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Volumn 172, Issue 1, 2013, Pages 169-178

Chemically and biologically synthesized CPP-modified gelonin for enhanced anti-tumor activity

Author keywords

Cancer; Cell penetrating peptide; Gelonin; LMWP; Ribosome inactivating protein; Toxin

Indexed keywords

CANCER; CELL-PENETRATING PEPTIDE; GELONIN; LMWP; RIBOSOME-INACTIVATING PROTEIN; TOXIN;

EID: 84883609896     PISSN: 01683659     EISSN: 18734995     Source Type: Journal    
DOI: 10.1016/j.jconrel.2013.08.016     Document Type: Article
Times cited : (35)

References (49)
  • 1
    • 79960439775 scopus 로고    scopus 로고
    • The power of chemotherapeutic engineering: Arresting cell cycle and suppressing senescence to protect from mitotic inhibitors
    • M.V. Blagosklonny The power of chemotherapeutic engineering: arresting cell cycle and suppressing senescence to protect from mitotic inhibitors Cell Cycle 10 2011 2295 2298
    • (2011) Cell Cycle , vol.10 , pp. 2295-2298
    • Blagosklonny, M.V.1
  • 3
    • 33747226732 scopus 로고    scopus 로고
    • SiRNA-based approaches in cancer therapy
    • G.R. Devi siRNA-based approaches in cancer therapy Cancer Gene Ther. 13 2006 819 829
    • (2006) Cancer Gene Ther. , vol.13 , pp. 819-829
    • Devi, G.R.1
  • 4
    • 27144449009 scopus 로고    scopus 로고
    • Monoclonal antibody therapy of cancer
    • DOI 10.1038/nbt1137, PII N1137
    • G.P. Adams, and L.M. Weiner Monoclonal antibody therapy of cancer Nat. Biotechnol. 23 2005 1147 1157 (Pubitemid 41486396)
    • (2005) Nature Biotechnology , vol.23 , Issue.9 , pp. 1147-1157
    • Adams, G.P.1    Weiner, L.M.2
  • 5
    • 39049130647 scopus 로고    scopus 로고
    • Cell-penetrating peptides for drug delivery across membrane barriers
    • DOI 10.1517/17425247.5.1.105
    • C. Foged, and H.M. Nielsen Cell-penetrating peptides for drug delivery across membrane barriers Expert Opin. Drug Deliv. 5 2008 105 117 (Pubitemid 351234112)
    • (2008) Expert Opinion on Drug Delivery , vol.5 , Issue.1 , pp. 105-117
    • Foged, C.1    Nielsen, H.M.2
  • 6
    • 1542721107 scopus 로고    scopus 로고
    • Cell penetrating peptides in drug delivery
    • DOI 10.1023/B:PHAM.0000019289.61978.f5
    • E.L. Snyder, and S.F. Dowdy Cell penetrating peptides in drug delivery Pharm. Res. 21 2004 389 393 (Pubitemid 38338971)
    • (2004) Pharmaceutical Research , vol.21 , Issue.3 , pp. 389-393
    • Snyder, E.L.1    Dowdy, S.F.2
  • 7
    • 0020482525 scopus 로고
    • On the action of ribosome-inactivating proteins: Are plant ribosomes species-specific?
    • F. Stirpe On the action of ribosome-inactivating proteins: are plant ribosomes species-specific? Biochem. J. 202 1982 279 280
    • (1982) Biochem. J. , vol.202 , pp. 279-280
    • Stirpe, F.1
  • 8
    • 84863519513 scopus 로고    scopus 로고
    • Ribosome-inactivating proteins: Current status and biomedical applications
    • M. Puri, I. Kaur, M.A. Perugini, and R.C. Gupta Ribosome-inactivating proteins: current status and biomedical applications Drug Discov. Today 17 2012 774 783
    • (2012) Drug Discov. Today , vol.17 , pp. 774-783
    • Puri, M.1    Kaur, I.2    Perugini, M.A.3    Gupta, R.C.4
  • 9
    • 4043133131 scopus 로고    scopus 로고
    • Ribosome-inactivating proteins
    • DOI 10.1016/j.toxicon.2004.05.004, PII S0041010104001904
    • F. Stirpe Ribosome-inactivating proteins Toxicon 44 2004 371 383 (Pubitemid 39070639)
    • (2004) Toxicon , vol.44 , Issue.4 , pp. 371-383
    • Stirpe, F.1
  • 10
    • 84863285459 scopus 로고    scopus 로고
    • Interaction of ricin and Shiga toxins with ribosomes
    • N.E. Tumer, and X.P. Li Interaction of ricin and Shiga toxins with ribosomes Curr. Top. Microbiol. Immunol. 357 2012 1 18
    • (2012) Curr. Top. Microbiol. Immunol. , vol.357 , pp. 1-18
    • Tumer, N.E.1    Li, X.P.2
  • 11
    • 0019212385 scopus 로고
    • Gelonin, a new inhibitor of protein synthesis, nontoxic to intact cells. Isolation, characterization, and preparation of cytotoxic complexes with concanavalin A
    • F. Stirpe, S. Olsnes, and A. Pihl Gelonin, a new inhibitor of protein synthesis, nontoxic to intact cells. Isolation, characterization, and preparation of cytotoxic complexes with concanavalin A J. Biol. Chem. 255 1980 6947 6953 (Pubitemid 11234436)
    • (1980) Journal of Biological Chemistry , vol.255 , Issue.14 , pp. 6947-6953
    • Stirpe, F.1    Olsnes, S.2    Pihl, A.3
  • 12
    • 0035958878 scopus 로고    scopus 로고
    • Conjugation of folate via gelonin carbohydrate residues retains ribosomal-inactivating properties of the toxin and permits targeting to folate receptor positive cells
    • S.F. Atkinson, T. Bettinger, L.W. Seymour, J.P. Behr, and C.M. Ward Conjugation of folate via gelonin carbohydrate residues retains ribosomal-inactivating properties of the toxin and permits targeting to folate receptor positive cells J. Biol. Chem. 276 2001 27930 27935
    • (2001) J. Biol. Chem. , vol.276 , pp. 27930-27935
    • Atkinson, S.F.1    Bettinger, T.2    Seymour, L.W.3    Behr, J.P.4    Ward, C.M.5
  • 13
    • 0018167496 scopus 로고
    • One molecule of diphtheria toxin fragment A introduced into a cell can kill the cell
    • M. Yamaizumi, E. Mekada, T. Uchida, and Y. Okada One molecule of diphtheria toxin fragment A introduced into a cell can kill the cell Cell 15 1978 245 250 (Pubitemid 9027527)
    • (1978) Cell , vol.15 , Issue.1 , pp. 245-250
    • Yamaizumi, M.1    Mekada, E.2    Uchida, T.3    Okada, Y.4
  • 14
    • 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
  • 15
    • 68549110328 scopus 로고    scopus 로고
    • Twenty years of cell-penetrating peptides: From molecular mechanisms to therapeutics
    • F. Heitz, M.C. Morris, and G. Divita Twenty years of cell-penetrating peptides: from molecular mechanisms to therapeutics Br. J. Pharmacol. 157 2009 195 206
    • (2009) Br. J. Pharmacol. , vol.157 , pp. 195-206
    • Heitz, F.1    Morris, M.C.2    Divita, G.3
  • 16
    • 84863099046 scopus 로고    scopus 로고
    • Cell-penetrating peptides: Breaking through to the other side
    • E. Koren, and V.P. Torchilin Cell-penetrating peptides: breaking through to the other side Trends Mol. Med. 18 2012 385 393
    • (2012) Trends Mol. Med. , vol.18 , pp. 385-393
    • Koren, E.1    Torchilin, V.P.2
  • 17
    • 20944447518 scopus 로고    scopus 로고
    • Cell-penetrating peptides: Small from inception to application
    • DOI 10.1017/S0033583505004014
    • M. Magzoub, and A. Graslund Cell-penetrating peptides: [corrected] from inception to application Q. Rev. Biophys. 37 2004 147 195 (Pubitemid 40867965)
    • (2004) Quarterly Reviews of Biophysics , vol.37 , Issue.2 , pp. 147-195
    • Magzoub, M.1    Graslund, A.2
  • 18
    • 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
  • 19
    • 50949115801 scopus 로고    scopus 로고
    • PTD-modified ATTEMPTS system for enhanced asparaginase therapy: A proof-of-concept investigation
    • Y.M. Kwon, Y.T. Li, J.F. Liang, Y.J. Park, L.C. Chang, and V.C. Yang PTD-modified ATTEMPTS system for enhanced asparaginase therapy: a proof-of-concept investigation J. Control. Release 130 2008 252 258
    • (2008) J. Control. Release , vol.130 , pp. 252-258
    • Kwon, Y.M.1    Li, Y.T.2    Liang, J.F.3    Park, Y.J.4    Chang, L.C.5    Yang, V.C.6
  • 20
    • 24644512176 scopus 로고    scopus 로고
    • Nontoxic membrane translocation peptide from protamine, low molecular weight protamine (LMWP), for enhanced intracellular protein delivery: In vitro and in vivo study
    • DOI 10.1096/fj.04-2322fje
    • Y.J. Park, L.C. Chang, J.F. Liang, C. Moon, C.P. Chung, and V.C. Yang Nontoxic membrane translocation peptide from protamine, low molecular weight protamine (LMWP), for enhanced intracellular protein delivery: in vitro and in vivo study FASEB J. 19 2005 1555 1557 (Pubitemid 41279029)
    • (2005) FASEB Journal , vol.19 , Issue.11 , pp. 1555-1557
    • Park, Y.J.1    Chang, L.-C.2    Liang, J.F.3    Moon, C.4    Chung, C.-P.5    Yang, V.C.6
  • 21
    • 84866165950 scopus 로고    scopus 로고
    • The effect of epidermal growth factor (EGF) conjugated with low-molecular-weight protamine (LMWP) on wound healing of the skin
    • J.K. Choi, J.H. Jang, W.H. Jang, J. Kim, I.H. Bae, J. Bae, Y.H. Park, B.J. Kim, K.M. Lim, and J.W. Park The effect of epidermal growth factor (EGF) conjugated with low-molecular-weight protamine (LMWP) on wound healing of the skin Biomaterials 33 2012 8579 8590
    • (2012) Biomaterials , vol.33 , pp. 8579-8590
    • Choi, J.K.1    Jang, J.H.2    Jang, W.H.3    Kim, J.4    Bae, I.H.5    Bae, J.6    Park, Y.H.7    Kim, B.J.8    Lim, K.M.9    Park, J.W.10
  • 22
    • 80054088405 scopus 로고    scopus 로고
    • Low molecular weight protamine-functionalized nanoparticles for drug delivery to the brain after intranasal administration
    • H. Xia, X. Gao, G. Gu, Z. Liu, N. Zeng, Q. Hu, Q. Song, L. Yao, Z. Pang, X. Jiang, J. Chen, and H. Chen Low molecular weight protamine-functionalized nanoparticles for drug delivery to the brain after intranasal administration Biomaterials 32 2011 9888 9898
    • (2011) Biomaterials , vol.32 , pp. 9888-9898
    • Xia, H.1    Gao, X.2    Gu, G.3    Liu, Z.4    Zeng, N.5    Hu, Q.6    Song, Q.7    Yao, L.8    Pang, Z.9    Jiang, X.10    Chen, J.11    Chen, H.12
  • 24
    • 77953811833 scopus 로고    scopus 로고
    • Specific down regulation of 3T3-L1 adipocyte differentiation by cell-permeable antisense HIF1alpha-oligonucleotide
    • Y.S. Park, Y. Huang, Y.J. Park, A.E. David, L. White, H. He, H.S. Chung, and V.C. Yang Specific down regulation of 3T3-L1 adipocyte differentiation by cell-permeable antisense HIF1alpha-oligonucleotide J. Control. Release 144 2010 82 90
    • (2010) J. Control. Release , vol.144 , pp. 82-90
    • Park, Y.S.1    Huang, Y.2    Park, Y.J.3    David, A.E.4    White, L.5    He, H.6    Chung, H.S.7    Yang, V.C.8
  • 25
    • 0011967676 scopus 로고    scopus 로고
    • Low molecular weight protamine (LMWP) as nontoxic heparin/low molecular weight heparin antidote (I): Preparation and characterization
    • L.C. Chang, H.F. Lee, Z. Yang, and V.C. Yang Low molecular weight protamine (LMWP) as nontoxic heparin/low molecular weight heparin antidote (I): preparation and characterization AAPS PharmSci 3 2001 E17
    • (2001) AAPS PharmSci , vol.3 , pp. 17
    • Chang, L.C.1    Lee, H.F.2    Yang, Z.3    Yang, V.C.4
  • 26
    • 0035783151 scopus 로고    scopus 로고
    • Low molecular weight protamine (LMWP) as nontoxic heparin/low molecular weight heparin antidote (II): In vitro evaluation of efficacy and toxicity
    • L.C. Chang, J.F. Liang, H.F. Lee, L.M. Lee, and V.C. Yang Low molecular weight protamine (LMWP) as nontoxic heparin/low molecular weight heparin antidote (II): in vitro evaluation of efficacy and toxicity AAPS PharmSci 3 2001 E18
    • (2001) AAPS PharmSci , vol.3 , pp. 18
    • Chang, L.C.1    Liang, J.F.2    Lee, H.F.3    Lee, L.M.4    Yang, V.C.5
  • 27
    • 0035783265 scopus 로고    scopus 로고
    • Low molecular weight protamine as nontoxic heparin/low molecular weight heparin antidote (III): Preliminary in vivo evaluation of efficacy and toxicity using a canine model
    • L.M. Lee, L.C. Chang, S. Wrobleski, T.W. Wakefield, and V.C. Yang Low molecular weight protamine as nontoxic heparin/low molecular weight heparin antidote (III): preliminary in vivo evaluation of efficacy and toxicity using a canine model AAPS PharmSci 3 2001 E19
    • (2001) AAPS PharmSci , vol.3 , pp. 19
    • Lee, L.M.1    Chang, L.C.2    Wrobleski, S.3    Wakefield, T.W.4    Yang, V.C.5
  • 28
    • 32644474374 scopus 로고    scopus 로고
    • Novel immunotoxin: A fusion protein consisting of gelonin and an acetylcholine receptor fragment as a potential immunotherapeutic agent for the treatment of Myasthenia gravis
    • DOI 10.1016/j.pep.2005.08.029, PII S1046592805002871
    • M. Hossann, Z. Li, Y. Shi, U. Kreilinger, J. Buttner, P.D. Vogel, J. Yuan, J.G. Wise, and W.E. Trommer Novel immunotoxin: a fusion protein consisting of gelonin and an acetylcholine receptor fragment as a potential immunotherapeutic agent for the treatment of Myasthenia gravis Protein Expr. Purif. 46 2006 73 84 (Pubitemid 43246998)
    • (2006) Protein Expression and Purification , vol.46 , Issue.1 , pp. 73-84
    • Hossann, M.1    Li, Z.2    Shi, Y.3    Kreilinger, U.4    Buttner, J.5    Vogel, P.D.6    Yuan, J.7    Wise, J.G.8    Trommer, W.E.9
  • 29
    • 76649094549 scopus 로고    scopus 로고
    • Physiologically based pharmacokinetic model for T84.66: A monoclonal anti-CEA antibody
    • S.R. Urva, V.C. Yang, and J.P. Balthasar Physiologically based pharmacokinetic model for T84.66: a monoclonal anti-CEA antibody J. Pharm. Sci. 99 2010 1582 1600
    • (2010) J. Pharm. Sci. , vol.99 , pp. 1582-1600
    • Urva, S.R.1    Yang, V.C.2    Balthasar, J.P.3
  • 30
    • 0026602040 scopus 로고
    • Interaction of gelonin with macrophages: Effect of lysosomotropic amines
    • S. Madan, and P.C. Ghosh Interaction of gelonin with macrophages: effect of lysosomotropic amines Exp. Cell Res. 198 1992 52 58
    • (1992) Exp. Cell Res. , vol.198 , pp. 52-58
    • Madan, S.1    Ghosh, P.C.2
  • 31
    • 0347926091 scopus 로고    scopus 로고
    • Drug delivery strategy utilizing conjugation via reversible disulfide linkages: Role and site of cellular reducing activities
    • DOI 10.1016/S0169-409X(02)00179-5, PII S0169409X02001795
    • G. Saito, J.A. Swanson, and K.D. Lee Drug delivery strategy utilizing conjugation via reversible disulfide linkages: role and site of cellular reducing activities Adv. Drug Deliv. Rev. 55 2003 199 215 (Pubitemid 36135916)
    • (2003) Advanced Drug Delivery Reviews , vol.55 , Issue.2 , pp. 199-215
    • Saito, G.1    Swanson, J.A.2    Lee, K.-D.3
  • 32
    • 1542609485 scopus 로고    scopus 로고
    • Transduction peptides: From technology to physiology
    • DOI 10.1038/ncb0304-189
    • A. Joliot, and A. Prochiantz Transduction peptides: from technology to physiology Nat. Cell Biol. 6 2004 189 196 (Pubitemid 38344356)
    • (2004) Nature Cell Biology , vol.6 , Issue.3 , pp. 189-196
    • Joliot, A.1    Prochiantz, A.2
  • 33
    • 84860707029 scopus 로고    scopus 로고
    • Cell permeable cocaine esterases constructed by chemical conjugation and genetic recombination
    • T.Y. Lee, Y.S. Park, G.A. Garcia, R.K. Sunahara, J.H. Woods, and V.C. Yang Cell permeable cocaine esterases constructed by chemical conjugation and genetic recombination Mol. Pharm. 9 2012 1361 1373
    • (2012) Mol. Pharm. , vol.9 , pp. 1361-1373
    • Lee, T.Y.1    Park, Y.S.2    Garcia, G.A.3    Sunahara, R.K.4    Woods, J.H.5    Yang, V.C.6
  • 34
    • 0030904245 scopus 로고    scopus 로고
    • A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus
    • DOI 10.1074/jbc.272.25.16010
    • E. Vives, P. Brodin, and B. Lebleu A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus J. Biol. Chem. 272 1997 16010 16017 (Pubitemid 27265584)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.25 , pp. 16010-16017
    • Vives, E.1    Brodin, P.2    Lebleu, B.3
  • 35
    • 82755194760 scopus 로고    scopus 로고
    • Protein transduction domain delivery of therapeutic macromolecules
    • A. van den Berg, and S.F. Dowdy Protein transduction domain delivery of therapeutic macromolecules Curr. Opin. Biotechnol. 22 2011 888 893
    • (2011) Curr. Opin. Biotechnol. , vol.22 , pp. 888-893
    • Van Den Berg, A.1    Dowdy, S.F.2
  • 36
    • 33748433244 scopus 로고    scopus 로고
    • Cell-penetrating peptides as vectors for peptide, protein and oligonucleotide delivery
    • DOI 10.1016/j.coph.2006.04.004, PII S1471489206001251, Anti-infectives/New Technologies
    • M. Mae, and U. Langel Cell-penetrating peptides as vectors for peptide, protein and oligonucleotide delivery Curr. Opin. Pharmacol. 6 2006 509 514 (Pubitemid 44340662)
    • (2006) Current Opinion in Pharmacology , vol.6 , Issue.5 , pp. 509-514
    • Mae, M.1    Langel, U.2
  • 37
    • 0022355089 scopus 로고
    • Purified immunotoxins that are reactive with human lymphoid cells. Monoclonal antibodies conjugated to the ribosome-inactivating proteins gelonin and the pokeweed antiviral proteins
    • J.M. Lambert, P.D. Senter, A. Yau-Young, W.A. Blattler, and V.S. Goldmacher Purified immunotoxins that are reactive with human lymphoid cells. Monoclonal antibodies conjugated to the ribosome-inactivating proteins gelonin and the pokeweed antiviral proteins J. Biol. Chem. 260 1985 12035 12041 (Pubitemid 16228361)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.22 , pp. 12035-12041
    • Lambert, J.M.1    Senter, P.D.2    Yau-Young, A.3
  • 38
    • 0028002716 scopus 로고
    • Preparation and characterization of interleukin-2-gelonin conjugates made using different cross-linking reagents
    • G.D. McIntyre, C.F. Scott Jr., J. Ritz, W.A. Blattler, and J.M. Lambert Preparation and characterization of interleukin-2-gelonin conjugates made using different cross-linking reagents Bioconjug. Chem. 5 1994 88 97 (Pubitemid 2043895)
    • (1994) Bioconjugate Chemistry , vol.5 , Issue.1 , pp. 88-97
    • McIntyre, G.D.1    Scott Jnr, C.F.2    Ritz, J.3    Blattler, W.A.4    Lambert, J.M.5
  • 39
    • 0015874433 scopus 로고
    • Methyl 4-mercaptobutyrimidate as a cleavable cross-linking reagent and its application to the Escherichia coli 30S ribosome
    • R.R. Traut, A. Bollen, T.T. Sun, J.W. Hershey, J. Sundberg, and L.R. Pierce Methyl 4-mercaptobutyrimidate as a cleavable cross-linking reagent and its application to the Escherichia coli 30S ribosome Biochemistry 12 1973 3266 3273
    • (1973) Biochemistry , vol.12 , pp. 3266-3273
    • Traut, R.R.1    Bollen, A.2    Sun, T.T.3    Hershey, J.W.4    Sundberg, J.5    Pierce, L.R.6
  • 41
    • 0028804911 scopus 로고
    • Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli
    • J.F. Kane Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli Curr. Opin. Biotechnol. 6 1995 494 500
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 494-500
    • Kane, J.F.1
  • 42
    • 0037208812 scopus 로고    scopus 로고
    • Thioredoxin and related proteins as multifunctional fusion tags for soluble expression in E coli
    • E.R. LaVallie, E.A. DiBlasio-Smith, L.A. Collins-Racie, Z. Lu, and J.M. McCoy Thioredoxin and related proteins as multifunctional fusion tags for soluble expression in E. coli Methods Mol. Biol. 205 2003 119 140
    • (2003) Methods Mol. Biol. , vol.205 , pp. 119-140
    • Lavallie, E.R.1    Diblasio-Smith, E.A.2    Collins-Racie, L.A.3    Lu, Z.4    McCoy, J.M.5
  • 43
    • 19644389665 scopus 로고    scopus 로고
    • Solubihzation and refolding of bacterial inclusion body proteins
    • DOI 10.1263/jbb.99.303
    • S.M. Singh, and A.K. Panda Solubilization and refolding of bacterial inclusion body proteins J. Biosci. Bioeng. 99 2005 303 310 (Pubitemid 40740579)
    • (2005) Journal of Bioscience and Bioengineering , vol.99 , Issue.4 , pp. 303-310
    • Singh, S.M.1    Panda, A.K.2
  • 44
    • 0025492865 scopus 로고
    • Immunotoxin construction with a ribosome-inactivating protein from barley
    • R.F. Ebert, and L.A. Spryn Immunotoxin construction with a ribosome-inactivating protein from barley Bioconjug. Chem. 1 1990 331 336
    • (1990) Bioconjug. Chem. , vol.1 , pp. 331-336
    • Ebert, R.F.1    Spryn, L.A.2
  • 45
    • 0025071055 scopus 로고
    • Toxicity of, and histological lesions caused by, ribosome-inactivating proteins, their IgG-conjugates, and their homopolymers
    • M.G. Battelli, L. Barbieri, and F. Stirpe Toxicity of, and histological lesions caused by, ribosome-inactivating proteins, their IgG-conjugates, and their homopolymers APMIS 98 1990 585 593 (Pubitemid 20255566)
    • (1990) APMIS , vol.98 , Issue.7 , pp. 585-593
    • Battelli, M.G.1    Barbieri, L.2    Stirpe, F.3
  • 47
    • 0029067014 scopus 로고
    • Pharmacokinetics, tissue distribution, and in vivo antitumor effects of the antimelanoma immunotoxin ZME-gelonin
    • K. Mujoo, L. Cheung, J.L. Murray, and M.G. Rosenblum Pharmacokinetics, tissue distribution, and in vivo antitumor effects of the antimelanoma immunotoxin ZME-gelonin Cancer Immunol. Immunother. 40 1995 339 345
    • (1995) Cancer Immunol. Immunother. , vol.40 , pp. 339-345
    • Mujoo, K.1    Cheung, L.2    Murray, J.L.3    Rosenblum, M.G.4
  • 48
    • 33847130982 scopus 로고    scopus 로고
    • Truncations of gelonin lead to a reduction in its cytotoxicity
    • DOI 10.1016/j.tox.2006.11.074, PII S0300483X06007116, Includes Special Issue Section: Proceedings of the Joint Meeting of the British Toxicology Society and The In Vitro Toxicology Society and The UK NC3 Rs, University of York, UK, 14-15 Sept 2006
    • Z. Li, Y. Qu, H. Li, and J. Yuan Truncations of gelonin lead to a reduction in its cytotoxicity Toxicology 231 2007 129 136 (Pubitemid 46283156)
    • (2007) Toxicology , vol.231 , Issue.2-3 , pp. 129-136
    • Li, Z.1    Qu, Y.2    Li, H.3    Yuan, J.4
  • 49
    • 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


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