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Volumn 132, Issue 3, 2008, Pages 171-183

Albumin as a drug carrier: Design of prodrugs, drug conjugates and nanoparticles

Author keywords

Albumin nanoparticles; Drug conjugates; Drug delivery; Human serum albumin; Prodrugs

Indexed keywords

ALBUMIN NANOPARTICLES; ANTIVIRAL ACTIVITIES; BIOACTIVE PROTEINS; BREAST CANCERS; CLINICAL SETTINGS; CLINICAL TRIALS; DOXORUBICIN; DRUG CARRIERS; DRUG CONJUGATES; DRUG DELIVERY SYSTEMS; FATTY ACID BINDINGS; FUSION PROTEINS; HEPATITIS C; HUMAN SERUM ALBUMIN; IN PHASE; MYRISTIC ACIDS; PACLITAXEL; PRODRUG; PRODRUGS; SOLID TUMORS; TUMOR TARGETING;

EID: 56949084877     PISSN: 01683659     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jconrel.2008.05.010     Document Type: Article
Times cited : (1925)

References (101)
  • 1
  • 3
    • 0028227096 scopus 로고
    • Structure of serum albumin
    • Carter D.C., and Ho J.X. Structure of serum albumin. Adv. Protein Chem. 45 (1994) 153-203
    • (1994) Adv. Protein Chem. , vol.45 , pp. 153-203
    • Carter, D.C.1    Ho, J.X.2
  • 5
    • 0035992779 scopus 로고    scopus 로고
    • Reversible and covalent binding of drugs to human serum albumin: methodological approaches and physiological relevance
    • Bertucci C., and Domenici E. Reversible and covalent binding of drugs to human serum albumin: methodological approaches and physiological relevance. Curr. Med. Chem. 9 (2002) 1463-1481
    • (2002) Curr. Med. Chem. , vol.9 , pp. 1463-1481
    • Bertucci, C.1    Domenici, E.2
  • 8
    • 0001363919 scopus 로고
    • Protein transfer in tumor-bearing rats
    • Babson A.L., and Winnick T. Protein transfer in tumor-bearing rats. Cancer Res. 14 (1954) 606-611
    • (1954) Cancer Res. , vol.14 , pp. 606-611
    • Babson, A.L.1    Winnick, T.2
  • 9
    • 0022858683 scopus 로고
    • A new concept for macromolecular therapeutics in cancer chemotherapy: mechanism of tumoritropic accumulation of proteins and the antitumor agent smancs
    • Matsumura Y., and Maeda H. A new concept for macromolecular therapeutics in cancer chemotherapy: mechanism of tumoritropic accumulation of proteins and the antitumor agent smancs. Cancer Res. 46 (1986) 6387-6392
    • (1986) Cancer Res. , vol.46 , pp. 6387-6392
    • Matsumura, Y.1    Maeda, H.2
  • 10
    • 0034000453 scopus 로고    scopus 로고
    • Tumor vascular permeability and the EPR effect in macromolecular therapeutics: a review
    • Maeda H., Wu J., Sawa T., Matsumura Y., and Hori K. Tumor vascular permeability and the EPR effect in macromolecular therapeutics: a review. J. Controlled Release 65 (2000) 271-284
    • (2000) J. Controlled Release , vol.65 , pp. 271-284
    • Maeda, H.1    Wu, J.2    Sawa, T.3    Matsumura, Y.4    Hori, K.5
  • 12
    • 0029150245 scopus 로고
    • Vascular permeability in a human tumor xenograft: molecular size dependence and cutoff size
    • Yuan F., Dellian M., Fukumura D., Leunig M., Berk D.A., Torchilin V.P., and Jain R.K. Vascular permeability in a human tumor xenograft: molecular size dependence and cutoff size. Cancer Res. 55 (1995) 3752-3756
    • (1995) Cancer Res. , vol.55 , pp. 3752-3756
    • Yuan, F.1    Dellian, M.2    Fukumura, D.3    Leunig, M.4    Berk, D.A.5    Torchilin, V.P.6    Jain, R.K.7
  • 13
    • 0031959490 scopus 로고    scopus 로고
    • Early phase tumor accumulation of macromolecules: a great difference in clearance rate between tumor and normal tissues
    • Noguchi Y., Wu J., Duncan R., Strohalm J., Ulbrich K., Akaike T., and Maeda H. Early phase tumor accumulation of macromolecules: a great difference in clearance rate between tumor and normal tissues. Jpn. J. Cancer Res. 89 (1998) 307-314
    • (1998) Jpn. J. Cancer Res. , vol.89 , pp. 307-314
    • Noguchi, Y.1    Wu, J.2    Duncan, R.3    Strohalm, J.4    Ulbrich, K.5    Akaike, T.6    Maeda, H.7
  • 14
    • 0032421248 scopus 로고    scopus 로고
    • Serum proteins as drug carriers of anticancer agents: a review
    • Kratz F., and Beyer U. Serum proteins as drug carriers of anticancer agents: a review. Drug Deliv. 5 (1998) 281-299
    • (1998) Drug Deliv. , vol.5 , pp. 281-299
    • Kratz, F.1    Beyer, U.2
  • 17
  • 18
    • 0024982210 scopus 로고
    • Serum albumin metabolism in rheumatic diseases: relationship to corticosteroids and peptic ulcer
    • Niwa Y., Iio A., Niwa G., Sakane T., Tsunematsu T., and Kanoh T. Serum albumin metabolism in rheumatic diseases: relationship to corticosteroids and peptic ulcer. J. Clin. Lab. Immunol. 31 (1990) 11-16
    • (1990) J. Clin. Lab. Immunol. , vol.31 , pp. 11-16
    • Niwa, Y.1    Iio, A.2    Niwa, G.3    Sakane, T.4    Tsunematsu, T.5    Kanoh, T.6
  • 19
    • 0019834651 scopus 로고
    • Permeability of rheumatoid and normal human synovium to specific plasma proteins
    • Levick J.R. Permeability of rheumatoid and normal human synovium to specific plasma proteins. Arthritis Rheum. 24 (1981) 1550-1560
    • (1981) Arthritis Rheum. , vol.24 , pp. 1550-1560
    • Levick, J.R.1
  • 24
    • 34548570767 scopus 로고    scopus 로고
    • Pharmacology of insulin detemir
    • Kurtzhals P. Pharmacology of insulin detemir. Endocrinol. Metab. Clin. North Am. 36 Suppl 1 (2007) 14-20
    • (2007) Endocrinol. Metab. Clin. North Am. , vol.36 , Issue.SUPPL. 1 , pp. 14-20
    • Kurtzhals, P.1
  • 25
    • 33745703563 scopus 로고    scopus 로고
    • Polymer therapeutics: concepts and applications
    • Haag R., and Kratz F. Polymer therapeutics: concepts and applications. Angew. Chem., Int. Ed. Engl. 45 (2006) 1198-1215
    • (2006) Angew. Chem., Int. Ed. Engl. , vol.45 , pp. 1198-1215
    • Haag, R.1    Kratz, F.2
  • 26
    • 0342314489 scopus 로고    scopus 로고
    • A novel macromolecular prodrug concept exploiting endogenous serum albumin as a drug carrier for cancer chemotherapy
    • Kratz F., Mueller-Driver R., Hofmann I., Drevs J., and Unger C. A novel macromolecular prodrug concept exploiting endogenous serum albumin as a drug carrier for cancer chemotherapy. J. Med. Chem. 43 (2000) 1253-1256
    • (2000) J. Med. Chem. , vol.43 , pp. 1253-1256
    • Kratz, F.1    Mueller-Driver, R.2    Hofmann, I.3    Drevs, J.4    Unger, C.5
  • 27
    • 24344508224 scopus 로고    scopus 로고
    • Doxorubicin coupled to lactosaminated albumin inhibits the growth of hepatocellular carcinomas induced in rats by diethylnitrosamine
    • Fiume L., Bolondi L., Busi C., Chieco P., Kratz F., Mattson G., Lanza M., and Di Stefano G. Doxorubicin coupled to lactosaminated albumin inhibits the growth of hepatocellular carcinomas induced in rats by diethylnitrosamine. J. Hepatol. 43 (2005) 645-652
    • (2005) J. Hepatol. , vol.43 , pp. 645-652
    • Fiume, L.1    Bolondi, L.2    Busi, C.3    Chieco, P.4    Kratz, F.5    Mattson, G.6    Lanza, M.7    Di Stefano, G.8
  • 28
    • 33644827912 scopus 로고    scopus 로고
    • RGD-based strategies for selective delivery of therapeutics and imaging agents to the tumour vasculature
    • Temming K., Schiffelers R.M., Molema G., and Kok R.J. RGD-based strategies for selective delivery of therapeutics and imaging agents to the tumour vasculature. Drug Resist. Update 8 (2005) 381-402
    • (2005) Drug Resist. Update , vol.8 , pp. 381-402
    • Temming, K.1    Schiffelers, R.M.2    Molema, G.3    Kok, R.J.4
  • 30
    • 0033868623 scopus 로고    scopus 로고
    • Laser-induced fluorescence detection of malignant gliomas using fluorescein-labeled serum albumin: experimental and preliminary clinical results
    • Kremer P., Wunder A., Sinn H., Haase T., Rheinwald M., Zillmann U., Albert F.K., and Kunze S. Laser-induced fluorescence detection of malignant gliomas using fluorescein-labeled serum albumin: experimental and preliminary clinical results. Neurol. Res. 22 (2000) 481-489
    • (2000) Neurol. Res. , vol.22 , pp. 481-489
    • Kremer, P.1    Wunder, A.2    Sinn, H.3    Haase, T.4    Rheinwald, M.5    Zillmann, U.6    Albert, F.K.7    Kunze, S.8
  • 34
    • 0036201980 scopus 로고    scopus 로고
    • A phase II trial of methotrexate-human serum albumin (MTX-HSA) in patients with metastatic renal cell carcinoma who progressed under immunotherapy
    • Vis A.N., van der Gaast A., van Rhijn B.W., Catsburg T.K., Schmidt C., and Mickisch G.H. A phase II trial of methotrexate-human serum albumin (MTX-HSA) in patients with metastatic renal cell carcinoma who progressed under immunotherapy. Cancer Chemother. Pharmacol. 49 (2002) 342-345
    • (2002) Cancer Chemother. Pharmacol. , vol.49 , pp. 342-345
    • Vis, A.N.1    van der Gaast, A.2    van Rhijn, B.W.3    Catsburg, T.K.4    Schmidt, C.5    Mickisch, G.H.6
  • 36
    • 56949087948 scopus 로고    scopus 로고
    • In vivo efficacy and pharmacokinetic study of an acid-sensitive albumin conjugate in a murine renal cell carcinoma model
    • Drevs J., Esser N., Richly H., Skorzec M., Scheulen M.E., Unger C., and Kratz F. In vivo efficacy and pharmacokinetic study of an acid-sensitive albumin conjugate in a murine renal cell carcinoma model. Clin. Cancer Res. 6 120 Suppl. (2000)
    • (2000) Clin. Cancer Res. , vol.6 , Issue.120 SUPPL
    • Drevs, J.1    Esser, N.2    Richly, H.3    Skorzec, M.4    Scheulen, M.E.5    Unger, C.6    Kratz, F.7
  • 37
    • 0037028050 scopus 로고    scopus 로고
    • Probing the cysteine-34 position of endogenous serum albumin with thiol-binding doxorubicin derivatives: improved efficacy of an acid-sensitive doxorubicin derivative with specific albumin-binding properties compared to that of the parent compound
    • Kratz F., Warnecke A., Scheuermann K., Stockmar C., Schwab J., Lazar P., Drückes P., Esser N., Drevs J., Rognan D., Bissantz C., Hinderling C., Folkers G., Fichtner I., and Unger C. Probing the cysteine-34 position of endogenous serum albumin with thiol-binding doxorubicin derivatives: improved efficacy of an acid-sensitive doxorubicin derivative with specific albumin-binding properties compared to that of the parent compound. J. Med. Chem. 45 (2002) 5523-5533
    • (2002) J. Med. Chem. , vol.45 , pp. 5523-5533
    • Kratz, F.1    Warnecke, A.2    Scheuermann, K.3    Stockmar, C.4    Schwab, J.5    Lazar, P.6    Drückes, P.7    Esser, N.8    Drevs, J.9    Rognan, D.10    Bissantz, C.11    Hinderling, C.12    Folkers, G.13    Fichtner, I.14    Unger, C.15
  • 38
    • 33847029969 scopus 로고    scopus 로고
    • Acute and repeat-dose toxicity studies of the (6-maleimidocaproyl)hydrazone derivative of doxorubicin (DOXO-EMCH), an albumin-binding prodrug of the anticancer agent doxorubicin
    • Kratz F., Ehling G., Kauffmann H.M., and Unger C. Acute and repeat-dose toxicity studies of the (6-maleimidocaproyl)hydrazone derivative of doxorubicin (DOXO-EMCH), an albumin-binding prodrug of the anticancer agent doxorubicin. Hum. Exp. Toxicol. 26 (2007) 19-35
    • (2007) Hum. Exp. Toxicol. , vol.26 , pp. 19-35
    • Kratz, F.1    Ehling, G.2    Kauffmann, H.M.3    Unger, C.4
  • 39
    • 33846594736 scopus 로고    scopus 로고
    • The 6-maleimidocaproyl hydrazone derivative of doxorubicin (DOXO-EMCH) is superior to free doxorubicin with respect to cardiotoxicity and mitochondrial damage
    • Lebrecht D., Geist A., Ketelsen U.P., Haberstroh J., Setzer B., Kratz F., and Walker U.A. The 6-maleimidocaproyl hydrazone derivative of doxorubicin (DOXO-EMCH) is superior to free doxorubicin with respect to cardiotoxicity and mitochondrial damage. Int. J. Cancer 120 (2007) 927-934
    • (2007) Int. J. Cancer , vol.120 , pp. 927-934
    • Lebrecht, D.1    Geist, A.2    Ketelsen, U.P.3    Haberstroh, J.4    Setzer, B.5    Kratz, F.6    Walker, U.A.7
  • 40
    • 34548106304 scopus 로고    scopus 로고
    • Phase I and pharmacokinetic study of the (6-maleimidocaproyl)hydrazone derivative of doxorubicin
    • Unger C., Haring B., Medinger M., Drevs J., Steinbild S., Kratz F., and Mross K. Phase I and pharmacokinetic study of the (6-maleimidocaproyl)hydrazone derivative of doxorubicin. Clin. Cancer Res. 13 (2007) 4858-4866
    • (2007) Clin. Cancer Res. , vol.13 , pp. 4858-4866
    • Unger, C.1    Haring, B.2    Medinger, M.3    Drevs, J.4    Steinbild, S.5    Kratz, F.6    Mross, K.7
  • 41
    • 0042173127 scopus 로고    scopus 로고
    • A new approach for the treatment of malignant melanoma: enhanced antitumor efficacy of an albumin-binding doxorubicin prodrug that is cleaved by matrix metalloproteinase 2
    • Mansour A.M., Drevs J., Esser N., Hamada F.M., Badary O.A., Unger C., Fichtner I., and Kratz F. A new approach for the treatment of malignant melanoma: enhanced antitumor efficacy of an albumin-binding doxorubicin prodrug that is cleaved by matrix metalloproteinase 2. Cancer Res. 63 (2003) 4062-4066
    • (2003) Cancer Res. , vol.63 , pp. 4062-4066
    • Mansour, A.M.1    Drevs, J.2    Esser, N.3    Hamada, F.M.4    Badary, O.A.5    Unger, C.6    Fichtner, I.7    Kratz, F.8
  • 42
    • 34347354414 scopus 로고    scopus 로고
    • Albumin-binding prodrugs of camptothecin and doxorubicin with an Ala-Leu-Ala-Leu-linker that are cleaved by cathepsin B: synthesis and antitumor efficacy
    • Schmid B., Chung D.E., Warnecke A., Fichtner I., and Kratz F. Albumin-binding prodrugs of camptothecin and doxorubicin with an Ala-Leu-Ala-Leu-linker that are cleaved by cathepsin B: synthesis and antitumor efficacy. Bioconjug. Chem. 18 (2007) 702-716
    • (2007) Bioconjug. Chem. , vol.18 , pp. 702-716
    • Schmid, B.1    Chung, D.E.2    Warnecke, A.3    Fichtner, I.4    Kratz, F.5
  • 43
    • 33747339731 scopus 로고    scopus 로고
    • Development of a novel albumin-binding prodrug that is cleaved by urokinase-type-plasminogen activator (uPA)
    • Chung D.E., and Kratz F. Development of a novel albumin-binding prodrug that is cleaved by urokinase-type-plasminogen activator (uPA). Bioorg. Med. Chem. Lett. 16 (2006) 5157-5163
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , pp. 5157-5163
    • Chung, D.E.1    Kratz, F.2
  • 44
    • 27644436770 scopus 로고    scopus 로고
    • Development of albumin-binding doxorubicin prodrugs that are cleaved by prostate-specific antigen (PSA)
    • Kratz F., Mansour A., Soltau J., Warnecke A., Fichtner I., Unger C., and Drevs J. Development of albumin-binding doxorubicin prodrugs that are cleaved by prostate-specific antigen (PSA). Arch. Pharm. 338 (2005) 462-472
    • (2005) Arch. Pharm. , vol.338 , pp. 462-472
    • Kratz, F.1    Mansour, A.2    Soltau, J.3    Warnecke, A.4    Fichtner, I.5    Unger, C.6    Drevs, J.7
  • 45
    • 38749154289 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of an albumin-binding prodrug of doxorubicin that is cleaved by prostate-specific antigen (PSA) in a PSA-positive orthotopic prostate carcinoma model (LNCaP)
    • Graeser R., Chung D.E., Esser N., Moor S., Schachtele C., Unger C., and Kratz F. Synthesis and biological evaluation of an albumin-binding prodrug of doxorubicin that is cleaved by prostate-specific antigen (PSA) in a PSA-positive orthotopic prostate carcinoma model (LNCaP). Int. J. Cancer 122 (2008) 1145-1154
    • (2008) Int. J. Cancer , vol.122 , pp. 1145-1154
    • Graeser, R.1    Chung, D.E.2    Esser, N.3    Moor, S.4    Schachtele, C.5    Unger, C.6    Kratz, F.7
  • 46
    • 34548067350 scopus 로고    scopus 로고
    • Synthesis, cleavage profile, and antitumor efficacy of an albumin-binding prodrug of methotrexate that is cleaved by plasmin and cathepsin B
    • Warnecke A., Fichtner I., Sass G., and Kratz F. Synthesis, cleavage profile, and antitumor efficacy of an albumin-binding prodrug of methotrexate that is cleaved by plasmin and cathepsin B. Arch. Pharm. (Weinheim) 340 (2007) 389-395
    • (2007) Arch. Pharm. (Weinheim) , vol.340 , pp. 389-395
    • Warnecke, A.1    Fichtner, I.2    Sass, G.3    Kratz, F.4
  • 47
    • 36849072730 scopus 로고    scopus 로고
    • Development of albumin-binding camptothecin prodrugs using a peptide positional scanning library
    • Schmid B., Warnecke A., Fichtner I., Jung M., and Kratz F. Development of albumin-binding camptothecin prodrugs using a peptide positional scanning library. Bioconjug. Chem. 18 (2007) 1786-1799
    • (2007) Bioconjug. Chem. , vol.18 , pp. 1786-1799
    • Schmid, B.1    Warnecke, A.2    Fichtner, I.3    Jung, M.4    Kratz, F.5
  • 48
    • 0037343958 scopus 로고    scopus 로고
    • Maleimide-oligo(ethylene glycol) derivatives of camptothecin as albumin-binding prodrugs: synthesis and antitumor efficacy
    • Warnecke A., and Kratz F. Maleimide-oligo(ethylene glycol) derivatives of camptothecin as albumin-binding prodrugs: synthesis and antitumor efficacy. Bioconjug. Chem. 14 (2003) 377-387
    • (2003) Bioconjug. Chem. , vol.14 , pp. 377-387
    • Warnecke, A.1    Kratz, F.2
  • 49
    • 0030839707 scopus 로고    scopus 로고
    • Synthesis of maleimide derivatives of the anticancer drugs 5-fluorouracil and 5′-deoxy-5-fluorouridine for the preparation of chemoimmunoconjugates
    • Beyer U., Schumacher P., Unger C., Frahm A.W., and Kratz F. Synthesis of maleimide derivatives of the anticancer drugs 5-fluorouracil and 5′-deoxy-5-fluorouridine for the preparation of chemoimmunoconjugates. Pharmazie 52 (1996) 480-482
    • (1996) Pharmazie , vol.52 , pp. 480-482
    • Beyer, U.1    Schumacher, P.2    Unger, C.3    Frahm, A.W.4    Kratz, F.5
  • 50
    • 9244222743 scopus 로고    scopus 로고
    • Synthesis and biological activity of water-soluble maleimide derivatives of the anticancer drug carboplatin designed as albumin-binding prodrugs
    • Warnecke A., Fichtner I., Garmann D., Jaehde U., and Kratz F. Synthesis and biological activity of water-soluble maleimide derivatives of the anticancer drug carboplatin designed as albumin-binding prodrugs. Bioconjug. Chem. 15 (2004) 1349-1359
    • (2004) Bioconjug. Chem. , vol.15 , pp. 1349-1359
    • Warnecke, A.1    Fichtner, I.2    Garmann, D.3    Jaehde, U.4    Kratz, F.5
  • 52
    • 3042698264 scopus 로고    scopus 로고
    • Methotrexate (MTX) and albumin coupled with MTX (MTX-HSA) suppress synovial fibroblast invasion and cartilage degradation in vivo
    • Fiehn C., Neumann E., Wunder A., Krienke S., Gay S., and Muller-Ladner U. Methotrexate (MTX) and albumin coupled with MTX (MTX-HSA) suppress synovial fibroblast invasion and cartilage degradation in vivo. Ann. Rheum. Dis. 63 (2004) 884-886
    • (2004) Ann. Rheum. Dis. , vol.63 , pp. 884-886
    • Fiehn, C.1    Neumann, E.2    Wunder, A.3    Krienke, S.4    Gay, S.5    Muller-Ladner, U.6
  • 53
    • 0034132379 scopus 로고    scopus 로고
    • Cathepsins B and L in synovial fluids from patients with rheumatoid arthritis and the effect of cathepsin B on the activation of pro-urokinase
    • Ikeda Y., Ikata T., Mishiro T., Nakano S., Ikebe M., and Yasuoka S. Cathepsins B and L in synovial fluids from patients with rheumatoid arthritis and the effect of cathepsin B on the activation of pro-urokinase. J. Med. Invest. 47 (2000) 61-75
    • (2000) J. Med. Invest. , vol.47 , pp. 61-75
    • Ikeda, Y.1    Ikata, T.2    Mishiro, T.3    Nakano, S.4    Ikebe, M.5    Yasuoka, S.6
  • 55
    • 0142093581 scopus 로고    scopus 로고
    • Doxorubicin coupled to lactosaminated human albumin remains confined within mouse liver cells after the intracellular release from the carrier
    • Di Stefano G., Kratz F., Lanza M., and Fiume L. Doxorubicin coupled to lactosaminated human albumin remains confined within mouse liver cells after the intracellular release from the carrier. Digestive and Liver Disease 35 (2003) 428-433
    • (2003) Digestive and Liver Disease , vol.35 , pp. 428-433
    • Di Stefano, G.1    Kratz, F.2    Lanza, M.3    Fiume, L.4
  • 57
    • 24344508224 scopus 로고    scopus 로고
    • Doxorubicin coupled to lactosaminated albumin inhibits the growth of hepatocellular carcinomas induced in rats by diethylnitrosamine
    • Fiume L., Bolondi L., Busi C., Chieco P., Kratz F., Lanza M., Mattioli A., and Di Stefano G. Doxorubicin coupled to lactosaminated albumin inhibits the growth of hepatocellular carcinomas induced in rats by diethylnitrosamine. J. Hepatol. 43 (2005) 645-652
    • (2005) J. Hepatol. , vol.43 , pp. 645-652
    • Fiume, L.1    Bolondi, L.2    Busi, C.3    Chieco, P.4    Kratz, F.5    Lanza, M.6    Mattioli, A.7    Di Stefano, G.8
  • 58
    • 0032836395 scopus 로고    scopus 로고
    • The asialoglycoprotein receptor in human hepatocellular carcinomas: its expression on proliferating cells
    • Trerè D., Fiume L., Badiali De Giorgi L., Di Stefano G., Migaldi M., and Derenzini M. The asialoglycoprotein receptor in human hepatocellular carcinomas: its expression on proliferating cells. Br. J. Cancer 81 (1999) 404-408
    • (1999) Br. J. Cancer , vol.81 , pp. 404-408
    • Trerè, D.1    Fiume, L.2    Badiali De Giorgi, L.3    Di Stefano, G.4    Migaldi, M.5    Derenzini, M.6
  • 59
    • 0036119489 scopus 로고    scopus 로고
    • Drug conjugates with albumin and transferrin
    • Kratz F. Drug conjugates with albumin and transferrin. Exp. Opin. Ther. Pat. 12 (2002) 433-439
    • (2002) Exp. Opin. Ther. Pat. , vol.12 , pp. 433-439
    • Kratz, F.1
  • 61
    • 0037312818 scopus 로고    scopus 로고
    • Glucagon-like peptides: regulators of cell proliferation, differentiation, and apoptosis
    • Drucker D.J. Glucagon-like peptides: regulators of cell proliferation, differentiation, and apoptosis. Mol. Endocrinol. 17 (2003) 161-171
    • (2003) Mol. Endocrinol. , vol.17 , pp. 161-171
    • Drucker, D.J.1
  • 62
    • 0037339649 scopus 로고    scopus 로고
    • Development and characterization of a glucagon-like peptide 1-albumin conjugate: the ability to activate the glucagon-like peptide 1 receptor in vivo
    • Kim J.G., Baggio L.L., Bridon D.P., Castaigne J.P., Robitaille M.F., Jette L., Benquet C., and Drucker D.J. Development and characterization of a glucagon-like peptide 1-albumin conjugate: the ability to activate the glucagon-like peptide 1 receptor in vivo. Diabetes 52 (2003) 751-759
    • (2003) Diabetes , vol.52 , pp. 751-759
    • Kim, J.G.1    Baggio, L.L.2    Bridon, D.P.3    Castaigne, J.P.4    Robitaille, M.F.5    Jette, L.6    Benquet, C.7    Drucker, D.J.8
  • 63
    • 0031446132 scopus 로고    scopus 로고
    • Effect of fatty acids and selected drugs on the albumin binding of a long-acting, acylated insulin analogue
    • Kurtzhals P., Havelund S., Jonassen I., and Markussen J. Effect of fatty acids and selected drugs on the albumin binding of a long-acting, acylated insulin analogue. J. Pharm. Sci. 86 (1997) 1365-1368
    • (1997) J. Pharm. Sci. , vol.86 , pp. 1365-1368
    • Kurtzhals, P.1    Havelund, S.2    Jonassen, I.3    Markussen, J.4
  • 64
    • 33144488817 scopus 로고    scopus 로고
    • Insulin detemir: from concept to clinical experience
    • Home P., and Kurtzhals P. Insulin detemir: from concept to clinical experience. Expert Opin. Pharmacother. 7 (2006) 325-343
    • (2006) Expert Opin. Pharmacother. , vol.7 , pp. 325-343
    • Home, P.1    Kurtzhals, P.2
  • 65
    • 33747738025 scopus 로고    scopus 로고
    • Drug evaluation: albuferon-alpha-an antiviral interferon-alpha/albumin fusion protein
    • Chemmanur A.T., and Wu G.Y. Drug evaluation: albuferon-alpha-an antiviral interferon-alpha/albumin fusion protein. Curr. Opin. Investig. Drugs 7 (2006) 750-758
    • (2006) Curr. Opin. Investig. Drugs , vol.7 , pp. 750-758
    • Chemmanur, A.T.1    Wu, G.Y.2
  • 67
    • 0024435933 scopus 로고
    • Albumin microspheres. II: Applications in drug delivery
    • Gupta P.K., and Hung C.T. Albumin microspheres. II: Applications in drug delivery. J. Microencapsul 6 (1989) 463-472
    • (1989) J. Microencapsul , vol.6 , pp. 463-472
    • Gupta, P.K.1    Hung, C.T.2
  • 68
    • 0024420485 scopus 로고
    • Albumin microspheres. I: Physico-chemical characteristics
    • Gupta P.K., and Hung C.T. Albumin microspheres. I: Physico-chemical characteristics. J. Microencapsul 6 (1989) 427-462
    • (1989) J. Microencapsul , vol.6 , pp. 427-462
    • Gupta, P.K.1    Hung, C.T.2
  • 69
    • 23944438949 scopus 로고    scopus 로고
    • Lymph kinetics with technetium-99 m labeled radiopharmaceuticals. Animal studies
    • Weiss M., Gildehaus F.J., Brinkbaumer K., Makowski M., and Hahn K. Lymph kinetics with technetium-99 m labeled radiopharmaceuticals. Animal studies. Nuklearmedizin 44 (2005) 156-165
    • (2005) Nuklearmedizin , vol.44 , pp. 156-165
    • Weiss, M.1    Gildehaus, F.J.2    Brinkbaumer, K.3    Makowski, M.4    Hahn, K.5
  • 72
    • 0035099089 scopus 로고    scopus 로고
    • Lymphoscintigraphic sentinel node imaging and gamma probe detection in breast cancer with Tc-99 m nanocolloidal albumin: results of an optimized protocol
    • Rink T., Heuser T., Fitz H., Schroth H.J., Weller E., and Zippel H.H. Lymphoscintigraphic sentinel node imaging and gamma probe detection in breast cancer with Tc-99 m nanocolloidal albumin: results of an optimized protocol. Clin. Nucl. Med. 26 (2001) 293-298
    • (2001) Clin. Nucl. Med. , vol.26 , pp. 293-298
    • Rink, T.1    Heuser, T.2    Fitz, H.3    Schroth, H.J.4    Weller, E.5    Zippel, H.H.6
  • 74
    • 32044475100 scopus 로고    scopus 로고
    • Relationship of 99mtechnetium labelled macroaggregated albumin (99mTc-MAA) uptake by colorectal liver metastases to response following selective internal radiation therapy (SIRT)
    • Dhabuwala A., Lamerton P., and Stubbs R.S. Relationship of 99mtechnetium labelled macroaggregated albumin (99mTc-MAA) uptake by colorectal liver metastases to response following selective internal radiation therapy (SIRT). BMC Nuclear Medicine 5 (2005) 7
    • (2005) BMC Nuclear Medicine , vol.5 , pp. 7
    • Dhabuwala, A.1    Lamerton, P.2    Stubbs, R.S.3
  • 75
    • 0035086593 scopus 로고    scopus 로고
    • Assessment of leg oedema by dynamic lymphoscintigraphy with intradermal injection of technetium-99 m human serum albumin and load produced by standing
    • Suga K., Kume N., Matsunaga N., Motoyama K., Hara A., and Ogasawara N. Assessment of leg oedema by dynamic lymphoscintigraphy with intradermal injection of technetium-99 m human serum albumin and load produced by standing. Eur. J. Nucl. Med. 28 (2001) 294-303
    • (2001) Eur. J. Nucl. Med. , vol.28 , pp. 294-303
    • Suga, K.1    Kume, N.2    Matsunaga, N.3    Motoyama, K.4    Hara, A.5    Ogasawara, N.6
  • 76
    • 0035088225 scopus 로고    scopus 로고
    • Protein-losing enteropathy: diagnosis with (99 m)Tc-labeled human serum albumin scintigraphy
    • Chiu N.T., Lee B.F., Hwang S.J., Chang J.M., Liu G.C., and Yu H.S. Protein-losing enteropathy: diagnosis with (99 m)Tc-labeled human serum albumin scintigraphy. Radiology 219 (2001) 86-90
    • (2001) Radiology , vol.219 , pp. 86-90
    • Chiu, N.T.1    Lee, B.F.2    Hwang, S.J.3    Chang, J.M.4    Liu, G.C.5    Yu, H.S.6
  • 77
    • 0034744685 scopus 로고    scopus 로고
    • 99Tc(m) nanocolloid scintigraphy: a reliable way to detect active joint disease in patients with peripheral joint pain
    • Adams B.K., Al Attia H.M., Khadim R.A., and Al Haider Z.Y. 99Tc(m) nanocolloid scintigraphy: a reliable way to detect active joint disease in patients with peripheral joint pain. Nucl. Med. Commun. 22 (2001) 315-318
    • (2001) Nucl. Med. Commun. , vol.22 , pp. 315-318
    • Adams, B.K.1    Al Attia, H.M.2    Khadim, R.A.3    Al Haider, Z.Y.4
  • 78
    • 33644753906 scopus 로고    scopus 로고
    • Increased antitumor activity, intratumor paclitaxel concentrations, and endothelial cell transport of cremophor-free, albumin-bound paclitaxel, ABI-007, compared with cremophor-based paclitaxel
    • Desai N., Trieu V., Yao Z., Louie L., Ci S., Yang A., Tao C., De T., Beals B., Dykes D., Noker P., Yao R., Labao E., Hawkins M., and Soon-Shiong P. Increased antitumor activity, intratumor paclitaxel concentrations, and endothelial cell transport of cremophor-free, albumin-bound paclitaxel, ABI-007, compared with cremophor-based paclitaxel. Clin. Cancer Res. 12 (2006) 1317-1324
    • (2006) Clin. Cancer Res. , vol.12 , pp. 1317-1324
    • Desai, N.1    Trieu, V.2    Yao, Z.3    Louie, L.4    Ci, S.5    Yang, A.6    Tao, C.7    De, T.8    Beals, B.9    Dykes, D.10    Noker, P.11    Yao, R.12    Labao, E.13    Hawkins, M.14    Soon-Shiong, P.15
  • 81
    • 0038156981 scopus 로고    scopus 로고
    • Emerging role of taxanes in adjuvant and neoadjuvant therapy for breast cancer: the potential and the questions
    • Goble S., and Bear H.D. Emerging role of taxanes in adjuvant and neoadjuvant therapy for breast cancer: the potential and the questions. Surg. Clin. North Am. 83 (2003) 943-971
    • (2003) Surg. Clin. North Am. , vol.83 , pp. 943-971
    • Goble, S.1    Bear, H.D.2
  • 85
    • 32944482677 scopus 로고    scopus 로고
    • Phase III trial of nanoparticle albumin-bound paclitaxel compared with polyethylated castor oil-based paclitaxel in women with breast cancer
    • Gradishar W.J., Tjulandin S., Davidson N., Shaw H., Desai N., Bhar P., Hawkins M., and O'Shaughnessy J. Phase III trial of nanoparticle albumin-bound paclitaxel compared with polyethylated castor oil-based paclitaxel in women with breast cancer. J. Clin. Oncol. 23 (2005) 7794-7803
    • (2005) J. Clin. Oncol. , vol.23 , pp. 7794-7803
    • Gradishar, W.J.1    Tjulandin, S.2    Davidson, N.3    Shaw, H.4    Desai, N.5    Bhar, P.6    Hawkins, M.7    O'Shaughnessy, J.8
  • 86
    • 36348989864 scopus 로고    scopus 로고
    • Randomized study comparing nab-paclitaxel with solvent-based paclitaxel in Chinese patients (pts) with metastatic breast cancer (MBC)
    • Guan Z., Feng F., Li Q.L., Jiang Z., Shen Z., Yu S., Feng J., Huang J., Yao Z., and Hawkins M.J. Randomized study comparing nab-paclitaxel with solvent-based paclitaxel in Chinese patients (pts) with metastatic breast cancer (MBC). J. Clin. Oncol. 25 (2007) 1038
    • (2007) J. Clin. Oncol. , vol.25 , pp. 1038
    • Guan, Z.1    Feng, F.2    Li, Q.L.3    Jiang, Z.4    Shen, Z.5    Yu, S.6    Feng, J.7    Huang, J.8    Yao, Z.9    Hawkins, M.J.10
  • 88
    • 0033091409 scopus 로고    scopus 로고
    • Receptor-mediated targeting of phthalocyanines to macrophages via covalent coupling to native or maleylated bovine serum albumin
    • Brasseur N., Langlois R., La Madeleine C., Ouellet R., and van Lier J.E. Receptor-mediated targeting of phthalocyanines to macrophages via covalent coupling to native or maleylated bovine serum albumin. Photochem. Photobiol. 69 (1999) 345-352
    • (1999) Photochem. Photobiol. , vol.69 , pp. 345-352
    • Brasseur, N.1    Langlois, R.2    La Madeleine, C.3    Ouellet, R.4    van Lier, J.E.5
  • 89
    • 0002792021 scopus 로고
    • Interactions of antitumour metal complexes with serum proteins. Perspectives for anticancer drug development. A review
    • Keppler B.K. (Ed), Verlag Chemie, Weinheim
    • Kratz F. Interactions of antitumour metal complexes with serum proteins. Perspectives for anticancer drug development. A review. In: Keppler B.K. (Ed). Metal Complexes as Antitumour Agents (1993), Verlag Chemie, Weinheim
    • (1993) Metal Complexes as Antitumour Agents
    • Kratz, F.1
  • 90
    • 0031656004 scopus 로고    scopus 로고
    • Anticancer metal complexes and tumour targeting strategies
    • Kratz F., and Schütte M.T. Anticancer metal complexes and tumour targeting strategies. Cancer J. 11 (1998) 60-67
    • (1998) Cancer J. , vol.11 , pp. 60-67
    • Kratz, F.1    Schütte, M.T.2
  • 91
    • 0032844002 scopus 로고    scopus 로고
    • Homing of negatively charged albumins to the lymphatic system: general implications for drug targeting to peripheral tissues and viral reservoirs
    • Swart P.J., Beljaars L., Kuipers M.E., Smit C., Nieuwenhuis P., and Meijer D.K. Homing of negatively charged albumins to the lymphatic system: general implications for drug targeting to peripheral tissues and viral reservoirs. Biochem. Pharmacol. 58 (1999) 1425-1435
    • (1999) Biochem. Pharmacol. , vol.58 , pp. 1425-1435
    • Swart, P.J.1    Beljaars, L.2    Kuipers, M.E.3    Smit, C.4    Nieuwenhuis, P.5    Meijer, D.K.6
  • 92
    • 0032962307 scopus 로고    scopus 로고
    • Anti-HIV-1 activity of combinations and covalent conjugates of negatively charged human serum albumins (NCAs) and AZT
    • Kuipers M.E., Swart P.J., Witvrouw M., Este J.A., Reymen D., De Clercq E., and Meijer D.K. Anti-HIV-1 activity of combinations and covalent conjugates of negatively charged human serum albumins (NCAs) and AZT. J. Drug. Targeting 6 (1999) 323-335
    • (1999) J. Drug. Targeting , vol.6 , pp. 323-335
    • Kuipers, M.E.1    Swart, P.J.2    Witvrouw, M.3    Este, J.A.4    Reymen, D.5    De Clercq, E.6    Meijer, D.K.7
  • 94
    • 0035292828 scopus 로고    scopus 로고
    • Delivery of peptides and proteins through the blood-brain barrier
    • Bickel U., Yoshikawa T., and Pardridge W.M. Delivery of peptides and proteins through the blood-brain barrier. Adv. Drug Deliv. Rev. 46 (2001) 247-279
    • (2001) Adv. Drug Deliv. Rev. , vol.46 , pp. 247-279
    • Bickel, U.1    Yoshikawa, T.2    Pardridge, W.M.3
  • 95
    • 0025136834 scopus 로고
    • Beta-endorphin chimeric peptides: transport through the blood-brain barrier in vivo and cleavage of disulfide linkage by brain
    • Pardridge W.M., Triguero D., and Buciak J.L. Beta-endorphin chimeric peptides: transport through the blood-brain barrier in vivo and cleavage of disulfide linkage by brain. Endocrinology 126 (1990) 977-984
    • (1990) Endocrinology , vol.126 , pp. 977-984
    • Pardridge, W.M.1    Triguero, D.2    Buciak, J.L.3
  • 96
    • 34249666727 scopus 로고    scopus 로고
    • Human serum albumin nanoparticles for efficient delivery of Cu, Zn superoxide dismutase gene
    • Mo Y., Barnett M.E., Takemoto D., Davidson H., and Kompella U.B. Human serum albumin nanoparticles for efficient delivery of Cu, Zn superoxide dismutase gene. Mol. Vis. 13 (2007) 746-757
    • (2007) Mol. Vis. , vol.13 , pp. 746-757
    • Mo, Y.1    Barnett, M.E.2    Takemoto, D.3    Davidson, H.4    Kompella, U.B.5
  • 97
    • 0035964457 scopus 로고    scopus 로고
    • Cationized human serum albumin as a non-viral vector system for gene delivery? Characterization of complex formation with plasmid DNA and transfection efficiency
    • Fischer D., Bieber T., Brusselbach S., Elsasser H., and Kissel T. Cationized human serum albumin as a non-viral vector system for gene delivery? Characterization of complex formation with plasmid DNA and transfection efficiency. Int. J. Pharm. 225 (2001) 97-111
    • (2001) Int. J. Pharm. , vol.225 , pp. 97-111
    • Fischer, D.1    Bieber, T.2    Brusselbach, S.3    Elsasser, H.4    Kissel, T.5
  • 98
    • 0034612205 scopus 로고    scopus 로고
    • Echocardiographic destruction of albumin microbubbles directs gene delivery to the myocardium
    • Shohet R.V., Chen S., Zhou Y.T., Wang Z., Meidell R.S., Unger R.H., and Grayburn P.A. Echocardiographic destruction of albumin microbubbles directs gene delivery to the myocardium. Circulation 101 (2000) 2554-2556
    • (2000) Circulation , vol.101 , pp. 2554-2556
    • Shohet, R.V.1    Chen, S.2    Zhou, Y.T.3    Wang, Z.4    Meidell, R.S.5    Unger, R.H.6    Grayburn, P.A.7
  • 99
    • 28844482895 scopus 로고    scopus 로고
    • Albumin clusters: structurally defined protein tetramer and oxygen carrier including thirty-two iron(II) porphyrins
    • Komatsu T., Oguro Y., Nakagawa A., and Tsuchida E. Albumin clusters: structurally defined protein tetramer and oxygen carrier including thirty-two iron(II) porphyrins. Biomacromolecules 6 (2005) 3397-3403
    • (2005) Biomacromolecules , vol.6 , pp. 3397-3403
    • Komatsu, T.1    Oguro, Y.2    Nakagawa, A.3    Tsuchida, E.4
  • 100
    • 31544455290 scopus 로고    scopus 로고
    • Human serum albumin hybrid incorporating tailed porphyrinatoiron(II) in the alpha,alpha,alpha,beta-conformer as an O2-binding site
    • Nakagawa A., Komatsu T., Iizuka M., and Tsuchida E. Human serum albumin hybrid incorporating tailed porphyrinatoiron(II) in the alpha,alpha,alpha,beta-conformer as an O2-binding site. Bioconjug. Chem. 17 (2006) 146-151
    • (2006) Bioconjug. Chem. , vol.17 , pp. 146-151
    • Nakagawa, A.1    Komatsu, T.2    Iizuka, M.3    Tsuchida, E.4
  • 101
    • 34249980937 scopus 로고    scopus 로고
    • DOXO-EMCH (INNO-206): the first albumin-binding prodrug of doxorubicin to enter clinical trials
    • Kratz F. DOXO-EMCH (INNO-206): the first albumin-binding prodrug of doxorubicin to enter clinical trials. Expert Opin. Investig. Drugs 16 (2007) 855-866
    • (2007) Expert Opin. Investig. Drugs , vol.16 , pp. 855-866
    • Kratz, F.1


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