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Volumn 24, Issue 1, 2008, Pages 2-7

Improving therapeutic properties of protein drugs through alteration of intracellular trafficking pathways

Author keywords

[No Author keywords available]

Indexed keywords

BIOTECHNOLOGY; PROTEINS;

EID: 38949188650     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp070080b     Document Type: Conference Paper
Times cited : (14)

References (30)
  • 2
    • 0344876636 scopus 로고    scopus 로고
    • Transferrin receptor ligand-targeted toxin conjugate (Tf-CRM107) for therapy of malignant gliomas
    • Weaver, M.; Laske, D. W. Transferrin receptor ligand-targeted toxin conjugate (Tf-CRM107) for therapy of malignant gliomas. J. Neurooncol. 2003, 65, 3-13.
    • (2003) J. Neurooncol , vol.65 , pp. 3-13
    • Weaver, M.1    Laske, D.W.2
  • 3
    • 0024271198 scopus 로고
    • Effects of recombinant human granulocyte colony-stimulating factor on hematopoietic progenitor cells in cancer patients
    • Duhrsen, U.; Villeval, J. L.; Boyd, J.; Kannourakis, G.; Morstyn, G.; Metcalf, D. Effects of recombinant human granulocyte colony-stimulating factor on hematopoietic progenitor cells in cancer patients. Blood 1988, 72, 2074-2081.
    • (1988) Blood , vol.72 , pp. 2074-2081
    • Duhrsen, U.1    Villeval, J.L.2    Boyd, J.3    Kannourakis, G.4    Morstyn, G.5    Metcalf, D.6
  • 4
    • 24944493938 scopus 로고    scopus 로고
    • Toward high-resolution de novo structure prediction for small proteins
    • Bradley, P.; Misura, K. M.; Baker, D. Toward high-resolution de novo structure prediction for small proteins. Science 2005, 309, 1868-1871.
    • (2005) Science , vol.309 , pp. 1868-1871
    • Bradley, P.1    Misura, K.M.2    Baker, D.3
  • 5
    • 0014770620 scopus 로고
    • Metabolic properties of IgG subclasses in man
    • Morell, A.; Terry, W. D.; Waldmann, T. A. Metabolic properties of IgG subclasses in man. J. Clin. Invest. 1970, 49, 673-680.
    • (1970) J. Clin. Invest , vol.49 , pp. 673-680
    • Morell, A.1    Terry, W.D.2    Waldmann, T.A.3
  • 7
    • 0018761581 scopus 로고
    • Rapid-turnover transport proteins: An index of subclinical protein-energy malnutrition
    • Shetty, P. S.; Watrasiewicz, K. E.; Jung, R. T.; James, W. P. Rapid-turnover transport proteins: an index of subclinical protein-energy malnutrition. Lancet 1979, 2, 230-232.
    • (1979) Lancet , vol.2 , pp. 230-232
    • Shetty, P.S.1    Watrasiewicz, K.E.2    Jung, R.T.3    James, W.P.4
  • 8
    • 0034042660 scopus 로고    scopus 로고
    • Multiple roles for the major histocompatibility complex class 1- related receptor FcRn
    • Ghetie, V.; Ward, E. S. Multiple roles for the major histocompatibility complex class 1- related receptor FcRn. Annu. Rev. Immunol. 2000, 18, 739-766.
    • (2000) Annu. Rev. Immunol , vol.18 , pp. 739-766
    • Ghetie, V.1    Ward, E.S.2
  • 9
    • 0035012654 scopus 로고    scopus 로고
    • Crystal structure at 2.8 A of an FcRn/heterodimeric Fc complex: Mechanism of pH-dependent binding
    • Martin, W. L.; West, A. P., Jr.; Gan, L.; Bjorkman, P. J. Crystal structure at 2.8 A of an FcRn/heterodimeric Fc complex: mechanism of pH-dependent binding. Mol. Cell 2001, 7, 867-877.
    • (2001) Mol. Cell , vol.7 , pp. 867-877
    • Martin, W.L.1    West Jr., A.P.2    Gan, L.3    Bjorkman, P.J.4
  • 10
    • 0028808880 scopus 로고
    • Analysis of the pH dependence of the neonatal Fc receptor/immunoglobulin G interaction using antibody and receptor variants
    • Raghavan, M.; Bonagura, V. R.; Morrison, S. L.; Bjorkman, P. J. Analysis of the pH dependence of the neonatal Fc receptor/immunoglobulin G interaction using antibody and receptor variants. Biochemistry 1995, 34, 14649-14657.
    • (1995) Biochemistry , vol.34 , pp. 14649-14657
    • Raghavan, M.1    Bonagura, V.R.2    Morrison, S.L.3    Bjorkman, P.J.4
  • 11
    • 0344069729 scopus 로고    scopus 로고
    • IL-2 receptor-targeted cytolytic IL-2/Fc fusion protein treatment blocks diabetogenic autoimmunity in nonobese diabetic mice
    • Zheng, X. X.; Steele, A. W.; Hancock, W. W.; Kawamoto, K.; Li, X. C.; Nickerson, P. W.; Li, Y.; Tian, Y.; Strom, T. B. IL-2 receptor-targeted cytolytic IL-2/Fc fusion protein treatment blocks diabetogenic autoimmunity in nonobese diabetic mice. J. Immunol. 1999, 163, 4041-4048.
    • (1999) J. Immunol , vol.163 , pp. 4041-4048
    • Zheng, X.X.1    Steele, A.W.2    Hancock, W.W.3    Kawamoto, K.4    Li, X.C.5    Nickerson, P.W.6    Li, Y.7    Tian, Y.8    Strom, T.B.9
  • 15
    • 0037222528 scopus 로고    scopus 로고
    • Cell-level pharmacokinetic model of granulocyte colony-stimulating factor: Implications for ligand lifetime and potency in vivo
    • Sarkar, C. A.; Lauffenburger, D. A. Cell-level pharmacokinetic model of granulocyte colony-stimulating factor: implications for ligand lifetime and potency in vivo. Mol. Pharmacol. 2003, 63, 147-158.
    • (2003) Mol. Pharmacol , vol.63 , pp. 147-158
    • Sarkar, C.A.1    Lauffenburger, D.A.2
  • 16
    • 0030570842 scopus 로고    scopus 로고
    • Intracellular receptor/ligand sorting based on endosomal retention components
    • French, A. R. D. A. L. Intracellular receptor/ligand sorting based on endosomal retention components. Biotechnol. Bioeng. 1996, 51, 281-297.
    • (1996) Biotechnol. Bioeng , vol.51 , pp. 281-297
    • French, A.R.D.A.L.1
  • 17
    • 0030743087 scopus 로고    scopus 로고
    • Controlling receptor/ligand trafficking: Effects of cellular and molecular properties on endosomal sorting
    • French, A. R.; Lauffenburger, D. A. Controlling receptor/ligand trafficking: effects of cellular and molecular properties on endosomal sorting. Ann. Biomed. Eng. 1997, 25, 690-707.
    • (1997) Ann. Biomed. Eng , vol.25 , pp. 690-707
    • French, A.R.1    Lauffenburger, D.A.2
  • 18
    • 12744281102 scopus 로고    scopus 로고
    • Sorting nexins - unifying trends and new perspectives
    • Carlton, J.; Bujny, M.; Rutherford, A.; Cullen, P. Sorting nexins - unifying trends and new perspectives. Traffic 2005, 6, 75-82.
    • (2005) Traffic , vol.6 , pp. 75-82
    • Carlton, J.1    Bujny, M.2    Rutherford, A.3    Cullen, P.4
  • 19
    • 9444263165 scopus 로고    scopus 로고
    • Regulation of epidermal growth factor receptor degradation by heterotrimeric Galphas protein
    • Zheng, B.; Lavoie, C.; Tang, T. D.; Ma, P.; Meerloo, T.; Beas, A.; Farquhar, M. G. Regulation of epidermal growth factor receptor degradation by heterotrimeric Galphas protein. Mol. Biol. Cell 2004, 15, 5538-5550.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5538-5550
    • Zheng, B.1    Lavoie, C.2    Tang, T.D.3    Ma, P.4    Meerloo, T.5    Beas, A.6    Farquhar, M.G.7
  • 20
    • 0036713917 scopus 로고    scopus 로고
    • Rational cytokine design for increased lifetime and enhanced potency using pH-activated "histidine switching
    • Sarkar, C. A.; Lowenhaupt, K.; Horan, T.; Boone, T. C.; Tidor, B.; Lauffenburger, D. A. Rational cytokine design for increased lifetime and enhanced potency using pH-activated "histidine switching". Nat. Biotechnol. 2002, 20, 908-913.
    • (2002) Nat. Biotechnol , vol.20 , pp. 908-913
    • Sarkar, C.A.1    Lowenhaupt, K.2    Horan, T.3    Boone, T.C.4    Tidor, B.5    Lauffenburger, D.A.6
  • 21
    • 0033554674 scopus 로고    scopus 로고
    • Atomic structure of the GCSF-receptor complex showing a new cytokine-receptor recognition scheme
    • Aritomi, M.; Kunishima, N.; Okamoto, T.; Kuroki, R.; Ota, Y.; Morikawa, K. Atomic structure of the GCSF-receptor complex showing a new cytokine-receptor recognition scheme. Nature 1999, 401, 713-717.
    • (1999) Nature , vol.401 , pp. 713-717
    • Aritomi, M.1    Kunishima, N.2    Okamoto, T.3    Kuroki, R.4    Ota, Y.5    Morikawa, K.6
  • 22
    • 0018850440 scopus 로고
    • Iron transport and storage proteins
    • Aisen, P.; Listowsky, I. Iron transport and storage proteins. Annu. Rev. Biochem. 1980, 49, 357-393.
    • (1980) Annu. Rev. Biochem , vol.49 , pp. 357-393
    • Aisen, P.1    Listowsky, I.2
  • 23
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: Molecular control of mammalian iron metabolism
    • Hentze, M. W.; Muckenthaler, M. U.; Andrews, N. C. Balancing acts: molecular control of mammalian iron metabolism. Cell 2004, 117, 285-297.
    • (2004) Cell , vol.117 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 24
    • 0025302688 scopus 로고
    • Manipulations of cellular iron metabolism for modulating normal and malignant cell proliferation: Achievements and prospects
    • Cazzola, M.; Bergamaschi, G.; Dezza, L.; Arosio, P. Manipulations of cellular iron metabolism for modulating normal and malignant cell proliferation: achievements and prospects. Blood 1990, 75, 1903-1919.
    • (1990) Blood , vol.75 , pp. 1903-1919
    • Cazzola, M.1    Bergamaschi, G.2    Dezza, L.3    Arosio, P.4
  • 25
    • 0036889760 scopus 로고    scopus 로고
    • Targeted drug delivery via the transferrin receptor-mediated endocytosis pathway
    • Qian, Z. M.; Li, H.; Sun, H.; Ho, K. Targeted drug delivery via the transferrin receptor-mediated endocytosis pathway. Pharmacol. Rev. 2002, 54, 561-587.
    • (2002) Pharmacol. Rev , vol.54 , pp. 561-587
    • Qian, Z.M.1    Li, H.2    Sun, H.3    Ho, K.4
  • 26
    • 0028656441 scopus 로고
    • Quantitative analysis of protein synthesis inhibition by transferrin-toxin conjugates
    • Yazdi, P. T.; Murphy, R. M. Quantitative analysis of protein synthesis inhibition by transferrin-toxin conjugates. Cancer Res. 1994, 54, 6387-6394.
    • (1994) Cancer Res , vol.54 , pp. 6387-6394
    • Yazdi, P.T.1    Murphy, R.M.2
  • 28
    • 13844267123 scopus 로고    scopus 로고
    • Integrating cell-level kinetic modeling into the design of engineered protein therapeutics
    • Rao, B. M.; Lauffenburger, D. A.; Wittrup, K. D. Integrating cell-level kinetic modeling into the design of engineered protein therapeutics. Nat. Biotechnol. 2005, 23, 191-194.
    • (2005) Nat. Biotechnol , vol.23 , pp. 191-194
    • Rao, B.M.1    Lauffenburger, D.A.2    Wittrup, K.D.3
  • 29
    • 1342264310 scopus 로고    scopus 로고
    • Structure of the human transferrin receptor-transferrin complex
    • Cheng, Y.; Zak, O.; Aisen, P.; Harrison, S. C.; Walz, T. Structure of the human transferrin receptor-transferrin complex. Cell 2004, 116, 565-576.
    • (2004) Cell , vol.116 , pp. 565-576
    • Cheng, Y.1    Zak, O.2    Aisen, P.3    Harrison, S.C.4    Walz, T.5
  • 30
    • 2342574817 scopus 로고    scopus 로고
    • The oxalate effect on release of iron from human serum transferrin explained
    • Halbrooks, P. J.; Mason, A. B.; Adams, T. E.; Briggs, S. K.; Everse, S. J. The oxalate effect on release of iron from human serum transferrin explained. J. Mol. Biol. 2004, 339, 217-26.
    • (2004) J. Mol. Biol , vol.339 , pp. 217-226
    • Halbrooks, P.J.1    Mason, A.B.2    Adams, T.E.3    Briggs, S.K.4    Everse, S.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.