메뉴 건너뛰기




Volumn 6, Issue 1, 2011, Pages 55-68

Transferrin-mediated targeting of bacteriophage HK97 nanoparticles into tumor cells

Author keywords

cancer; HK97; protein conjugation; targeted cellular entry; transferrin; viral nanoparticles

Indexed keywords

FLUORESCENT DYE; NANOPARTICLE; TRANSFERRIN; TRANSFERRIN RECEPTOR; UNCLASSIFIED DRUG; VIRAL NANOPARTICLE;

EID: 78650670099     PISSN: 17435889     EISSN: None     Source Type: Journal    
DOI: 10.2217/nnm.10.99     Document Type: Article
Times cited : (53)

References (57)
  • 1
    • 33644994202 scopus 로고    scopus 로고
    • Vascular targeting: Recent advances and therapeutic perspectives
    • Hajitou A, Pasqualini R, Arap W: Vascular targeting: recent advances and therapeutic perspectives. Trends cardiovasc. Med. 16(3), 80-88 (2006).
    • (2006) Trends Cardiovasc. Med , vol.16 , Issue.3 , pp. 80-88
    • Hajitou, A.1    Pasqualini, R.2    Arap, W.3
  • 2
    • 39649092973 scopus 로고    scopus 로고
    • Nanotechnology and cancer
    • Heath Jr, DME: Nanotechnology and cancer. Annu. Rev. Med. 59, 251-265 (2008).
    • (2008) Annu. Rev. Med , vol.59 , pp. 251-265
    • Heath Jr., D.M.E.1
  • 3
    • 52949130961 scopus 로고    scopus 로고
    • Current dendrimer applications in cancer diagnosis and therapy
    • Majoros IJ, Williams CR, Baker Jr: Current dendrimer applications in cancer diagnosis and therapy. Curr. Top. Med. Chem. 8(14), 1165-1179 (2008).
    • (2008) Curr. Top. Med. Chem , vol.8 , Issue.14 , pp. 1165-1179
    • Majoros, I.J.1    Williams, C.R.2    Baker, Jr.3
  • 4
    • 33751534216 scopus 로고    scopus 로고
    • Virus-based nanoparticles (VNPS): Platform technologies for diagnostic imaging
    • Manchester M, Singh P: Virus-based nanoparticles (VNPS): platform technologies for diagnostic imaging. Adv. Drug Deliv. Rev. 58(14), 1505-1522 (2006).
    • (2006) Adv. Drug Deliv. Rev , vol.58 , Issue.14 , pp. 1505-1522
    • Manchester, M.1    Singh, P.2
  • 6
    • 58149375843 scopus 로고    scopus 로고
    • Quantum dot bioconjugates for in vitro diagnostics & in vivo imaging
    • Xing Y, Rao J: Quantum dot bioconjugates for in vitro diagnostics & in vivo imaging. Cancer Biomark. 4(6), 307-319 (2008).
    • (2008) Cancer Biomark , vol.4 , Issue.6 , pp. 307-319
    • Xing, Y.1    Rao, J.2
  • 8
    • 34250836946 scopus 로고    scopus 로고
    • Viruses as building blocks for materials and devices
    • Fischlechner M, Donath E: Viruses as building blocks for materials and devices. Angew. Chem. Int. Ed. Engl. 46(18), 3184-3193 (2007).
    • (2007) Angew. Chem. Int. Ed. Engl , vol.46 , Issue.18 , pp. 3184-3193
    • Fischlechner, M.1    Donath, E.2
  • 9
    • 21244491577 scopus 로고    scopus 로고
    • A AV hybrid serotypes: Improved vectors for gene delivery
    • Choi VW, Mccarty DM, Samulski RJ: A AV hybrid serotypes: improved vectors for gene delivery. Curr. Gene Ther. 5(3), 299-310 (2005).
    • (2005) Curr. Gene Ther , vol.5 , Issue.3 , pp. 299-310
    • Choi, V.W.1    McCarty, D.M.2    Samulski, R.J.3
  • 10
    • 36249015420 scopus 로고    scopus 로고
    • Gene delivery by lentivirus vectors
    • Cockrell AS, Kafri T: Gene delivery by lentivirus vectors. Mol. Biotechnol. 36(3), 184-204 (2007).
    • (2007) Mol. Biotechnol , vol.36 , Issue.3 , pp. 184-204
    • Cockrell, A.S.1    Kafri, T.2
  • 11
    • 1542425319 scopus 로고    scopus 로고
    • Adenovirus-mediated gene delivery: An overview
    • Douglas JT: Adenovirus-mediated gene delivery: an overview. Methods Mol. Biol. 246, 3-14 (2004).
    • (2004) Methods Mol. Biol , vol.246 , pp. 3-14
    • Douglas, J.T.1
  • 12
    • 34547892332 scopus 로고    scopus 로고
    • Viral capsids as MRI contrast agents
    • Liepold L, Anderson S, Willits D et al.: Viral capsids as MRI contrast agents. Magn. Reson. Med. 58(5), 871-879 (2007).
    • (2007) Magn. Reson. Med , vol.58 , Issue.5 , pp. 871-879
    • Liepold, L.1    Anderson, S.2    Willits, D.3
  • 13
    • 0036980063 scopus 로고    scopus 로고
    • RNA bacteriophage capsid-mediated drug delivery and epitope presentation
    • Brown WL, Mastico RA, Wu M et al.: RNA bacteriophage capsid-mediated drug delivery and epitope presentation. Intervirology 45(4-6), 371-380 (2002).
    • (2002) Intervirology , vol.45 , Issue.4-6 , pp. 371-380
    • Brown, W.L.1    Mastico, R.A.2    Wu, M.3
  • 14
    • 33644822413 scopus 로고    scopus 로고
    • Viral nanoparticles as tools for intravital vascular imaging
    • Lewis JD, Destito G, Zijlstra A et al.: Viral nanoparticles as tools for intravital vascular imaging. Nat. Med. 12(3), 354-360 (2006).
    • (2006) Nat. Med , vol.12 , Issue.3 , pp. 354-360
    • Lewis, J.D.1    Destito, G.2    Zijlstra, A.3
  • 15
    • 34347347264 scopus 로고    scopus 로고
    • Folic acid-conjugated protein cages of a plant virus: A novel delivery platform for doxorubicin
    • Ren Y, Wong SM, Lim LY: Folic acid-conjugated protein cages of a plant virus: a novel delivery platform for doxorubicin. Bioconjug. Chem. 18(3), 836-843 (2007).
    • (2007) Bioconjug. Chem , vol.18 , Issue.3 , pp. 836-843
    • Ren, Y.1    Wong, S.M.2    Lim, L.Y.3
  • 16
    • 34249946384 scopus 로고    scopus 로고
    • Bio-distribution, toxicity and pathology of cowpea mosaic virus nanoparticles in vivo
    • Singh P, Prasuhn D, Yeh RM et al.: Bio-distribution, toxicity and pathology of cowpea mosaic virus nanoparticles in vivo. J. Control. Release 120(1-2), 41-50 (2007).
    • (2007) J. Control. Release , vol.120 , Issue.1-2 , pp. 41-50
    • Singh, P.1    Prasuhn, D.2    Yeh, R.M.3
  • 17
    • 0019065328 scopus 로고
    • Host range, immunity and antigenic properties of lambdoid coliphage hk97
    • Dhillon EK, Dhillon TS, Lai AN, Linn S: Host range, immunity and antigenic properties of lambdoid coliphage hk97 J. Gen. Virol. 50(1), 217-220 (1980).
    • (1980) J. Gen. Virol , vol.50 , Issue.1 , pp. 217-220
    • Dhillon, E.K.1    Dhillon, T.S.2    Lai, A.N.3    Linn, S.4
  • 19
    • 2942572925 scopus 로고    scopus 로고
    • Control of crosslinking by quaternary structure changes during bacteriophage HK97 maturation
    • Gan L, Conway JF, Firek BA et al.: Control of crosslinking by quaternary structure changes during bacteriophage HK97 maturation. Mol. Cell 14(5), 559-569 (2004).
    • (2004) Mol. Cell , vol.14 , Issue.5 , pp. 559-569
    • Gan, L.1    Conway, J.F.2    Firek, B.A.3
  • 20
    • 17044437232 scopus 로고    scopus 로고
    • Crosslinking renders bacteriophage HK97 capsid maturation irreversible and effects an essential stabilization
    • Ross PD, Cheng N, Conway JF et al.: Crosslinking renders bacteriophage HK97 capsid maturation irreversible and effects an essential stabilization. EMBO J. 24(7), 1352-1363 (2005).
    • (2005) EMBO J , vol.24 , Issue.7 , pp. 1352-1363
    • Ross, P.D.1    Cheng, N.2    Conway, J.F.3
  • 21
    • 34548761987 scopus 로고    scopus 로고
    • Encapsidation of nanoparticles by red clover necrotic mosaic virus
    • Loo L, Guenther RH, Lommel SA, Franzen S: Encapsidation of nanoparticles by red clover necrotic mosaic virus. J. Am. Chem. Soc. 129(36), 11111-11117 (2007).
    • (2007) J. Am. Chem. Soc , vol.129 , Issue.36 , pp. 11111-11117
    • Loo, L.1    Guenther, R.H.2    Lommel, S.A.3    Franzen, S.4
  • 22
    • 71749104916 scopus 로고    scopus 로고
    • Controlled encapsulation of multiple proteins in virus capsids
    • Minten IJ, Hendriks LJ, Nolte RJ, Cornelissen JJ: Controlled encapsulation of multiple proteins in virus capsids. J. Am. Chem. Soc. 131(49), 17771-17773 (2009).
    • (2009) J. Am. Chem. Soc , vol.131 , Issue.49 , pp. 17771-17773
    • Minten, I.J.1    Hendriks, L.J.2    Nolte, R.J.3    Cornelissen, J.J.4
  • 23
    • 0028927348 scopus 로고
    • Genetic basis of bacteriophage HK97 prohead assembly
    • Duda RL, Martincic K, Hendrix RW: Genetic basis of bacteriophage HK97 prohead assembly J. Mol. Biol. 247(4), 636-647 (1995).
    • (1995) J. Mol. Biol , vol.247 , Issue.4 , pp. 636-647
    • Duda, R.L.1    Martincic, K.2    Hendrix, R.W.3
  • 25
    • 63849128084 scopus 로고    scopus 로고
    • An unexpected twist in viral capsid maturation
    • Gertsman I, Gan L, Guttman M et al.: An unexpected twist in viral capsid maturation. Nature 458(7238), 646-650 (2009).
    • (2009) Nature , vol.458 , Issue.7238 , pp. 646-650
    • Gertsman, I.1    Gan, L.2    Guttman, M.3
  • 26
  • 27
    • 34547589312 scopus 로고    scopus 로고
    • Chemical introduction of reactive thiols into a viral nanoscaffold: A method that avoids virus aggregation
    • Steinmetz NF, Evans DJ, Lomonossoff GP: Chemical introduction of reactive thiols into a viral nanoscaffold: a method that avoids virus aggregation. Chembiochem 8(10), 1131-1136 (2007).
    • (2007) Chembiochem , vol.8 , Issue.10 , pp. 1131-1136
    • Steinmetz, N.F.1    Evans, D.J.2    Lomonossoff, G.P.3
  • 28
    • 0035989991 scopus 로고    scopus 로고
    • Natural supramolecular building blocks: Cysteine-added mutants of Cowpea mosaic virus
    • DOI 10.1016/S1074-5521(02)00166-7, PII S1074552102001667
    • Wang Q, Lin T, Johnson JE, Finn MG: Natural supramolecular building blocks: cysteine-added mutants of cowpea mosaic virus. Chem. Biol. 9(7), 813-819 (2002). (Pubitemid 34861158)
    • (2002) Chemistry and Biology , vol.9 , Issue.7 , pp. 813-819
    • Wang, Q.1    Lin, T.2    Johnson, J.E.3    Finn, M.G.4
  • 29
    • 0036889760 scopus 로고    scopus 로고
    • Targeted drug delivery via the transferrin receptor-mediated endocytosis pathway
    • Qian ZM, Li H, Sun H, Ho K: Targeted drug delivery via the transferrin receptor-mediated endocytosis pathway. Pharmacol. Rev. 54(4), 561-587 (2002).
    • (2002) Pharmacol. Rev , vol.54 , Issue.4 , pp. 561-587
    • Qian, Z.M.1    Li, H.2    Sun, H.3    Ho, K.4
  • 31
    • 0027290910 scopus 로고
    • Differences in transferrin response and numbers of transferrin receptors in rat and human mammary carcinoma lines of different metastatic potentials
    • Inoue T, Cavanaugh PG, Steck PA, Brunner N, Nicolson GL: Differences in transferrin response and numbers of transferrin receptors in rat and human mammary carcinoma lines of different metastatic potentials. J. Cell Physiol. 156(1), 212-217 (1993).
    • (1993) J. Cell Physiol , vol.156 , Issue.1 , pp. 212-217
    • Inoue, T.1    Cavanaugh, P.G.2    Steck, P.A.3    Brunner, N.4    Nicolson, G.L.5
  • 32
    • 0022411688 scopus 로고
    • Discordance between transferrin receptor expression and susceptibility to lysis by natural killer cells
    • Bridges KR, Smith BR: Discordance between transferrin receptor expression and susceptibility to lysis by natural killer cells. J. Clin. Invest. 76(3), 913-918 (1985).
    • (1985) J. Clin. Invest , vol.76 , Issue.3 , pp. 913-918
    • Bridges, K.R.1    Smith, B.R.2
  • 33
    • 0018850974 scopus 로고
    • Transferrin and transferrin receptors in carcinoma of the breast
    • Faulk WP, Hsi BL, Stevens PJ: Transferrin and transferrin receptors in carcinoma of the breast. Lancet 2(8191), 390-392 (1980).
    • (1980) Lancet , vol.2 , Issue.8191 , pp. 390-392
    • Faulk, W.P.1    Hsi, B.L.2    Stevens, P.J.3
  • 34
    • 0020597630 scopus 로고
    • Transferrin receptors in human tissues: Their distribution and possible clinical relevance
    • Gatter KC, Brown G, Trowbridge IS, Woolston RE, Mason DY: Transferrin receptors in human tissues: Their distribution and possible clinical relevance. J. Clin. Pathol. 36(5), 539-545 (1983).
    • (1983) J. Clin. Pathol , vol.36 , Issue.5 , pp. 539-545
    • Gatter, K.C.1    Brown, G.2    Trowbridge, I.S.3    Woolston, R.E.4    Mason, D.Y.5
  • 35
    • 0023217393 scopus 로고
    • The physiology of transferrin and transferrin receptors
    • Huebers HA, Finch CA: The physiology of transferrin and transferrin receptors. Physiol. Rev. 67(2), 520-582 (1987).
    • (1987) Physiol. Rev , vol.67 , Issue.2 , pp. 520-582
    • Huebers, H.A.1    Finch, C.A.2
  • 36
    • 33846460777 scopus 로고    scopus 로고
    • Tumor cell targeting of transferrin-PEG-TNF-a conjugate via a receptor-mediated delivery system: Design, synthesis, and biological evaluation
    • Jiang YY, Liu C, Hong MH, Zhu SJ, Pei YY: Tumor cell targeting of transferrin-PEG-TNF-a conjugate via a receptor-mediated delivery system: design, synthesis, and biological evaluation. Bioconjug. Chem. 18(1), 41-49 (2007).
    • (2007) Bioconjug. Chem , vol.18 , Issue.1 , pp. 41-49
    • Jiang, Y.Y.1    Liu, C.2    Hong, M.H.3    Zhu, S.J.4    Pei, Y.Y.5
  • 37
    • 0020629655 scopus 로고
    • The primary structure of human serum transferrin. The structures of seven cyanogen bromide fragments and the assembly of the complete structure
    • Macgillivray RT, Mendez E, Shewale JG, Sinha SK, Lineback-Zins J, Brew K: The primary structure of human serum transferrin. The structures of seven cyanogen bromide fragments and the assembly of the complete structure. J. Biol. Chem. 258(6), 3543-3553 (1983).
    • (1983) J. Biol. Chem , vol.258 , Issue.6 , pp. 3543-3553
    • MacGillivray, R.T.1    Mendez, E.2    Shewale, J.G.3    Sinha, S.K.4    Lineback-Zins, J.5    Brew, K.6
  • 38
    • 0033596746 scopus 로고    scopus 로고
    • X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32
    • Bewley MC, Tam BM, Grewal J et al.: X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32. Biochemistry 38(8), 2535-2541 (1999).
    • (1999) Biochemistry , vol.38 , Issue.8 , pp. 2535-2541
    • Bewley, M.C.1    Tam, B.M.2    Grewal, J.3
  • 39
    • 0026634034 scopus 로고
    • Conjugation of soluble cd4 without loss of biological activity via a novel carbohydrate- directed cross-linking reagent
    • Chamow SM, Kogan TP, Peers DH, Hastings RC, Byrn RA, Ashkenazi A: Conjugation of soluble cd4 without loss of biological activity via a novel carbohydrate- directed cross-linking reagent. J. Biol. Chem. 267(22), 15916-15922 (1992).
    • (1992) J. Biol. Chem , vol.267 , Issue.22 , pp. 15916-15922
    • Chamow, S.M.1    Kogan, T.P.2    Peers, D.H.3    Hastings, R.C.4    Byrn, R.A.5    Ashkenazi, A.6
  • 40
    • 27944488746 scopus 로고    scopus 로고
    • Accelerated bioorthogonal conjugation: A practical method for the ligation of diverse functional molecules to a polyvalent virus scaffold
    • Sen Gupta S, Kuzelka J, Singh P, Lewis WG, Manchester M, Finn MG: Accelerated bioorthogonal conjugation: a practical method for the ligation of diverse functional molecules to a polyvalent virus scaffold. Bioconjug. Chem. 16(6), 1572-1579 (2005).
    • (2005) Bioconjug. Chem , vol.16 , Issue.6 , pp. 1572-1579
    • Sen Gupta, S.1    Kuzelka, J.2    Singh, P.3    Lewis, W.G.4    Manchester, M.5    Finn, M.G.6
  • 41
    • 0029366201 scopus 로고
    • Cell-specifc delivery of bacteriophage-encapsidated ricin a chain
    • Wu M, Brown WL, Stockley PG: Cell-specifc delivery of bacteriophage-encapsidated ricin a chain. Bioconjug. Chem. 6(5), 587-595 (1995).
    • (1995) Bioconjug. Chem , vol.6 , Issue.5 , pp. 587-595
    • Wu, M.1    Brown, W.L.2    Stockley, P.G.3
  • 42
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera - A visualization system for exploratory research and ana lysis
    • Pettersen EF, Goddard TD, Huang CC et al.: UCSF Chimera - a visualization system for exploratory research and ana lysis. J. Comput. Chem. 25(13), 1605-1612 (2004).
    • (2004) J. Comput. Chem , vol.25 , Issue.13 , pp. 1605-1612
    • Pettersen, E.F.1    Goddard, T.D.2    Huang, C.C.3
  • 43
    • 71049187676 scopus 로고    scopus 로고
    • Interaction of cowpea mosaic virus (CPMV) nanoparticles with antigen presenting cells in vitro and in vivo
    • Gonzalez MJ, Plummer EM, Rae CS, Manchester M: Interaction of cowpea mosaic virus (CPMV) nanoparticles with antigen presenting cells in vitro and in vivo. PLoS One 4(11), e7981 (2009).
    • (2009) PLoS One , vol.4 , Issue.11
    • Gonzalez, M.J.1    Plummer, E.M.2    Rae, C.S.3    Manchester, M.4
  • 45
    • 67349200288 scopus 로고    scopus 로고
    • Viral nanoparticles associate with regions of infammation and blood brain barrier disruption during CNS infection
    • Shriver LP, Koudelka KJ, Manchester M: Viral nanoparticles associate with regions of infammation and blood brain barrier disruption during CNS infection. J. Neuroimmunol. 211(1-2), 66-72 (2009).
    • (2009) J. Neuroimmunol , vol.211 , Issue.1-2 , pp. 66-72
    • Shriver, L.P.1    Koudelka, K.J.2    Manchester, M.3
  • 46
    • 65249114149 scopus 로고    scopus 로고
    • Pegylated viral nanoparticles for biomedicine: The impact of PEG chain length on VNP cell interactions in vitro and ex vivo
    • Steinmetz NF, Manchester M: Pegylated viral nanoparticles for biomedicine: the impact of PEG chain length on VNP cell interactions in vitro and ex vivo. Biomacromolecules 10(4), 784-792 (2009).
    • (2009) Biomacromolecules , vol.10 , Issue.4 , pp. 784-792
    • Steinmetz, N.F.1    Manchester, M.2
  • 47
    • 72249099458 scopus 로고    scopus 로고
    • Buckyballs meet viral nanoparticles: Candidates for biomedicine
    • Steinmetz NF, Hong V, Spoerke ED et al.: Buckyballs meet viral nanoparticles: Candidates for biomedicine. J. Am. Chem. Soc. 131(47), 17093-17095 (2009).
    • (2009) J. Am. Chem. Soc , vol.131 , Issue.47 , pp. 17093-17095
    • Steinmetz, N.F.1    Hong, V.2    Spoerke, E.D.3
  • 48
    • 74849109414 scopus 로고    scopus 로고
    • Potato virus X as a novel platform for potential biomedical applications
    • Steinmetz NF, Mertens ME, Taurog RE et al.: Potato virus X as a novel platform for potential biomedical applications. Nano Lett. 10(1), 305-312 (2010).
    • (2010) Nano Lett , vol.10 , Issue.1 , pp. 305-312
    • Steinmetz, N.F.1    Mertens, M.E.2    Taurog, R.E.3
  • 49
    • 51849123089 scopus 로고    scopus 로고
    • Biodistribution studies of protein cage nanoparticles demonstrate broad tissue distribution and rapid clearance in vivo
    • Kaiser CR, Flenniken ML, Gillitzer E et al.: Biodistribution studies of protein cage nanoparticles demonstrate broad tissue distribution and rapid clearance in vivo. Int. J. Nanomedicine 2(4), 715-733 (2007).
    • (2007) Int. J. Nanomedicine , vol.2 , Issue.4 , pp. 715-733
    • Kaiser, C.R.1    Flenniken, M.L.2    Gillitzer, E.3
  • 50
    • 38649111325 scopus 로고    scopus 로고
    • Plasma clearance of bacteriophage qbeta particles as a function of surface charge
    • Prasuhn De Jr, Singh P, Strable E, Brown S, Manchester M, Finn MG: Plasma clearance of bacteriophage qbeta particles as a function of surface charge. J. Am. Chem. Soc. 130(4), 1328-1334 (2008).
    • (2008) J. Am. Chem. Soc , vol.130 , Issue.4 , pp. 1328-1334
    • Prasuhn Jr., D.1    Singh, P.2    Strable, E.3    Brown, S.4    Manchester, M.5    Finn, M.G.6
  • 51
    • 46849103828 scopus 로고    scopus 로고
    • Antibody tumor penetration: Transport opposed by systemic and antigen-mediated clearance
    • Thurber GM, Schmidt MM, Wittrup KD: Antibody tumor penetration: transport opposed by systemic and antigen-mediated clearance. Adv. Drug Deliv. Rev. 60, 1421-1434 (2008).
    • (2008) Adv. Drug Deliv. Rev , vol.60 , pp. 1421-1434
    • Thurber, G.M.1    Schmidt, M.M.2    Wittrup, K.D.3
  • 52
    • 0036238011 scopus 로고    scopus 로고
    • Transferrin/transferrin receptor-mediated drug delivery
    • Li H, Qian ZM: Transferrin/transferrin receptor-mediated drug delivery. Med. Res. Rev. 22(3), 225-250 (2002).
    • (2002) Med. Res. Rev , vol.22 , Issue.3 , pp. 225-250
    • Li, H.1    Qian, Z.M.2
  • 53
    • 0021755746 scopus 로고
    • Structural comparison of the two distinct sugar binding sites in wheat germ agglutinin isolectin II
    • Wright CS: Structural comparison of the two distinct sugar binding sites in wheat germ agglutinin isolectin II. J. Mol. Biol. 178(1), 91-104 (1984).
    • (1984) J. Mol. Biol , vol.178 , Issue.1 , pp. 91-104
    • Wright, C.S.1
  • 54
    • 0031876774 scopus 로고    scopus 로고
    • Targeting of ultrasmall superparamagnetic iron oxide (USPIO) particles to tumor cells in vivo by using transferrin receptor pathways
    • Kresse M, Wagner S, Pfefferer D, Lawaczeck R, Elste V, Semmler W: Targeting of ultrasmall superparamagnetic iron oxide (USPIO) particles to tumor cells in vivo by using transferrin receptor pathways. Magn. Reson. Med. 40(2), 236-242 (1998).
    • (1998) Magn. Reson. Med , vol.40 , Issue.2 , pp. 236-242
    • Kresse, M.1    Wagner, S.2    Pfefferer, D.3    Lawaczeck, R.4    Elste, V.5    Semmler, W.6
  • 55
    • 33744464256 scopus 로고    scopus 로고
    • The in vitro antitumor effect and in vivo tumor-specifcity distribution of human- mouse chimeric antibody against transferrin receptor
    • Qing Y, Shuo W, Zhihua W et al.: The in vitro antitumor effect and in vivo tumor-specifcity distribution of human- mouse chimeric antibody against transferrin receptor. Cancer Immunol. Immunother. 55(9), 1111-1121 (2006).
    • (2006) Cancer Immunol. Immunother , vol.55 , Issue.9 , pp. 1111-1121
    • Qing, Y.1    Shuo, W.2    Zhihua, W.3
  • 56
    • 0033820595 scopus 로고    scopus 로고
    • In vivo gene delivery to tumor cells by transferrin-streptavidin-DNA conjugate
    • Sato Y, Yamauchi N, Takahashi M et al.: In vivo gene delivery to tumor cells by transferrin-streptavidin-DNA conjugate. FASEB J. 14(13), 2108-2118 (2000).
    • (2000) FASEB J , vol.14 , Issue.13 , pp. 2108-2118
    • Sato, Y.1    Yamauchi, N.2    Takahashi, M.3
  • 57
    • 0025005475 scopus 로고
    • Combinations of anti-transferrin receptor monoclonal antibodies inhibit human tumor cell growth in vitro and in vivo: Evidence for synergistic antiproliferative effects
    • White S, Taetle R, Seligman PA, Rutherford M, Trowbridge IS: Combinations of anti-transferrin receptor monoclonal antibodies inhibit human tumor cell growth in vitro and in vivo: evidence for synergistic antiproliferative effects. Cancer Res. 50(19), 6295-6301 (1990).
    • (1990) Cancer Res , vol.50 , Issue.19 , pp. 6295-6301
    • White, S.1    Taetle, R.2    Seligman, P.A.3    Rutherford, M.4    Trowbridge, I.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.