메뉴 건너뛰기




Volumn 11, Issue 5, 2010, Pages 1314-1325

Influence of surface functionality of poly(propylene imine) dendrimers on protease resistance and propagation of the scrapie prion protein

Author keywords

[No Author keywords available]

Indexed keywords

CELLULAR PRION PROTEINS; INFECTED CELLS; ISOFORMS; MALTOTRIOSE; MOLECULAR BASIS; NEUROBLASTOMAS; POLY(PROPYLENE IMINE); POLYAMINES; POLYAMINO; POSITIVELY CHARGED; PRION DISEASE; PRION PROTEIN; SURFACE FUNCTIONALITIES; SURFACE GROUPS; TIME-DEPENDENT;

EID: 77952160044     PISSN: 15257797     EISSN: 15264602     Source Type: Journal    
DOI: 10.1021/bm100101s     Document Type: Article
Times cited : (80)

References (69)
  • 1
    • 0029831213 scopus 로고    scopus 로고
    • Molecular analysis of prion strain variation and the aetiology of "new variant" CJD
    • Collinge, J.; Sidle, K. C.; Meads, J.; Ironside, J.; Hill, A. F. Molecular analysis of prion strain variation and the aetiology of "new variant" CJD Nature 1996, 383 (6602) 685-90
    • (1996) Nature , vol.383 , Issue.6602 , pp. 685-90
    • Collinge, J.1    Sidle, K.C.2    Meads, J.3    Ironside, J.4    Hill, A.F.5
  • 3
    • 0025991466 scopus 로고
    • The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive
    • Caughey, B.; Raymond, G. J. The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive J. Biol. Chem. 1991, 266 (27) 18217-23
    • (1991) J. Biol. Chem. , vol.266 , Issue.27 , pp. 18217-23
    • Caughey, B.1    Raymond, G.J.2
  • 4
    • 0025304678 scopus 로고
    • Scrapie and cellular prion proteins differ in their kinetics of synthesis and topology in cultured cells
    • Borchelt, D. R.; Scott, M.; Taraboulos, A.; Stahl, N.; Prusiner, S. B. Scrapie and cellular prion proteins differ in their kinetics of synthesis and topology in cultured cells J. Cell Biol. 1990, 110 (3) 743-52
    • (1990) J. Cell Biol. , vol.110 , Issue.3 , pp. 743-52
    • Borchelt, D.R.1    Scott, M.2    Taraboulos, A.3    Stahl, N.4    Prusiner, S.B.5
  • 5
    • 0021023167 scopus 로고
    • A protease-resistant protein is a structural component of the scrapie prion
    • McKinley, M. P.; Bolton, D. C.; Prusiner, S. B. A protease-resistant protein is a structural component of the scrapie prion Cell 1983, 35 (1) 57-62
    • (1983) Cell , vol.35 , Issue.1 , pp. 57-62
    • McKinley, M.P.1    Bolton, D.C.2    Prusiner, S.B.3
  • 6
    • 0020490156 scopus 로고
    • Identification of a protein that purifies with the scrapie prion
    • Bolton, D. C.; McKinley, M. P.; Prusiner, S. B. Identification of a protein that purifies with the scrapie prion Science 1982, 218 (4579) 1309-11
    • (1982) Science , vol.218 , Issue.4579 , pp. 1309-11
    • Bolton, D.C.1    McKinley, M.P.2    Prusiner, S.B.3
  • 7
    • 0025944507 scopus 로고
    • Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy
    • Caughey, B. W.; Dong, A.; Bhat, K. S.; Ernst, D.; Hayes, S. F.; Caughey, W. S. Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy Biochemistry 1991, 30 (31) 7672-80
    • (1991) Biochemistry , vol.30 , Issue.31 , pp. 7672-80
    • Caughey, B.W.1    Dong, A.2    Bhat, K.S.3    Ernst, D.4    Hayes, S.F.5    Caughey, W.S.6
  • 9
    • 0034916581 scopus 로고    scopus 로고
    • Prion diseases of humans and animals: Their causes and molecular basis
    • Collinge, J. Prion diseases of humans and animals: their causes and molecular basis Annu. Rev. Neurosci. 2001, 24, 519-50
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 519-50
    • Collinge, J.1
  • 10
    • 0024474822 scopus 로고
    • Diagnosis of Gerstmann-Straussler syndrome in familial dementia with prion protein gene analysis
    • Collinge, J.; Harding, A. E.; Owen, F.; Poulter, M.; Lofthouse, R.; Boughey, A. M.; Shah, T.; Crow, T. J. Diagnosis of Gerstmann-Straussler syndrome in familial dementia with prion protein gene analysis Lancet 1989, 2 (8653) 15-7
    • (1989) Lancet , vol.2 , Issue.8653 , pp. 15-7
    • Collinge, J.1    Harding, A.E.2    Owen, F.3    Poulter, M.4    Lofthouse, R.5    Boughey, A.M.6    Shah, T.7    Crow, T.J.8
  • 17
    • 0035902194 scopus 로고    scopus 로고
    • Shattuck lecture - Neurodegenerative diseases and prions
    • Prusiner, S. B. Shattuck lecture - neurodegenerative diseases and prions N. Engl. J. Med. 2001, 344 (20) 1516-26
    • (2001) N. Engl. J. Med. , vol.344 , Issue.20 , pp. 1516-26
    • Prusiner, S.B.1
  • 19
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner, S. B. Molecular biology of prion diseases Science 1991, 252 (5012) 1515-22
    • (1991) Science , vol.252 , Issue.5012 , pp. 1515-22
    • Prusiner, S.B.1
  • 20
    • 0032923522 scopus 로고    scopus 로고
    • Molecular genetics of transmissible spongiform encephalopathies
    • Weissmann, C. Molecular genetics of transmissible spongiform encephalopathies J. Biol. Chem. 1999, 274 (1) 3-6
    • (1999) J. Biol. Chem. , vol.274 , Issue.1 , pp. 3-6
    • Weissmann, C.1
  • 21
    • 0029066886 scopus 로고
    • Species specificity in the cell-free conversion of prion protein to protease-resistant forms: A model for the scrapie species barrier
    • Kocisko, D. A.; Priola, S. A.; Raymond, G. J.; Chesebro, B.; Lansbury, P. T., Jr.; Caughey, B. Species specificity in the cell-free conversion of prion protein to protease-resistant forms: a model for the scrapie species barrier Proc. Natl. Acad. Sci. U.S.A. 1995, 92 (9) 3923-7
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , Issue.9 , pp. 3923-7
    • Kocisko, D.A.1    Priola, S.A.2    Raymond, G.J.3    Chesebro, B.4    Lansbury Jr., P.T.5    Caughey, B.6
  • 23
    • 0347992944 scopus 로고    scopus 로고
    • Prion diseases: From molecular biology to intervention strategies
    • Nunziante, M.; Gilch, S.; Schatzl, H. M. Prion diseases: from molecular biology to intervention strategies ChemBioChem 2003, 4 (12) 1268-84
    • (2003) ChemBioChem , vol.4 , Issue.12 , pp. 1268-84
    • Nunziante, M.1    Gilch, S.2    Schatzl, H.M.3
  • 25
    • 21344445937 scopus 로고    scopus 로고
    • Molecular neurology of prion disease
    • Collinge, J. Molecular neurology of prion disease J. Neurol. Neurosurg. Psychiatry 2005, 76 (7) 906-19
    • (2005) J. Neurol. Neurosurg. Psychiatry , vol.76 , Issue.7 , pp. 906-19
    • Collinge, J.1
  • 26
    • 0342545936 scopus 로고    scopus 로고
    • Molecular pathogenesis of prion diseases
    • Kretzschmar, H. A. Molecular pathogenesis of prion diseases Eur. Arch. Psychiatry Clin. Neurosci. 1999, 249 (Suppl 3) 56-63
    • (1999) Eur. Arch. Psychiatry Clin. Neurosci. , vol.249 , Issue.SUPPL 3 , pp. 56-63
    • Kretzschmar, H.A.1
  • 29
    • 84989581991 scopus 로고
    • Cascade"- and "nonskid-chain-like" syntheses of molecular cavity topologies
    • Buhleier, E.; Wehner, W.; Vögtle, F. Cascade"- and "nonskid-chain-like" syntheses of molecular cavity topologies Synthesis 1978, 155-158
    • (1978) Synthesis , pp. 155-158
    • Buhleier, E.1    Wehner, W.2    Vögtle, F.3
  • 31
    • 33845378981 scopus 로고
    • Micelles. Part 1. Cascade molecules: A new approach to micelles. A [27]-arborol
    • Newkome, G. R.; Yao, Z.; Baker, G. R.; Gupta, V. K. Micelles. Part 1. Cascade molecules: a new approach to micelles. A [27]-arborol J. Org. Chem. 1985, 50 (11) 2003-2004
    • (1985) J. Org. Chem. , vol.50 , Issue.11 , pp. 2003-2004
    • Newkome, G.R.1    Yao, Z.2    Baker, G.R.3    Gupta, V.K.4
  • 33
    • 0036899037 scopus 로고    scopus 로고
    • Biological applications of dendrimers
    • Cloninger, M. J. Biological applications of dendrimers Curr. Opin. Chem. Biol. 2002, 6 (6) 742-8
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , Issue.6 , pp. 742-8
    • Cloninger, M.J.1
  • 34
    • 0037091001 scopus 로고    scopus 로고
    • Dendritic polymers in biomedical applications: From potential to clinical use in diagnostics and therapy
    • Stiriba, S. E.; Frey, H.; Haag, R. Dendritic polymers in biomedical applications: From potential to clinical use in diagnostics and therapy Angew. Chem., Int. Ed. 2002, 41, 1329-1334
    • (2002) Angew. Chem., Int. Ed. , vol.41 , pp. 1329-1334
    • Stiriba, S.E.1    Frey, H.2    Haag, R.3
  • 35
    • 1642414039 scopus 로고    scopus 로고
    • Dendrimers in drug research
    • Boas, U.; Heegaard, P. M. Dendrimers in drug research Chem. Soc. Rev. 2004, 33 (1) 43-63
    • (2004) Chem. Soc. Rev. , vol.33 , Issue.1 , pp. 43-63
    • Boas, U.1    Heegaard, P.M.2
  • 36
    • 12844258906 scopus 로고    scopus 로고
    • Dendrimers and dendritic polymers in drug delivery
    • Gillies, E. R.; Frechet, J. M. Dendrimers and dendritic polymers in drug delivery Drug Discovery Today 2005, 10 (1) 35-43
    • (2005) Drug Discovery Today , vol.10 , Issue.1 , pp. 35-43
    • Gillies, E.R.1    Frechet, J.M.2
  • 37
    • 28644434579 scopus 로고    scopus 로고
    • Designing dendrimers for biological applications
    • Lee, C. C.; MacKay, J. A.; Frechet, J. M.; Szoka, F. C. Designing dendrimers for biological applications Nat. Biotechnol. 2005, 23 (12) 1517-26
    • (2005) Nat. Biotechnol. , vol.23 , Issue.12 , pp. 1517-26
    • Lee, C.C.1    MacKay, J.A.2    Frechet, J.M.3    Szoka, F.C.4
  • 39
    • 36649016409 scopus 로고    scopus 로고
    • Guanidino- and urea-modified dendrimers as potent solubilizers of misfolded prion protein aggregates under non-cytotoxic conditions. Dependence on dendrimer generation and surface charge
    • Cordes, H.; Boas, U.; Olsen, P.; Heegaard, P. M. Guanidino- and urea-modified dendrimers as potent solubilizers of misfolded prion protein aggregates under non-cytotoxic conditions. Dependence on dendrimer generation and surface charge Biomacromolecules 2007, 8 (11) 3578-83
    • (2007) Biomacromolecules , vol.8 , Issue.11 , pp. 3578-83
    • Cordes, H.1    Boas, U.2    Olsen, P.3    Heegaard, P.M.4
  • 41
    • 2942613703 scopus 로고    scopus 로고
    • Transport of dendrimer nanocarriers through epithelial cells via the transcellular route
    • Jevprasesphant, R.; Penny, J.; Attwood, D.; D'Emanuele, A. Transport of dendrimer nanocarriers through epithelial cells via the transcellular route J. Controlled Release 2004, 97 (2) 259-67
    • (2004) J. Controlled Release , vol.97 , Issue.2 , pp. 259-67
    • Jevprasesphant, R.1    Penny, J.2    Attwood, D.3    D'emanuele, A.4
  • 42
    • 34848888660 scopus 로고    scopus 로고
    • Endocytosis and interaction of poly(amidoamine) dendrimers with Caco-2 cells
    • Kitchens, K. M.; Foraker, A. B.; Kolhatkar, R. B.; Swaan, P. W.; Ghandehari, H. Endocytosis and interaction of poly(amidoamine) dendrimers with Caco-2 cells Pharm. Res. 2007, 24 (11) 2138-45
    • (2007) Pharm. Res. , vol.24 , Issue.11 , pp. 2138-45
    • Kitchens, K.M.1    Foraker, A.B.2    Kolhatkar, R.B.3    Swaan, P.W.4    Ghandehari, H.5
  • 43
    • 0141867744 scopus 로고    scopus 로고
    • Transport mechanism(s) of poly(amidoamine) dendrimers across Caco-2 cell monolayers
    • El-Sayed, M.; Rhodes, C. A.; Ginski, M.; Ghandehari, H. Transport mechanism(s) of poly(amidoamine) dendrimers across Caco-2 cell monolayers Int. J. Pharm. 2003, 265 (1-2) 151-7
    • (2003) Int. J. Pharm. , vol.265 , Issue.1-2 , pp. 151-7
    • El-Sayed, M.1    Rhodes, C.A.2    Ginski, M.3    Ghandehari, H.4
  • 44
    • 46549084447 scopus 로고    scopus 로고
    • The effect of surface functionality on cellular trafficking of dendrimers
    • Perumal, O. P.; Inapagolla, R.; Kannan, S.; Kannan, R. M. The effect of surface functionality on cellular trafficking of dendrimers Biomaterials 2008, 29 (24-25) 3469-76
    • (2008) Biomaterials , vol.29 , Issue.24-25 , pp. 3469-76
    • Perumal, O.P.1    Inapagolla, R.2    Kannan, S.3    Kannan, R.M.4
  • 45
    • 42549146106 scopus 로고    scopus 로고
    • Endocytosis inhibitors prevent poly(amidoamine) dendrimer internalization and permeability across Caco-2 cells
    • Kitchens, K. M.; Kolhatkar, R. B.; Swaan, P. W.; Ghandehari, H. Endocytosis inhibitors prevent poly(amidoamine) dendrimer internalization and permeability across Caco-2 cells Mol. Pharm. 2008, 5 (2) 364-9
    • (2008) Mol. Pharm. , vol.5 , Issue.2 , pp. 364-9
    • Kitchens, K.M.1    Kolhatkar, R.B.2    Swaan, P.W.3    Ghandehari, H.4
  • 46
    • 28444448086 scopus 로고    scopus 로고
    • Influence of heparin and dendrimers on the aggregation of two amyloid peptides related to Alzheimer's and prion diseases
    • Klajnert, B.; Cortijo-Arellano, M.; Bryszewska, M.; Cladera, J. Influence of heparin and dendrimers on the aggregation of two amyloid peptides related to Alzheimer's and prion diseases Biochem. Biophys. Res. Commun. 2006, 339 (2) 577-82
    • (2006) Biochem. Biophys. Res. Commun. , vol.339 , Issue.2 , pp. 577-82
    • Klajnert, B.1    Cortijo-Arellano, M.2    Bryszewska, M.3    Cladera, J.4
  • 49
    • 53849139796 scopus 로고    scopus 로고
    • The influence of densely organized maltose shells on the biological properties of poly(propylene imine) dendrimers: New effects dependent on hydrogen bonding
    • Klajnert, B.; Appelhans, D.; Komber, H.; Morgner, N.; Schwarz, S.; Richter, S.; Brutschy, B.; Ionov, M.; Tonkikh, A. K.; Bryszewska, M.; Voit, B. The influence of densely organized maltose shells on the biological properties of poly(propylene imine) dendrimers: new effects dependent on hydrogen bonding Chem. Eur. J. 2008, 14 (23) 7030-41
    • (2008) Chem. Eur. J. , vol.14 , Issue.23 , pp. 7030-41
    • Klajnert, B.1    Appelhans, D.2    Komber, H.3    Morgner, N.4    Schwarz, S.5    Richter, S.6    Brutschy, B.7    Ionov, M.8    Tonkikh, A.K.9    Bryszewska, M.10    Voit, B.11
  • 50
    • 7544239102 scopus 로고    scopus 로고
    • Amyloid aggregates of the prion peptide PrP106-126 are destabilised by oxidation and by the action of dendrimers
    • Heegaard, P. M.; Pedersen, H. G.; Flink, J.; Boas, U. Amyloid aggregates of the prion peptide PrP106-126 are destabilised by oxidation and by the action of dendrimers FEBS Lett. 2004, 577 (1-2) 127-33
    • (2004) FEBS Lett. , vol.577 , Issue.1-2 , pp. 127-33
    • Heegaard, P.M.1    Pedersen, H.G.2    Flink, J.3    Boas, U.4
  • 53
    • 0033999635 scopus 로고    scopus 로고
    • Cultured cell sublines highly susceptible to prion infection
    • Bosque, P. J.; Prusiner, S. B. Cultured cell sublines highly susceptible to prion infection J. Virol. 2000, 74 (9) 4377-86
    • (2000) J. Virol. , vol.74 , Issue.9 , pp. 4377-86
    • Bosque, P.J.1    Prusiner, S.B.2
  • 54
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosmann, T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays J. Immunol. Methods 1983, 65 (1-2) 55-63
    • (1983) J. Immunol. Methods , vol.65 , Issue.1-2 , pp. 55-63
    • Mosmann, T.1
  • 56
    • 0030042315 scopus 로고    scopus 로고
    • Preliminary biological evaluation of polyamidoamine (PAMAM) Starburst dendrimers
    • Roberts, J. C.; Bhalgat, M. K.; Zera, R. T. Preliminary biological evaluation of polyamidoamine (PAMAM) Starburst dendrimers J. Biomed. Mater. Res. 1996, 30 (1) 53-65
    • (1996) J. Biomed. Mater. Res. , vol.30 , Issue.1 , pp. 53-65
    • Roberts, J.C.1    Bhalgat, M.K.2    Zera, R.T.3
  • 57
    • 0032212052 scopus 로고    scopus 로고
    • Biotin reagents for antibody pretargeting. 3. Synthesis, radioiodination, and evaluation of biotinylated starburst dendrimers
    • Wilbur, D. S.; Pathare, P. M.; Hamlin, D. K.; Buhler, K. R.; Vessella, R. L. Biotin reagents for antibody pretargeting. 3. Synthesis, radioiodination, and evaluation of biotinylated starburst dendrimers Bioconjugate Chem. 1998, 9 (6) 813-25
    • (1998) Bioconjugate Chem. , vol.9 , Issue.6 , pp. 813-25
    • Wilbur, D.S.1    Pathare, P.M.2    Hamlin, D.K.3    Buhler, K.R.4    Vessella, R.L.5
  • 58
    • 0034005436 scopus 로고    scopus 로고
    • Dendrimers: Relationship between structure and biocompatibility in vitro, and preliminary studies on the biodistribution of 125I-labelled polyamidoamine dendrimers in vivo
    • Malik, N.; Wiwattanapatapee, R.; Klopsch, R.; Lorenz, K.; Frey, H.; Weener, J. W.; Meijer, E. W.; Paulus, W.; Duncan, R. Dendrimers: relationship between structure and biocompatibility in vitro, and preliminary studies on the biodistribution of 125I-labelled polyamidoamine dendrimers in vivo J. Controlled Release 2000, 65 (1-2) 133-48
    • (2000) J. Controlled Release , vol.65 , Issue.1-2 , pp. 133-48
    • Malik, N.1    Wiwattanapatapee, R.2    Klopsch, R.3    Lorenz, K.4    Frey, H.5    Weener, J.W.6    Meijer, E.W.7    Paulus, W.8    Duncan, R.9
  • 59
    • 33751232325 scopus 로고    scopus 로고
    • Investigations on the toxicological profile of functionalized fifth-generation poly (propylene imine) dendrimer
    • Agashe, H. B.; Dutta, T.; Garg, M.; Jain, N. K. Investigations on the toxicological profile of functionalized fifth-generation poly (propylene imine) dendrimer J. Pharm. Pharmacol. 2006, 58 (11) 1491-8
    • (2006) J. Pharm. Pharmacol. , vol.58 , Issue.11 , pp. 1491-8
    • Agashe, H.B.1    Dutta, T.2    Garg, M.3    Jain, N.K.4
  • 61
    • 0032094708 scopus 로고    scopus 로고
    • Acid-base properties of poly(propylene imine) dendrimers
    • van Duijvenbode, R. C.; Borkovec, M.; Koper, G. J. M. Acid-base properties of poly(propylene imine) dendrimers Polymer 1998, 39 (12) 2657-2664
    • (1998) Polymer , vol.39 , Issue.12 , pp. 2657-2664
    • Van Duijvenbode, R.C.1    Borkovec, M.2    Koper, G.J.M.3
  • 62
    • 0030915989 scopus 로고    scopus 로고
    • Optimizing lectin-carbohydrate interactions: Improved binding of divalent alpha-mannosylated ligands towards Concanavalin A
    • Page, D.; Roy, R. Optimizing lectin-carbohydrate interactions: improved binding of divalent alpha-mannosylated ligands towards Concanavalin A Glycoconjugate J. 1997, 14 (3) 345-56
    • (1997) Glycoconjugate J. , vol.14 , Issue.3 , pp. 345-56
    • Page, D.1    Roy, R.2
  • 63
    • 47949127624 scopus 로고    scopus 로고
    • Trehalose impairs aggregation of PrPSc molecules and protects prion-infected cells against oxidative damage
    • Beranger, F.; Crozet, C.; Goldsborough, A.; Lehmann, S. Trehalose impairs aggregation of PrPSc molecules and protects prion-infected cells against oxidative damage Biochem. Biophys. Res. Commun. 2008, 374 (1) 44-8
    • (2008) Biochem. Biophys. Res. Commun. , vol.374 , Issue.1 , pp. 44-8
    • Beranger, F.1    Crozet, C.2    Goldsborough, A.3    Lehmann, S.4
  • 64
    • 35148878615 scopus 로고    scopus 로고
    • Cyclodextrins inhibit replication of scrapie prion protein in cell culture
    • Prior, M.; Lehmann, S.; Sy, M. S.; Molloy, B.; McMahon, H. E. Cyclodextrins inhibit replication of scrapie prion protein in cell culture J. Virol. 2007, 81 (20) 11195-207
    • (2007) J. Virol. , vol.81 , Issue.20 , pp. 11195-207
    • Prior, M.1    Lehmann, S.2    Sy, M.S.3    Molloy, B.4    McMahon, H.E.5
  • 65
    • 34548133091 scopus 로고    scopus 로고
    • Dendrimer effects on peptide and protein fibrillation
    • Heegaard, P. M.; Boas, U.; Otzen, D. E. Dendrimer effects on peptide and protein fibrillation Macromol. Biosci. 2007, 7 (8) 1047-59
    • (2007) Macromol. Biosci. , vol.7 , Issue.8 , pp. 1047-59
    • Heegaard, P.M.1    Boas, U.2    Otzen, D.E.3
  • 68
    • 14544280704 scopus 로고    scopus 로고
    • Approaches to therapy of prion diseases
    • Weissmann, C.; Aguzzi, A. Approaches to therapy of prion diseases Annu. Rev. Med. 2005, 56, 321-44
    • (2005) Annu. Rev. Med. , vol.56 , pp. 321-44
    • Weissmann, C.1    Aguzzi, A.2
  • 69
    • 39749200864 scopus 로고    scopus 로고
    • Methotrexate loaded polyether-copolyester dendrimers for the treatment of gliomas: Enhanced efficacy and intratumoral transport capability
    • Dhanikula, R. S.; Argaw, A.; Bouchard, J. F.; Hildgen, P. Methotrexate loaded polyether-copolyester dendrimers for the treatment of gliomas: enhanced efficacy and intratumoral transport capability Mol. Pharm. 2008, 5 (1) 105-16
    • (2008) Mol. Pharm. , vol.5 , Issue.1 , pp. 105-16
    • Dhanikula, R.S.1    Argaw, A.2    Bouchard, J.F.3    Hildgen, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.