
    • Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis
    • Wadia, J. S., Stan, R. V., and Dowdy, S. F. (2004) Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis. Nat. Med. 10, 310-5.
    • (2004) Nat. Med. , vol.10 , pp. 310-315
    • Wadia, J.S.1    Stan, R.V.2    Dowdy, S.F.3
  • 17
    • 13844256698 scopus 로고    scopus 로고
    • Tat peptide-mediated cellular delivery: Back to basics
    • Brooks, H., Lebleu, B., and Vives, E. (2005) Tat peptide-mediated cellular delivery: back to basics. Adv. Drug Delivery Rev. 57, 559-77.
    • (2005) Adv. Drug Delivery Rev. , vol.57 , pp. 559-577
    • Brooks, H.1    Lebleu, B.2    Vives, E.3
  • 18
    • 0035210628 scopus 로고    scopus 로고
    • Cellular delivery of impermeable effector molecules in the form of conjugates with peptides capable of mediating membrane translocation
    • Fischer, P. M., Krausz, E., and Lane, D. P. (2001) Cellular delivery of impermeable effector molecules in the form of conjugates with peptides capable of mediating membrane translocation. Bioconjugate Chem. 12, 825-41.
    • (2001) Bioconjugate Chem. , vol.12 , pp. 825-841
    • Fischer, P.M.1    Krausz, E.2    Lane, D.P.3
  • 20
    • 2342507144 scopus 로고    scopus 로고
    • HIV-1 Tat enters T cells using coated pits before translocating from acidified endosomes and eliciting biological responses
    • Vendeville, A., Rayne, F., Bonhoure, A., Bettache, N., Montcourrier, P., and Beaumelle, B. (2004) HIV-1 Tat enters T cells using coated pits before translocating from acidified endosomes and eliciting biological responses. Mol. Biol. Cell 15, 2347-60.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2347-2360
    • Vendeville, A.1    Rayne, F.2    Bonhoure, A.3    Bettache, N.4    Montcourrier, P.5    Beaumelle, B.6
  • 21
    • 16544368801 scopus 로고    scopus 로고
    • Changing picture of cellular drug resistance in human leukemia
    • Norgaard, J. M., Olesen, L. H., and Hokland, P. (2004) Changing picture of cellular drug resistance in human leukemia. Crit. Rev. Oncol. Hematol. 50, 39-49.
    • (2004) Crit. Rev. Oncol. Hematol. , vol.50 , pp. 39-49
    • Norgaard, J.M.1    Olesen, L.H.2    Hokland, P.3
  • 22
    • 0037471140 scopus 로고    scopus 로고
    • High efficiency protein transduction of quiescent and proliferating primary hematopoietic cells
    • Lea, N. C., Buggins, A. G., Orr, S. J., Mufti, G. J., and Thomas, N. S. (2003) High efficiency protein transduction of quiescent and proliferating primary hematopoietic cells. J. Biochem. Biophys. Methods 55, 251-8.
    • (2003) J. Biochem. Biophys. Methods , vol.55 , pp. 251-258
    • Lea, N.C.1    Buggins, A.G.2    Orr, S.J.3    Mufti, G.J.4    Thomas, N.S.5
  • 24
    • 45949123116 scopus 로고
    • Solid-phase synthesis of protected peptide fragments using a trialkoxy-diphenyl-methylester resin
    • Rink, H. (1987) Solid-phase synthesis of protected peptide fragments using a trialkoxy-diphenyl-methylester resin. Tetrahedron Lett. 28, 3787-3790.
    • (1987) Tetrahedron Lett. , vol.28 , pp. 3787-3790
    • Rink, H.1
  • 26
    • 0030794881 scopus 로고    scopus 로고
    • Embodying a stable alpha-helical protein structure through efficient chemical ligation via thioether formation
    • Futaki, S., Ishikawa, T., Niwa, M., Kitagawa, K., and Yagami, T. (1997) Embodying a stable alpha-helical protein structure through efficient chemical ligation via thioether formation. Bioorg. Med. Chem. 5, 1883-91.
    • (1997) Bioorg. Med. Chem. , vol.5 , pp. 1883-1891
    • Futaki, S.1    Ishikawa, T.2    Niwa, M.3    Kitagawa, K.4    Yagami, T.5
  • 31
    • 0030037845 scopus 로고    scopus 로고
    • Membranes and sorting
    • Mellman, I. (1996) Membranes and sorting. Curr. Opin. Cell Biol. 8, 497-8.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 497-498
    • Mellman, I.1
  • 32
    • 17544367319 scopus 로고    scopus 로고
    • Transferrin recycling and dextran transport to lysosomes is differentially affected by bafilomycin, nocodazole, and low temperature
    • Baravalle, G., Schober, D., Huber, M., Bayer, N., Murphy, R. F., and Fuchs, R. (2005) Transferrin recycling and dextran transport to lysosomes is differentially affected by bafilomycin, nocodazole, and low temperature. Cell Tissue Res. 320, 99-113.
    • (2005) Cell Tissue Res. , vol.320 , pp. 99-113
    • Baravalle, G.1    Schober, D.2    Huber, M.3    Bayer, N.4    Murphy, R.F.5    Fuchs, R.6
  • 33
    • 13944258097 scopus 로고    scopus 로고
    • Endocytic delivery to lysosomes mediated by concurrent fusion and kissing events in living cells
    • Bright, N. A., Gratian, M. J., and Luzio, J. P. (2005) Endocytic delivery to lysosomes mediated by concurrent fusion and kissing events in living cells. Curr. Biol. 15, 360-5.
    • (2005) Curr. Biol. , vol.15 , pp. 360-365
    • Bright, N.A.1    Gratian, M.J.2    Luzio, J.P.3
  • 34
    • 0030027394 scopus 로고    scopus 로고
    • Potential sites of PI-3 kinase function in the endocytic pathway revealed by the PI-3 kinase inhibitor, wortmannin
    • Shpetner, H., Joly, M., Hartley, D., and Corvera, S. (1996) Potential sites of PI-3 kinase function in the endocytic pathway revealed by the PI-3 kinase inhibitor, wortmannin. J. Cell Biol. 132, 595-605.
    • (1996) J. Cell Biol. , vol.132 , pp. 595-605
    • Shpetner, H.1    Joly, M.2    Hartley, D.3    Corvera, S.4
  • 35
    • 0033868155 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinases and the regulation of vesicular trafficking
    • Backer, J. M. (2000) Phosphoinositide 3-kinases and the regulation of vesicular trafficking. Mol. Cell Biol. Res. Commun. 3, 193-204.
    • (2000) Mol. Cell Biol. Res. Commun. , vol.3 , pp. 193-204
    • Backer, J.M.1
  • 36
    • 0344851732 scopus 로고    scopus 로고
    • Roles of the cytoskeleton and motor proteins in endocytic sorting
    • Murray, J. W., and Wolkoff, A. W. (2003) Roles of the cytoskeleton and motor proteins in endocytic sorting. Adv. Drug. Delivery Rev. 55, 1385-403.
    • (2003) Adv. Drug. Delivery Rev. , vol.55 , pp. 1385-1403
    • Murray, J.W.1    Wolkoff, A.W.2
  • 37
    • 0024836461 scopus 로고
    • Distinct endocytotic pathways in epidermal growth factor-stimulated human carcinoma A431 cells
    • West, M. A., Bretscher, M. S., and Watts, C. (1989) Distinct endocytotic pathways in epidermal growth factor-stimulated human carcinoma A431 cells. J. Cell Biol. 109, 2731-9.
    • (1989) J. Cell Biol. , vol.109 , pp. 2731-2739
    • West, M.A.1    Bretscher, M.S.2    Watts, C.3
  • 38
    • 0034652007 scopus 로고    scopus 로고
    • Apoptosis of leukemic cells accompanies reduction in intracellular pH after targeted inhibition of the Na(+)/H(+) exchanger
    • Rich, I. N., Worthington-White, D., Garden, O. A., and Musk, P. (2000) Apoptosis of leukemic cells accompanies reduction in intracellular pH after targeted inhibition of the Na(+)/H(+) exchanger. Blood 95, 1427-34.
    • (2000) Blood , vol.95 , pp. 1427-1434
    • Rich, I.N.1    Worthington-White, D.2    Garden, O.A.3    Musk, P.4
  • 39
    • 11844268027 scopus 로고    scopus 로고
    • Cationic TAT peptide transduction domain enters cells by macropinocytosis
    • Kaplan, I. M., Wadia, J. S., and Dowdy, S. F. (2005) Cationic TAT peptide transduction domain enters cells by macropinocytosis. J. Controlled Release 102, 247-53.
    • (2005) J. Controlled Release , vol.102 , pp. 247-253
    • Kaplan, I.M.1    Wadia, J.S.2    Dowdy, S.F.3
  • 40
    • 0034852440 scopus 로고    scopus 로고
    • The relationship between lumenal and limiting membranes in swollen late endocytic compartments formed after wortmannin treatment or sucrose accumulation
    • Bright, N. A., Lindsay, M. R., Stewart, A., and Luzio, J. P. (2001) The relationship between lumenal and limiting membranes in swollen late endocytic compartments formed after wortmannin treatment or sucrose accumulation. Traffic 2, 631-42.
    • (2001) Traffic , vol.2 , pp. 631-642
    • Bright, N.A.1    Lindsay, M.R.2    Stewart, A.3    Luzio, J.P.4
  • 42
    • 0024591235 scopus 로고
    • Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: Evidence for membrane cycling from Golgi to ER
    • Lippincott-Schwartz, J., Yuan, L. C., Bonifacino, J. S., and Klausner, R. D. (1989) Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER. Cell 56, 801-13.
    • (1989) Cell , vol.56 , pp. 801-813
    • Lippincott-Schwartz, J.1    Yuan, L.C.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 43
    • 0024308993 scopus 로고
    • Brefeldin a redistributes resident and itinerant Golgi proteins to the endoplasmic reticulum
    • Doms, R. W., Russ, G., and Yewdell, J. W. (1989) Brefeldin A redistributes resident and itinerant Golgi proteins to the endoplasmic reticulum. J. Cell Biol. 109, 61-72.
    • (1989) J. Cell Biol. , vol.109 , pp. 61-72
    • Doms, R.W.1    Russ, G.2    Yewdell, J.W.3
  • 44
    • 0025232841 scopus 로고
    • Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin a suggests an ER recycling pathway
    • Lippincott-Schwartz, J., Donaldson, J. G., Schweizer, A., Berger, E. G., Hauri, H. P., Yuan, L. C., and Klausner, R. D. (1990) Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway. Cell 60, 821-36.
    • (1990) Cell , vol.60 , pp. 821-836
    • Lippincott-Schwartz, J.1    Donaldson, J.G.2    Schweizer, A.3    Berger, E.G.4    Hauri, H.P.5    Yuan, L.C.6    Klausner, R.D.7
  • 45
    • 0026570788 scopus 로고
    • Perturbation of the morphology of the trans-Golgi network following Brefeldin a treatment: Redistribution of a TGN-specific integral membrane protein, TGN38
    • Reaves, B., and Banting, G. (1992) Perturbation of the morphology of the trans-Golgi network following Brefeldin A treatment: redistribution of a TGN-specific integral membrane protein, TGN38. J. Cell Biol. 116, 85-94.
    • (1992) J. Cell Biol. , vol.116 , pp. 85-94
    • Reaves, B.1    Banting, G.2
  • 46
    • 0023580391 scopus 로고
    • Kinetics of intracellular transport and sorting of lysosomal membrane and plasma membrane proteins
    • Green, S. A., Zimmer, K. P., Griffiths, G., and Mellman, I. (1987) Kinetics of intracellular transport and sorting of lysosomal membrane and plasma membrane proteins. J. Cell Biol. 105, 1227-40.
    • (1987) J. Cell Biol. , vol.105 , pp. 1227-1240
    • Green, S.A.1    Zimmer, K.P.2    Griffiths, G.3    Mellman, I.4
  • 47
    • 0024787848 scopus 로고
    • A quantitative analysis of the endocytic pathway in baby hamster kidney cells
    • Griffiths, G., Back, R., and Marsh, M. (1989) A quantitative analysis of the endocytic pathway in baby hamster kidney cells. J. Cell Biol. 109, 2703-20.
    • (1989) J. Cell Biol. , vol.109 , pp. 2703-2720
    • Griffiths, G.1    Back, R.2    Marsh, M.3
  • 48
    • 0021321990 scopus 로고
    • Lysosomes are associated with microtubules and not with intermediate filaments in cultured fibroblasts
    • Collot, M., Louvard, D., and Singer, S. J. (1984) Lysosomes are associated with microtubules and not with intermediate filaments in cultured fibroblasts. Proc. Natl. Acad. Sci. U.S.A. 81, 788-92.
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 788-792
    • Collot, M.1    Louvard, D.2    Singer, S.J.3
  • 49
    • 0024517745 scopus 로고
    • Characterization of the early endosome and putative endocytic carrier vesicles in vivo and with an assay of vesicle fusion in vitro
    • Gruenberg, J., Griffiths, G., and Howell, K. E. (1989) Characterization of the early endosome and putative endocytic carrier vesicles in vivo and with an assay of vesicle fusion in vitro. J. Cell Biol. 108, 1301-16.
    • (1989) J. Cell Biol. , vol.108 , pp. 1301-1316
    • Gruenberg, J.1    Griffiths, G.2    Howell, K.E.3
  • 50
    • 1842866714 scopus 로고    scopus 로고
    • A role for the lysosomal membrane protein LGP85 in the biogenesis and maintenance of endosomal and lysosomal morphology
    • Kuronita, T., Eskelinen, E. L., Fujita, H., Saftig, P., Himeno, M., and Tanaka, Y. (2002) A role for the lysosomal membrane protein LGP85 in the biogenesis and maintenance of endosomal and lysosomal morphology. J. Cell Sci. 115, 4117-31.
    • (2002) J. Cell Sci. , vol.115 , pp. 4117-4131
    • Kuronita, T.1    Eskelinen, E.L.2    Fujita, H.3    Saftig, P.4    Himeno, M.5    Tanaka, Y.6
  • 52
    • 0348010364 scopus 로고    scopus 로고
    • Cytoplasmic and nuclear delivery of a TAT-derived peptide and a beta-peptide after endocytic uptake into HeLa cells
    • Potocky, T. B., Menon, A. K., and Gellman, S. H. (2003) Cytoplasmic and nuclear delivery of a TAT-derived peptide and a beta-peptide after endocytic uptake into HeLa cells. J. Biol. Chem. 278, 50188-94.
    • (2003) J. Biol. Chem. , vol.278 , pp. 50188-50194
    • Potocky, T.B.1    Menon, A.K.2    Gellman, S.H.3
  • 54
    • 17644386231 scopus 로고    scopus 로고
    • Cellular uptake of unconjugated TAT peptide involves clathrin-dependent endocytosis and heparan sulfate receptors
    • Richard, J. P., Melikov, K., Brooks, H., Prevot, P., Lebleu, B., and Chernomordik, L. V. (2005) Cellular uptake of unconjugated TAT peptide involves clathrin-dependent endocytosis and heparan sulfate receptors. J. Biol. Chem. 280, 15300-15306.
    • (2005) J. Biol. Chem. , vol.280 , pp. 15300-15306
    • Richard, J.P.1    Melikov, K.2    Brooks, H.3    Prevot, P.4    Lebleu, B.5    Chernomordik, L.V.6
  • 55
    • 0038105847 scopus 로고    scopus 로고
    • Organelle acidification and disease
    • Weisz, O. A. (2003) Organelle acidification and disease. Traffic 4, 57-64.
    • (2003) Traffic , vol.4 , pp. 57-64
    • Weisz, O.A.1
  • 56
    • 0042232110 scopus 로고    scopus 로고
    • Studies on the internalization mechanism of cationic cell-penetrating peptides
    • Drin, G., Cottin, S., Blanc, E., Rees, A. R., and Temsamani, J. (2003) Studies on the internalization mechanism of cationic cell-penetrating peptides. J. Biol. Chem. 278, 31192-201.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31192-31201
    • Drin, G.1    Cottin, S.2    Blanc, E.3    Rees, A.R.4    Temsamani, J.5
  • 58
    • 0027237639 scopus 로고
    • Role of microtubules in transferrin receptor transport from the cell surface to endosomes and the Golgi complex
    • Jin, M., and Snider, M. D. (1993) Role of microtubules in transferrin receptor transport from the cell surface to endosomes and the Golgi complex. J. Biol. Chem. 268, 18390-7.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18390-18397
    • Jin, M.1    Snider, M.D.2
  • 59
    • 0037345697 scopus 로고    scopus 로고
    • Quantitative analysis of permeation peptide complexes labeled with Technetium-99m: Chiral and sequence-specific effects on net cell uptake
    • Gammon, S. T., Villalobos, V. M., Prior, J. L., Sharma, V., and Piwnica-Worms, D. (2003) Quantitative analysis of permeation peptide complexes labeled with Technetium-99m: chiral and sequence-specific effects on net cell uptake. Bioconjugate Chem. 14, 368-76.
    • (2003) Bioconjugate Chem. , vol.14 , pp. 368-376
    • Gammon, S.T.1    Villalobos, V.M.2    Prior, J.L.3    Sharma, V.4    Piwnica-Worms, D.5


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