메뉴 건너뛰기




Volumn 147, Issue 2, 2010, Pages 269-277

An ultrasound-responsive nano delivery system of tissue-type plasminogen activator for thrombolytic therapy

Author keywords

Gelatin; Polyethylene glycol; T PA; Thrombolytic therapy; Ultrasound

Indexed keywords

BIOLOGICAL ACTIVITIES; BLOOD CIRCULATION; BODY DISTRIBUTIONS; CATIONIZED; DELIVERY SYSTEMS; ETHYLENE DIAMINE; GELATIN; IN-VITRO; INTRAVENOUS ADMINISTRATION; NANO-DELIVERY SYSTEMS; NANO-SIZED; POLYETHYLENE GLYCOLS (PEG); RECANALIZATION; T-PA; THROMBOLYTIC; TISSUE-TYPE PLASMINOGEN ACTIVATOR; ULTRASOUND; ULTRASOUND IRRADIATION;

EID: 77957020900     PISSN: 01683659     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jconrel.2010.07.127     Document Type: Article
Times cited : (96)

References (82)
  • 1
    • 17444392120 scopus 로고    scopus 로고
    • Fibrinogen and fibrin
    • Weisel J.W. Fibrinogen and fibrin. Adv. Protein Chem. 2005, 70:247-299.
    • (2005) Adv. Protein Chem. , vol.70 , pp. 247-299
    • Weisel, J.W.1
  • 2
    • 28344448202 scopus 로고    scopus 로고
    • Fibrinogen and fibrin structure and functions
    • Mosesson M.W. Fibrinogen and fibrin structure and functions. J. Thromb. Haemost. 2005, 3:1894-1904.
    • (2005) J. Thromb. Haemost. , vol.3 , pp. 1894-1904
    • Mosesson, M.W.1
  • 3
    • 0025266912 scopus 로고
    • Plasminogen activators: pharmacology and therapy
    • Holden R.W. Plasminogen activators: pharmacology and therapy. Radiology 1990, 174:993-1001.
    • (1990) Radiology , vol.174 , pp. 993-1001
    • Holden, R.W.1
  • 4
    • 85007755756 scopus 로고    scopus 로고
    • An overview of antithrombotic therapy
    • Blann A.D., Landray M.L., Lip G.Y. An overview of antithrombotic therapy. BMJ 2002, 325:762-765.
    • (2002) BMJ , vol.325 , pp. 762-765
    • Blann, A.D.1    Landray, M.L.2    Lip, G.Y.3
  • 5
    • 0029844320 scopus 로고    scopus 로고
    • The future of thrombolysis in the treatment of acute myocardial infarction
    • Bode C., Runge M.S., Smalling R.W. The future of thrombolysis in the treatment of acute myocardial infarction. Eur. Heart J. 1996, 17:55-60.
    • (1996) Eur. Heart J. , vol.17 , pp. 55-60
    • Bode, C.1    Runge, M.S.2    Smalling, R.W.3
  • 6
    • 0037180227 scopus 로고    scopus 로고
    • Venous thromboembolism: treatment strategies
    • Turpie A.G., Chin B.S., Lip G.Y. Venous thromboembolism: treatment strategies. BMJ 2002, 325:948-950.
    • (2002) BMJ , vol.325 , pp. 948-950
    • Turpie, A.G.1    Chin, B.S.2    Lip, G.Y.3
  • 7
    • 35648976623 scopus 로고    scopus 로고
    • Accelerating thrombolysis with chitosan-coated plasminogen activators encapsulated in poly-(lactide-co-glycolide) (PLGA) nanoparticles
    • Chung T.W., Wang S.S., Tsai W.J. Accelerating thrombolysis with chitosan-coated plasminogen activators encapsulated in poly-(lactide-co-glycolide) (PLGA) nanoparticles. Biomaterials 2008, 29:228-237.
    • (2008) Biomaterials , vol.29 , pp. 228-237
    • Chung, T.W.1    Wang, S.S.2    Tsai, W.J.3
  • 8
    • 33947325967 scopus 로고    scopus 로고
    • Ultrasound-facilitated thrombolysis using tissue-plasminogen activator-loaded echogenic liposomes
    • Tiukinhoy-Laing S.D., Huang S., Klegerman M., Holland C.K., McPherson D.D. Ultrasound-facilitated thrombolysis using tissue-plasminogen activator-loaded echogenic liposomes. Thromb. Res. 2007, 119:777-784.
    • (2007) Thromb. Res. , vol.119 , pp. 777-784
    • Tiukinhoy-Laing, S.D.1    Huang, S.2    Klegerman, M.3    Holland, C.K.4    McPherson, D.D.5
  • 10
    • 0028943185 scopus 로고
    • Thrombolytic treatment with tissue-type plasminogen activator (t-PA) containing liposomes in rabbits: a comparison with free t-PA
    • Heeremans J.L., Prevost R., Bekkers M.E., Los P., Emeis J.J., Kluft C., Crommelin D.J. Thrombolytic treatment with tissue-type plasminogen activator (t-PA) containing liposomes in rabbits: a comparison with free t-PA. Thromb. Haemost. 1995, 73:488-494.
    • (1995) Thromb. Haemost. , vol.73 , pp. 488-494
    • Heeremans, J.L.1    Prevost, R.2    Bekkers, M.E.3    Los, P.4    Emeis, J.J.5    Kluft, C.6    Crommelin, D.J.7
  • 12
    • 0037961999 scopus 로고    scopus 로고
    • Accelerated thrombolysis in a rabbit model of carotid artery thrombosis with liposome-encapsulated and microencapsulated streptokinase
    • Leach J.K., O'Rear E.A., Patterson E., Miao Y., Johnson A.E. Accelerated thrombolysis in a rabbit model of carotid artery thrombosis with liposome-encapsulated and microencapsulated streptokinase. Thromb. Haemost. 2003, 90:64-70.
    • (2003) Thromb. Haemost. , vol.90 , pp. 64-70
    • Leach, J.K.1    O'Rear, E.A.2    Patterson, E.3    Miao, Y.4    Johnson, A.E.5
  • 13
    • 0025261137 scopus 로고
    • Accelerated thrombolysis and reperfusion in a canine model of myocardial infarction by liposomal encapsulation of streptokinase
    • Nguyen P.D., O'Rear E.A., Johnson A.E., Patterson E., Whitsett T.L., Bhakta R. Accelerated thrombolysis and reperfusion in a canine model of myocardial infarction by liposomal encapsulation of streptokinase. Circ. Res. 1990, 66:875-878.
    • (1990) Circ. Res. , vol.66 , pp. 875-878
    • Nguyen, P.D.1    O'Rear, E.A.2    Johnson, A.E.3    Patterson, E.4    Whitsett, T.L.5    Bhakta, R.6
  • 14
    • 33646701192 scopus 로고    scopus 로고
    • Thrombus localization by using streptokinase containing vesicular systems
    • Erdoǧan S., Ozer A.Y., Volkan B., Caner B., Bilgili H. Thrombus localization by using streptokinase containing vesicular systems. Drug Deliv. 2006, 13:303-309.
    • (2006) Drug Deliv. , vol.13 , pp. 303-309
    • Erdoǧan, S.1    Ozer, A.Y.2    Volkan, B.3    Caner, B.4    Bilgili, H.5
  • 15
    • 68549092406 scopus 로고    scopus 로고
    • The use of PEGylated liposomes to prolong circulation lifetimes of tissue plasminogen activator
    • Kim J.Y., Kim J.K., Park J.S., Byun Y., Kim C.K. The use of PEGylated liposomes to prolong circulation lifetimes of tissue plasminogen activator. Biomaterials 2009, 30:5751-5756.
    • (2009) Biomaterials , vol.30 , pp. 5751-5756
    • Kim, J.Y.1    Kim, J.K.2    Park, J.S.3    Byun, Y.4    Kim, C.K.5
  • 18
    • 34250184500 scopus 로고    scopus 로고
    • Identification and characterization of Harobin, a novel fibrino(geno)lytic serine protease from a sea snake (Lapemis hardwickii)
    • He J., Chen S., Gu J. Identification and characterization of Harobin, a novel fibrino(geno)lytic serine protease from a sea snake (Lapemis hardwickii). FEBS Lett. 2007, 581:2965-2973.
    • (2007) FEBS Lett. , vol.581 , pp. 2965-2973
    • He, J.1    Chen, S.2    Gu, J.3
  • 19
    • 22244493880 scopus 로고    scopus 로고
    • Biochemical and molecular modeling analysis of the ability of two p-aminobenzamidine-based sorbents to selectively purify serine proteases (fibrinogenases) from snake venoms
    • De-Simone S.G., Correa-Netto C., Antunes O.A., De-Alencastro R.B., Silva F.P. Biochemical and molecular modeling analysis of the ability of two p-aminobenzamidine-based sorbents to selectively purify serine proteases (fibrinogenases) from snake venoms. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 2005, 822:1-9.
    • (2005) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.822 , pp. 1-9
    • De-Simone, S.G.1    Correa-Netto, C.2    Antunes, O.A.3    De-Alencastro, R.B.4    Silva, F.P.5
  • 20
    • 1642411066 scopus 로고    scopus 로고
    • Purification and characterization of a serine protease with fibrinolytic activity from dung beetles, Catharsius molossus
    • Ahn M.Y., Hahn B.S., Ryu K.S., Kim J.W., Kim I., Kim Y.S. Purification and characterization of a serine protease with fibrinolytic activity from dung beetles, Catharsius molossus. Thromb. Res. 2003, 112:339-347.
    • (2003) Thromb. Res. , vol.112 , pp. 339-347
    • Ahn, M.Y.1    Hahn, B.S.2    Ryu, K.S.3    Kim, J.W.4    Kim, I.5    Kim, Y.S.6
  • 21
    • 0026590461 scopus 로고
    • Fibrinolysis relating substances in marine creatures
    • Sumi H., Nakajima N., Mihara H. Fibrinolysis relating substances in marine creatures. Comp. Biochem. Physiol. B 1992, 102:163-167.
    • (1992) Comp. Biochem. Physiol. B , vol.102 , pp. 163-167
    • Sumi, H.1    Nakajima, N.2    Mihara, H.3
  • 22
    • 0023656415 scopus 로고
    • A novel fibrinolytic enzyme (nattokinase) in the vegetable cheese Natto; a typical and popular soybean food in the Japanese diet
    • Sumi H., Hamada H., Tsushima H., Mihara H., Muraki H. A novel fibrinolytic enzyme (nattokinase) in the vegetable cheese Natto; a typical and popular soybean food in the Japanese diet. Experientia 1987, 43:1110-1111.
    • (1987) Experientia , vol.43 , pp. 1110-1111
    • Sumi, H.1    Hamada, H.2    Tsushima, H.3    Mihara, H.4    Muraki, H.5
  • 23
    • 0025134853 scopus 로고
    • Enhancement of the fibrinolytic activity in plasma by oral administration of nattokinase
    • Sumi H., Hamada H., Nakanishi K., Hiratani H. Enhancement of the fibrinolytic activity in plasma by oral administration of nattokinase. Acta Haematol. 1990, 84:139-143.
    • (1990) Acta Haematol. , vol.84 , pp. 139-143
    • Sumi, H.1    Hamada, H.2    Nakanishi, K.3    Hiratani, H.4
  • 24
    • 0027741228 scopus 로고
    • Purification and characterization of a strong fibrinolytic enzyme (nattokinase) in the vegetable cheese Natto, a popular soybean fermented food in Japan
    • Fujita M., Nomura K., Hong K., Ito Y., Asada A., Nishimuro S. Purification and characterization of a strong fibrinolytic enzyme (nattokinase) in the vegetable cheese Natto, a popular soybean fermented food in Japan. Biochem. Biophys. Res. Commun. 1993, 197:1340-1347.
    • (1993) Biochem. Biophys. Res. Commun. , vol.197 , pp. 1340-1347
    • Fujita, M.1    Nomura, K.2    Hong, K.3    Ito, Y.4    Asada, A.5    Nishimuro, S.6
  • 25
    • 0028786992 scopus 로고
    • Thrombolytic effect of nattokinase on a chemically induced thrombosis model in rat
    • Fujita M., Hong K., Ito Y., Fujii R., Kariya K., Nishimuro S. Thrombolytic effect of nattokinase on a chemically induced thrombosis model in rat. Biol. Pharm. Bull. 1995, 18:1387-1391.
    • (1995) Biol. Pharm. Bull. , vol.18 , pp. 1387-1391
    • Fujita, M.1    Hong, K.2    Ito, Y.3    Fujii, R.4    Kariya, K.5    Nishimuro, S.6
  • 26
    • 0029960565 scopus 로고    scopus 로고
    • Purification and characterization of a fibrinolytic enzyme produced from Bacillus sp. strain CK 11-4 screened from Chungkook-Jang
    • Kim W., Choi K., Kim Y., Park H., Choi J., Lee Y., Oh H., Kwon I., Lee S. Purification and characterization of a fibrinolytic enzyme produced from Bacillus sp. strain CK 11-4 screened from Chungkook-Jang. Appl. Environ. Microbiol. 1996, 62:2482-2488.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2482-2488
    • Kim, W.1    Choi, K.2    Kim, Y.3    Park, H.4    Choi, J.5    Lee, Y.6    Oh, H.7    Kwon, I.8    Lee, S.9
  • 27
    • 36148973934 scopus 로고    scopus 로고
    • The fibrinolytic activity of a novel protease derived from a tempeh producing fungus, Fusarium sp. BLB
    • Sugimoto S., Fujii T., Morimiya T., Johdo O., Nakamura T. The fibrinolytic activity of a novel protease derived from a tempeh producing fungus, Fusarium sp. BLB. Biosci. Biotechnol. Biochem. 2007, 71:2184-2189.
    • (2007) Biosci. Biotechnol. Biochem. , vol.71 , pp. 2184-2189
    • Sugimoto, S.1    Fujii, T.2    Morimiya, T.3    Johdo, O.4    Nakamura, T.5
  • 28
    • 52949120292 scopus 로고    scopus 로고
    • Improvement of the stability of nattokinase using γ-polyglutamic acid as a coating material for microencapsulation
    • Hsieh C.-W., Lu W.-C., Hsieh W.-C., Huang Y.-P., Lai C.-H., Ko W.-C. Improvement of the stability of nattokinase using γ-polyglutamic acid as a coating material for microencapsulation. LWT - Food Sci. Technol. Bull. 2009, 42:144-149.
    • (2009) LWT - Food Sci. Technol. Bull. , vol.42 , pp. 144-149
    • Hsieh, C.-W.1    Lu, W.-C.2    Hsieh, W.-C.3    Huang, Y.-P.4    Lai, C.-H.5    Ko, W.-C.6
  • 29
    • 34249317625 scopus 로고    scopus 로고
    • Stabilization and target delivery of Nattokinase using compression coating
    • Law D., Zhang Z. Stabilization and target delivery of Nattokinase using compression coating. Drug Dev. Ind. Pharm. 2007, 33:495-503.
    • (2007) Drug Dev. Ind. Pharm. , vol.33 , pp. 495-503
    • Law, D.1    Zhang, Z.2
  • 30
    • 34547941484 scopus 로고    scopus 로고
    • Stabilisation and targeted delivery of a fibrinolytic enzyme (nattokinase) by shellac
    • Law D., Zhang Z. Stabilisation and targeted delivery of a fibrinolytic enzyme (nattokinase) by shellac. Minerva Biotecnol. 2007, 19:17-26.
    • (2007) Minerva Biotecnol. , vol.19 , pp. 17-26
    • Law, D.1    Zhang, Z.2
  • 31
    • 65449148821 scopus 로고    scopus 로고
    • Mammalian cell penetration, siRNA transfection, and DNA transfection by supercharged proteins
    • McNaughton B.R., Cronican J.J., Thompson D.B., Liu D.R. Mammalian cell penetration, siRNA transfection, and DNA transfection by supercharged proteins. Proc. Nat. Acad. Sci. U.S.A. 2009, 106:6111-6116.
    • (2009) Proc. Nat. Acad. Sci. U.S.A. , vol.106 , pp. 6111-6116
    • McNaughton, B.R.1    Cronican, J.J.2    Thompson, D.B.3    Liu, D.R.4
  • 33
    • 43349096262 scopus 로고    scopus 로고
    • Complexation of a poly-l-arginine with low molecular weight heparin enhances pulmonary absorption of the drug
    • Rawat A., Yang T., Hussain A., Ahsan F. Complexation of a poly-l-arginine with low molecular weight heparin enhances pulmonary absorption of the drug. Pharm. Res. 2008, 25:936-948.
    • (2008) Pharm. Res. , vol.25 , pp. 936-948
    • Rawat, A.1    Yang, T.2    Hussain, A.3    Ahsan, F.4
  • 34
    • 77149174799 scopus 로고    scopus 로고
    • Effect of amine type on the expression of plasmid DNA by cationized dextran
    • Jo J., Nagane K., Yamamoto M., Tabata Y. Effect of amine type on the expression of plasmid DNA by cationized dextran. J. Biomater. Sci. Polym. Ed. 2010, 21:225-236.
    • (2010) J. Biomater. Sci. Polym. Ed. , vol.21 , pp. 225-236
    • Jo, J.1    Nagane, K.2    Yamamoto, M.3    Tabata, Y.4
  • 35
    • 75149167354 scopus 로고    scopus 로고
    • Dendrimer nanocarriers as versatile vectors in gene delivery
    • Dutta T., Jain N.K., McMillan N.A., Parekh H.S. Dendrimer nanocarriers as versatile vectors in gene delivery. Nanomedicine 2010, 6:25-34.
    • (2010) Nanomedicine , vol.6 , pp. 25-34
    • Dutta, T.1    Jain, N.K.2    McMillan, N.A.3    Parekh, H.S.4
  • 36
    • 77953609568 scopus 로고    scopus 로고
    • Targeting anticancer drugs to tumor vasculature using cationic liposomes
    • Abu Lila S., Ishida T., Kiwada H. Targeting anticancer drugs to tumor vasculature using cationic liposomes. Pharm. Res. 2010, 27:1171-1183.
    • (2010) Pharm. Res. , vol.27 , pp. 1171-1183
    • Abu Lila, S.1    Ishida, T.2    Kiwada, H.3
  • 37
    • 0038497548 scopus 로고
    • The physical chemistry of gelatin
    • Veis A. The physical chemistry of gelatin. Int. Rev. Connect. Tissue Res. 1965, 3:113-200.
    • (1965) Int. Rev. Connect. Tissue Res. , vol.3 , pp. 113-200
    • Veis, A.1
  • 38
    • 0032482156 scopus 로고    scopus 로고
    • Protein release from gelatin matrices
    • Ikada Y., Tabata Y. Protein release from gelatin matrices. Adv. Drug Deliv. Rev. 1998, 31:287-301.
    • (1998) Adv. Drug Deliv. Rev. , vol.31 , pp. 287-301
    • Ikada, Y.1    Tabata, Y.2
  • 39
    • 0031835259 scopus 로고    scopus 로고
    • Ectopic bone formation induced by biodegradable hydrogels incorporating bone morphogenetic protein
    • Yamamoto M., Tabata Y., Ikada Y. Ectopic bone formation induced by biodegradable hydrogels incorporating bone morphogenetic protein. J. Biomater. Sci. Polym. Ed. 1998, 9:439-458.
    • (1998) J. Biomater. Sci. Polym. Ed. , vol.9 , pp. 439-458
    • Yamamoto, M.1    Tabata, Y.2    Ikada, Y.3
  • 40
    • 0033985633 scopus 로고    scopus 로고
    • Bone regeneration by transforming growth factor beta1 released from a biodegradable hydrogel
    • Yamamoto M., Tabata Y., Hong L., Miyamoto S., Hashimoto N., Ikada Y. Bone regeneration by transforming growth factor beta1 released from a biodegradable hydrogel. J. Control. Release 2000, 64:133-142.
    • (2000) J. Control. Release , vol.64 , pp. 133-142
    • Yamamoto, M.1    Tabata, Y.2    Hong, L.3    Miyamoto, S.4    Hashimoto, N.5    Ikada, Y.6
  • 41
    • 0035692862 scopus 로고    scopus 로고
    • Controlled release of hepatocyte growth factor from gelatin hydrogels based on hydrogel degradation
    • Ozeki M., Ishii T., Hirano Y., Tabata Y. Controlled release of hepatocyte growth factor from gelatin hydrogels based on hydrogel degradation. J. Drug Target. 2001, 9:461-471.
    • (2001) J. Drug Target. , vol.9 , pp. 461-471
    • Ozeki, M.1    Ishii, T.2    Hirano, Y.3    Tabata, Y.4
  • 42
    • 3242715129 scopus 로고    scopus 로고
    • Suppression of the progress of disseminated pancreatic cancer cells by NK4 plasmid DNA released from cationized gelatin microspheres
    • Kushibiki T., Matsumoto K., Nakamura T., Tabata Y. Suppression of the progress of disseminated pancreatic cancer cells by NK4 plasmid DNA released from cationized gelatin microspheres. Pharm. Res. 2004, 21:1109-1118.
    • (2004) Pharm. Res. , vol.21 , pp. 1109-1118
    • Kushibiki, T.1    Matsumoto, K.2    Nakamura, T.3    Tabata, Y.4
  • 43
    • 0344152902 scopus 로고    scopus 로고
    • Local delivery of matrix metalloproteinase gene prevents the onset of renal sclerosis in streptozotocin-induced diabetic mice
    • Aoyama T., Yamamoto S., Kanematsu A., Ogawa O., Tabata Y. Local delivery of matrix metalloproteinase gene prevents the onset of renal sclerosis in streptozotocin-induced diabetic mice. Tissue Eng. 2003, 9:1289-1299.
    • (2003) Tissue Eng. , vol.9 , pp. 1289-1299
    • Aoyama, T.1    Yamamoto, S.2    Kanematsu, A.3    Ogawa, O.4    Tabata, Y.5
  • 44
    • 73449102212 scopus 로고    scopus 로고
    • Controlled release of matrix metalloproteinase-1 plasmid DNA prevents left ventricular remodeling in chronic myocardial infarction of rats
    • Lin X., Jo H., Ishii T.M., Fujita M., Fu M., Tambara K., Yamamoto M., Tabata Y., Komeda M., Matsuoka S. Controlled release of matrix metalloproteinase-1 plasmid DNA prevents left ventricular remodeling in chronic myocardial infarction of rats. Circ. J. 2009, 73:2315-2321.
    • (2009) Circ. J. , vol.73 , pp. 2315-2321
    • Lin, X.1    Jo, H.2    Ishii, T.M.3    Fujita, M.4    Fu, M.5    Tambara, K.6    Yamamoto, M.7    Tabata, Y.8    Komeda, M.9    Matsuoka, S.10
  • 45
    • 40449092256 scopus 로고    scopus 로고
    • Controlled delivery of T-box21 small interfering RNA ameliorates autoimmune alopecia (Alopecia Areata) in a C3H/HeJ mouse model
    • Nakamura M., Jo J., Tabata Y., Ishikawa O. Controlled delivery of T-box21 small interfering RNA ameliorates autoimmune alopecia (Alopecia Areata) in a C3H/HeJ mouse model. Am. J. Pathol. 2008, 172:650-658.
    • (2008) Am. J. Pathol. , vol.172 , pp. 650-658
    • Nakamura, M.1    Jo, J.2    Tabata, Y.3    Ishikawa, O.4
  • 46
    • 77950341612 scopus 로고    scopus 로고
    • Sustained release of water-insoluble simvastatin from biodegradable hydrogel augments bone regeneration
    • Tanigo T., Takaoka R., Tabata Y. Sustained release of water-insoluble simvastatin from biodegradable hydrogel augments bone regeneration. J. Control. Release 2010, 143:201-206.
    • (2010) J. Control. Release , vol.143 , pp. 201-206
    • Tanigo, T.1    Takaoka, R.2    Tabata, Y.3
  • 48
    • 33644818689 scopus 로고    scopus 로고
    • Preparation of poly(ethylene glycol)-introduced cationized gelatin as a non-viral gene carrier
    • Kushibiki T., Tabata Y. Preparation of poly(ethylene glycol)-introduced cationized gelatin as a non-viral gene carrier. J. Biomater. Sci. Polym. Ed. 2005, 16:1447-1461.
    • (2005) J. Biomater. Sci. Polym. Ed. , vol.16 , pp. 1447-1461
    • Kushibiki, T.1    Tabata, Y.2
  • 49
    • 0346216863 scopus 로고    scopus 로고
    • Chemical and biological properties of polymer-modified proteins
    • Kochendoerfer G. Chemical and biological properties of polymer-modified proteins. Expert Opin. Biol. Ther. 2003, 3:1253-1261.
    • (2003) Expert Opin. Biol. Ther. , vol.3 , pp. 1253-1261
    • Kochendoerfer, G.1
  • 50
    • 55749111387 scopus 로고    scopus 로고
    • The pharmacology of PEGylation: balancing PD with PK to generate novel therapeutics
    • Fishburn C.S. The pharmacology of PEGylation: balancing PD with PK to generate novel therapeutics. J. Pharm. Sci. 2008, 97:4167-4183.
    • (2008) J. Pharm. Sci. , vol.97 , pp. 4167-4183
    • Fishburn, C.S.1
  • 51
    • 26944452043 scopus 로고    scopus 로고
    • PEGylation, successful approach to drug delivery
    • Veronese F.M., Pasut G. PEGylation, successful approach to drug delivery. Drug Discov. Today 2005, 10:1451-1458.
    • (2005) Drug Discov. Today , vol.10 , pp. 1451-1458
    • Veronese, F.M.1    Pasut, G.2
  • 52
    • 0037362655 scopus 로고    scopus 로고
    • Effect of pegylation on pharmaceuticals
    • Harris J.M., Chess R.B. Effect of pegylation on pharmaceuticals. Nat. Rev. Drug Discov. 2003, 2:214-221.
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 214-221
    • Harris, J.M.1    Chess, R.B.2
  • 55
    • 0038179220 scopus 로고    scopus 로고
    • In vivo release and gene expression of plasmid DNA by hydrogels of gelatin with different cationization extents
    • Kushibiki T., Tomoshige R., Fukunaka Y., Kakemi M., Tabata Y. In vivo release and gene expression of plasmid DNA by hydrogels of gelatin with different cationization extents. J. Control. Release 2003, 90:207-216.
    • (2003) J. Control. Release , vol.90 , pp. 207-216
    • Kushibiki, T.1    Tomoshige, R.2    Fukunaka, Y.3    Kakemi, M.4    Tabata, Y.5
  • 56
    • 0016636179 scopus 로고
    • An improved 2, 4, 6-trinitrobenzenesulfonic acid method for the determination of amines
    • Snyder S.L., Sobocinski P.Z. An improved 2, 4, 6-trinitrobenzenesulfonic acid method for the determination of amines. Anal. Biochem. 1975, 64:284-288.
    • (1975) Anal. Biochem. , vol.64 , pp. 284-288
    • Snyder, S.L.1    Sobocinski, P.Z.2
  • 57
    • 50449151040 scopus 로고
    • The fibrin plate method for estimating fibrinolytic activity
    • Astrup T., Müllertz S. The fibrin plate method for estimating fibrinolytic activity. Arch. Biochem. Biophys. 1952, 40:346-351.
    • (1952) Arch. Biochem. Biophys. , vol.40 , pp. 346-351
    • Astrup, T.1    Müllertz, S.2
  • 58
    • 0842301626 scopus 로고    scopus 로고
    • Synthesis and physical characterization of poly(ethylene glycol)-gelatin conjugates
    • Kushibiki T., Matsuoka H., Tabata Y. Synthesis and physical characterization of poly(ethylene glycol)-gelatin conjugates. Biomacromolecules 2004, 5:202-208.
    • (2004) Biomacromolecules , vol.5 , pp. 202-208
    • Kushibiki, T.1    Matsuoka, H.2    Tabata, Y.3
  • 61
    • 0038120848 scopus 로고    scopus 로고
    • Contribution of von Willebrand factor to thrombus formation on neointima of rabbit stenotic iliac artery under high blood-flow velocity
    • Yamashita A., Asada Y., Sugimura H., Yamamoto H., Marutsuka K., Hatakeyama K., et al. Contribution of von Willebrand factor to thrombus formation on neointima of rabbit stenotic iliac artery under high blood-flow velocity. Arterioscler. Thromb. Vasc. Biol. 2003, 23:1105-1110.
    • (2003) Arterioscler. Thromb. Vasc. Biol. , vol.23 , pp. 1105-1110
    • Yamashita, A.1    Asada, Y.2    Sugimura, H.3    Yamamoto, H.4    Marutsuka, K.5    Hatakeyama, K.6
  • 62
    • 10644234022 scopus 로고    scopus 로고
    • Increased vascular wall thrombogenicity combined with reduced blood flow promotes occlusive thrombus formation in rabbit femoral artery
    • Yamashita A., Furukoji E., Marutsuka K., Hatakeyama K., Yamamoto H., Tamura S., et al. Increased vascular wall thrombogenicity combined with reduced blood flow promotes occlusive thrombus formation in rabbit femoral artery. Arterioscler. Thromb. Vasc. Biol. 2004, 24:2420-2424.
    • (2004) Arterioscler. Thromb. Vasc. Biol. , vol.24 , pp. 2420-2424
    • Yamashita, A.1    Furukoji, E.2    Marutsuka, K.3    Hatakeyama, K.4    Yamamoto, H.5    Tamura, S.6
  • 63
    • 0021916187 scopus 로고
    • The Thrombolysis in Myocardial Infarction (TIMI) trial: phase I findings
    • The TIMI Study Group
    • The TIMI Study Group The Thrombolysis in Myocardial Infarction (TIMI) trial: phase I findings. N. Engl. J. Med. 1985, 312:932-936.
    • (1985) N. Engl. J. Med. , vol.312 , pp. 932-936
  • 64
    • 57749189817 scopus 로고    scopus 로고
    • New insights into the molecular mechanisms of the fibrinolytic system
    • Rijken D.C., Lijnen H.R. New insights into the molecular mechanisms of the fibrinolytic system. J. Thromb. Haemost. 2008, 7:4-13.
    • (2008) J. Thromb. Haemost. , vol.7 , pp. 4-13
    • Rijken, D.C.1    Lijnen, H.R.2
  • 65
    • 0036882394 scopus 로고    scopus 로고
    • Serine protease mechanism and specificity
    • Hedstrom L. Serine protease mechanism and specificity. Chem. Rev. 2002, 102:4501-4523.
    • (2002) Chem. Rev. , vol.102 , pp. 4501-4523
    • Hedstrom, L.1
  • 66
    • 34547523373 scopus 로고    scopus 로고
    • Expression profile of plasmid DNA obtained using spermine derivatives of pullulan with different molecular weights
    • Jo J., Ikai T., Okazaki A., Nagane K., Yamamoto M., Hirano Y., Tabata Y. Expression profile of plasmid DNA obtained using spermine derivatives of pullulan with different molecular weights. J. Biomater. Sci. Polym. Ed. 2007, 18:883-899.
    • (2007) J. Biomater. Sci. Polym. Ed. , vol.18 , pp. 883-899
    • Jo, J.1    Ikai, T.2    Okazaki, A.3    Nagane, K.4    Yamamoto, M.5    Hirano, Y.6    Tabata, Y.7
  • 67
    • 48149110814 scopus 로고    scopus 로고
    • Ultrasound enhanced thrombolysis in acute arterial ischemia
    • Tsivgoulis G., Culp W.C., Alexandrov A.X.V. Ultrasound enhanced thrombolysis in acute arterial ischemia. Ultrasound 2008, 48:303-311.
    • (2008) Ultrasound , vol.48 , pp. 303-311
    • Tsivgoulis, G.1    Culp, W.C.2    Alexandrov, A.X.V.3
  • 68
    • 0036093213 scopus 로고    scopus 로고
    • Can transcranial ultrasonication increase recanalization flow with tissue plasminogen activator ?
    • Ishibashi T., Akiyama M., Onoue H., Abe T., Furuhata H. Can transcranial ultrasonication increase recanalization flow with tissue plasminogen activator ?. Stroke 2002, 33:1399-1404.
    • (2002) Stroke , vol.33 , pp. 1399-1404
    • Ishibashi, T.1    Akiyama, M.2    Onoue, H.3    Abe, T.4    Furuhata, H.5
  • 69
    • 0027998090 scopus 로고
    • Study of the mechanism of ultrasound angioplasty from human thrombi and bovine aorta
    • Rosenschein U., Frimerman A., Laniado S., Miller H.I. Study of the mechanism of ultrasound angioplasty from human thrombi and bovine aorta. Am. J. Cardiol. 1994, 74:1263-1266.
    • (1994) Am. J. Cardiol. , vol.74 , pp. 1263-1266
    • Rosenschein, U.1    Frimerman, A.2    Laniado, S.3    Miller, H.I.4
  • 70
    • 0001121655 scopus 로고    scopus 로고
    • Lactose-poly(ethylene glycol)-grafted poly-l-lysine as hepatoma cell-targeted gene carrier
    • Choi Y.H., Liu F., Park J.S., Kim S.W. Lactose-poly(ethylene glycol)-grafted poly-l-lysine as hepatoma cell-targeted gene carrier. Bioconjug. Chem. 1998, 9:708-718.
    • (1998) Bioconjug. Chem. , vol.9 , pp. 708-718
    • Choi, Y.H.1    Liu, F.2    Park, J.S.3    Kim, S.W.4
  • 72
    • 0034996764 scopus 로고    scopus 로고
    • Long-circulating and target-specific nanoparticles: theory to practice
    • Moghimi S.M., Hunter A.C., Murray J.C. Long-circulating and target-specific nanoparticles: theory to practice. Pharm. Res. 2001, 53:283-318.
    • (2001) Pharm. Res. , vol.53 , pp. 283-318
    • Moghimi, S.M.1    Hunter, A.C.2    Murray, J.C.3
  • 73
    • 67650400226 scopus 로고    scopus 로고
    • Collagen-coated microparticles in drug delivery
    • Sehgal P.K., Srinivasan A. Collagen-coated microparticles in drug delivery. Expert Opin. Drug Deliv. 2009, 6:687-695.
    • (2009) Expert Opin. Drug Deliv. , vol.6 , pp. 687-695
    • Sehgal, P.K.1    Srinivasan, A.2
  • 74
    • 28444496349 scopus 로고    scopus 로고
    • In vivo tumor targeting of tumor necrosis factor-alpha-loaded stealth nanoparticles: effect of MePEG molecular weight and particle size
    • Fang C., Shi B., Pei Y.Y., Hong M.H., Wu J., Chen H.Z. In vivo tumor targeting of tumor necrosis factor-alpha-loaded stealth nanoparticles: effect of MePEG molecular weight and particle size. Eur. J. Pharm. Sci. 2006, 27:27-36.
    • (2006) Eur. J. Pharm. Sci. , vol.27 , pp. 27-36
    • Fang, C.1    Shi, B.2    Pei, Y.Y.3    Hong, M.H.4    Wu, J.5    Chen, H.Z.6
  • 76
    • 0035838377 scopus 로고    scopus 로고
    • Mechanism of the ultrasound activition of micellar drug delivery
    • Marin A., Muniruzzaman M., Rapoport N. Mechanism of the ultrasound activition of micellar drug delivery. J. Control. Release 2001, 75:69-81.
    • (2001) J. Control. Release , vol.75 , pp. 69-81
    • Marin, A.1    Muniruzzaman, M.2    Rapoport, N.3
  • 77
    • 4644292155 scopus 로고    scopus 로고
    • Acoustically active liposomes for drug encapsulation and ultrasound-triggered release
    • Huang S.L., MacDonald R.C. Acoustically active liposomes for drug encapsulation and ultrasound-triggered release. Biochim. Biophys. Acta 2004, 1665:134-141.
    • (2004) Biochim. Biophys. Acta , vol.1665 , pp. 134-141
    • Huang, S.L.1    MacDonald, R.C.2
  • 78
    • 77957021334 scopus 로고    scopus 로고
    • A novel fluoride anion modified gelatin nanogel system for ultrasound-triggered drug release
    • Daocheng W., Mingxi W. A novel fluoride anion modified gelatin nanogel system for ultrasound-triggered drug release. J. Pharm. Pharmaceut. Sci. 2008, 11:32-45.
    • (2008) J. Pharm. Pharmaceut. Sci. , vol.11 , pp. 32-45
    • Daocheng, W.1    Mingxi, W.2
  • 79
    • 38949113153 scopus 로고    scopus 로고
    • The role of ultrasound and magnetic resonance in local drug delivery
    • Deckers R., Rome C., Moonen C.T. The role of ultrasound and magnetic resonance in local drug delivery. J. Magn. Reson. Imaging 2008, 27:400-409.
    • (2008) J. Magn. Reson. Imaging , vol.27 , pp. 400-409
    • Deckers, R.1    Rome, C.2    Moonen, C.T.3
  • 80
    • 8644230974 scopus 로고    scopus 로고
    • And CLOTBUST investigators, ultrasound-enhanced systemic thrombolysis for acute ischemic stroke
    • Alexandrov A.V., Molina C.A., Grotta J.C., Garami Z., Ford S.R., Alvarez-Sabin J., et al. and CLOTBUST investigators, ultrasound-enhanced systemic thrombolysis for acute ischemic stroke. N Engl J. Med. 2004, 351:2170-2178.
    • (2004) N Engl J. Med. , vol.351 , pp. 2170-2178
    • Alexandrov, A.V.1    Molina, C.A.2    Grotta, J.C.3    Garami, Z.4    Ford, S.R.5    Alvarez-Sabin, J.6
  • 81
    • 0037766220 scopus 로고    scopus 로고
    • Effect of ultrasound on thrombolysis of middle cerebral artery occlusion
    • Eggers J., Koch B., Meyer K., Konig I., Seidel G. Effect of ultrasound on thrombolysis of middle cerebral artery occlusion. Ann. Neurol. 2003, 53:797-800.
    • (2003) Ann. Neurol. , vol.53 , pp. 797-800
    • Eggers, J.1    Koch, B.2    Meyer, K.3    Konig, I.4    Seidel, G.5
  • 82


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.