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Volumn 128, Issue 3, 2007, Pages 638-647

Overexpression of biologically active VEGF121 fusion proteins in Escherichia coli

Author keywords

E. coli AD494 (DE3) pLysS; Fed batch cultivation; Vascular endothelial growth factor (VEGF); VEGF121 rGel

Indexed keywords

CELLS; ESCHERICHIA COLI; GENETIC ENGINEERING; GLYCEROL; GROWTH KINETICS; TUMORS;

EID: 33846358984     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2006.11.027     Document Type: Article
Times cited : (16)

References (28)
  • 2
    • 0032943892 scopus 로고    scopus 로고
    • Vascular endothelial growth factor chimeric toxin is highly active against endothelial cells
    • Arora N., Masood R., Zheng T., Cai J., Smith D.L., and Gill P.S. Vascular endothelial growth factor chimeric toxin is highly active against endothelial cells. Cancer Res. 59 (1999) 183-188
    • (1999) Cancer Res. , vol.59 , pp. 183-188
    • Arora, N.1    Masood, R.2    Zheng, T.3    Cai, J.4    Smith, D.L.5    Gill, P.S.6
  • 3
    • 0034804396 scopus 로고    scopus 로고
    • Functionally active VEGF fusion proteins
    • Backer M.V., and Backer J.M. Functionally active VEGF fusion proteins. Protein Express. Purif. 23 1 (2001) 1-7
    • (2001) Protein Express. Purif. , vol.23 , Issue.1 , pp. 1-7
    • Backer, M.V.1    Backer, J.M.2
  • 4
    • 0029882313 scopus 로고    scopus 로고
    • T-cell-targeted immunofusion proteins from E. coli
    • Better M. T-cell-targeted immunofusion proteins from E. coli. Ann. NY Acad. Sci. 782 1 (1996) 544-554
    • (1996) Ann. NY Acad. Sci. , vol.782 , Issue.1 , pp. 544-554
    • Better, M.1
  • 5
    • 0034791258 scopus 로고    scopus 로고
    • Development and optimization of two-stage cyclic fed-batch culture for hG-CSF production using l-arabinose promoter of Escherichia coli
    • Choi S.-J., Park D.-H., and Jung K.-H. Development and optimization of two-stage cyclic fed-batch culture for hG-CSF production using l-arabinose promoter of Escherichia coli. Bioprocess Biosyst. Eng. 24 (2001) 51-58
    • (2001) Bioprocess Biosyst. Eng. , vol.24 , pp. 51-58
    • Choi, S.-J.1    Park, D.-H.2    Jung, K.-H.3
  • 6
    • 0028865891 scopus 로고
    • Production of hydroxyectoine: high cell-density cultivation and osmotic downshock of Marinococcus strain M52
    • Frings E., Sauer T., and Galinski E.A. Production of hydroxyectoine: high cell-density cultivation and osmotic downshock of Marinococcus strain M52. J. Biotechnol. 43 (1995) 53-61
    • (1995) J. Biotechnol. , vol.43 , pp. 53-61
    • Frings, E.1    Sauer, T.2    Galinski, E.A.3
  • 7
    • 1842415422 scopus 로고    scopus 로고
    • Factors affecting the fermentative production of a lysozyme-binding antibody fragment in Escherichia coli
    • Harrison J.S., Keshavarz-Moore E., Dunnill P., Berry M.J., Fellinger A., and Frenken L. Factors affecting the fermentative production of a lysozyme-binding antibody fragment in Escherichia coli. Biotechnol. Bioeng. 53 6 (1997) 611-622
    • (1997) Biotechnol. Bioeng. , vol.53 , Issue.6 , pp. 611-622
    • Harrison, J.S.1    Keshavarz-Moore, E.2    Dunnill, P.3    Berry, M.J.4    Fellinger, A.5    Frenken, L.6
  • 8
    • 0029379752 scopus 로고
    • Lactose fed-batch overexpression of recombinant metalloproteins in Escherichia coli BL21(DE3): process control yielding high level of metal-incorporated, soluble protein
    • Hoffman B.J., Broadwater J.A., Johnson P., Harper J., Fox B.G., and Kenealy W.R. Lactose fed-batch overexpression of recombinant metalloproteins in Escherichia coli BL21(DE3): process control yielding high level of metal-incorporated, soluble protein. Protein Express. Purif. 6 (1995) 646-654
    • (1995) Protein Express. Purif. , vol.6 , pp. 646-654
    • Hoffman, B.J.1    Broadwater, J.A.2    Johnson, P.3    Harper, J.4    Fox, B.G.5    Kenealy, W.R.6
  • 9
    • 19044367102 scopus 로고    scopus 로고
    • Specific targeting of tumor vasculature by diphtheria toxin-vascular endothelial growth factor fusion protein reduces angiogenesis and growth of pancreatic cancer
    • Hotz H.G., Gill P.S., Masood R., Hotz B., Buhr H.J., Foitzik T., Hines O.J., and Reber H.A. Specific targeting of tumor vasculature by diphtheria toxin-vascular endothelial growth factor fusion protein reduces angiogenesis and growth of pancreatic cancer. J. Gastrointest. Surg. 6 2 (2002) 159-166
    • (2002) J. Gastrointest. Surg. , vol.6 , Issue.2 , pp. 159-166
    • Hotz, H.G.1    Gill, P.S.2    Masood, R.3    Hotz, B.4    Buhr, H.J.5    Foitzik, T.6    Hines, O.J.7    Reber, H.A.8
  • 10
    • 0034761654 scopus 로고    scopus 로고
    • Secretory production of human granulocyte colony stimulating factor in Escherichia coli
    • Jeong K.J., and Lee S.Y. Secretory production of human granulocyte colony stimulating factor in Escherichia coli. Protein Express. Purif. 23 (2001) 311-318
    • (2001) Protein Express. Purif. , vol.23 , pp. 311-318
    • Jeong, K.J.1    Lee, S.Y.2
  • 11
    • 0036296338 scopus 로고    scopus 로고
    • Production of functional single-chain Fv antibodies in the cytoplasm of Escherichia coli
    • Jurado P., Ritz D., Beckwith J., Lorenzo V., and Fernández L.A. Production of functional single-chain Fv antibodies in the cytoplasm of Escherichia coli. J. Mol. Biol. 320 (2002) 1-10
    • (2002) J. Mol. Biol. , vol.320 , pp. 1-10
    • Jurado, P.1    Ritz, D.2    Beckwith, J.3    Lorenzo, V.4    Fernández, L.A.5
  • 13
    • 33645655303 scopus 로고    scopus 로고
    • Biologically active vascular endothelial growth factor as a bacterial recombinant glutathione S-transferase fusion protein
    • Morera Y., Lamdan H., Bequet M., Ayala M., Rojas G., Muñoz Y., and Gavilondo J.V. Biologically active vascular endothelial growth factor as a bacterial recombinant glutathione S-transferase fusion protein. Biotechnol. Appl. Biochem. 44 (2006) 45-53
    • (2006) Biotechnol. Appl. Biochem. , vol.44 , pp. 45-53
    • Morera, Y.1    Lamdan, H.2    Bequet, M.3    Ayala, M.4    Rojas, G.5    Muñoz, Y.6    Gavilondo, J.V.7
  • 14
    • 0026446102 scopus 로고
    • Vascular endothelial growth factor is a potential tumor angiogenesis factor in human gliomas in vivo
    • Plate K.H., Breier G., Weich H.A., and Risau W. Vascular endothelial growth factor is a potential tumor angiogenesis factor in human gliomas in vivo. Nature 359 (1992) 845-848
    • (1992) Nature , vol.359 , pp. 845-848
    • Plate, K.H.1    Breier, G.2    Weich, H.A.3    Risau, W.4
  • 15
    • 0042317093 scopus 로고    scopus 로고
    • Tumor cell killing enabled by listeriolysin O-liposome-mediated delivery of the protein toxin gelonin
    • Provoda C.J., Stier E.M., and Lee K.-D. Tumor cell killing enabled by listeriolysin O-liposome-mediated delivery of the protein toxin gelonin. J. Biol. Chem. 278 37 (2003) 35102-35108
    • (2003) J. Biol. Chem. , vol.278 , Issue.37 , pp. 35102-35108
    • Provoda, C.J.1    Stier, E.M.2    Lee, K.-D.3
  • 17
    • 3042651591 scopus 로고    scopus 로고
    • Heterologous expression and purification of active divercin V41, a class IIa bacteriocin encoded by a synthetic gene in Escherichia coli
    • Richard C., Drider D., Elmorjani K., Marion D., and Prévost H. Heterologous expression and purification of active divercin V41, a class IIa bacteriocin encoded by a synthetic gene in Escherichia coli. J. Bacteriol. 186 13 (2004) 4276-4284
    • (2004) J. Bacteriol. , vol.186 , Issue.13 , pp. 4276-4284
    • Richard, C.1    Drider, D.2    Elmorjani, K.3    Marion, D.4    Prévost, H.5
  • 18
    • 33646569993 scopus 로고    scopus 로고
    • Biology of vascular endothelial growth factors
    • Roy H., Bhardwaj S., and Ylä-Herttuala S. Biology of vascular endothelial growth factors. FEBS Lett. 580 (2006) 2879-2887
    • (2006) FEBS Lett. , vol.580 , pp. 2879-2887
    • Roy, H.1    Bhardwaj, S.2    Ylä-Herttuala, S.3
  • 19
    • 23244448782 scopus 로고    scopus 로고
    • Combination of Dsb coexpression and an addition of sorbitol markedly enhanced soluble expression of single-chain Fv in Escherichia coli
    • Sandee D., Tungpradabkul S., Kurokawa Y., Fukui K., and Takagi M. Combination of Dsb coexpression and an addition of sorbitol markedly enhanced soluble expression of single-chain Fv in Escherichia coli. Biotechnol. Bioeng. 91 4 (2005) 418-424
    • (2005) Biotechnol. Bioeng. , vol.91 , Issue.4 , pp. 418-424
    • Sandee, D.1    Tungpradabkul, S.2    Kurokawa, Y.3    Fukui, K.4    Takagi, M.5
  • 20
    • 20744450629 scopus 로고    scopus 로고
    • Delivery into cells: lessons learned from plant and bacterial toxins
    • Sandvig K., and Deurs B. Delivery into cells: lessons learned from plant and bacterial toxins. Gene Therapy 12 (2005) 865-872
    • (2005) Gene Therapy , vol.12 , pp. 865-872
    • Sandvig, K.1    Deurs, B.2
  • 21
    • 0347634531 scopus 로고    scopus 로고
    • Production of a biotinylated single-chain antibody fragment in the cytoplasm of Escherichia coli
    • Santala V., and Lamminmäki U. Production of a biotinylated single-chain antibody fragment in the cytoplasm of Escherichia coli. J. Immunol. Meth. 284 (2004) 165-175
    • (2004) J. Immunol. Meth. , vol.284 , pp. 165-175
    • Santala, V.1    Lamminmäki, U.2
  • 22
    • 0033781533 scopus 로고    scopus 로고
    • Purification and refolding of vascular endothelial growth factor-B
    • Scrofani S.D., Fabri L.J., Xu P., Maccarone P., and Nash A.D. Purification and refolding of vascular endothelial growth factor-B. Protein Sci. 9 10 (2000) 2018-2025
    • (2000) Protein Sci. , vol.9 , Issue.10 , pp. 2018-2025
    • Scrofani, S.D.1    Fabri, L.J.2    Xu, P.3    Maccarone, P.4    Nash, A.D.5
  • 23
    • 0343196718 scopus 로고    scopus 로고
    • Enhanced production of human mini-proinsulin in fed-batch cultures at high cell density of Escherichia coli BL21(DE3)[pET-3aT2M2]
    • Shin C.S., Hong M.S., Bae C.S., and Lee J. Enhanced production of human mini-proinsulin in fed-batch cultures at high cell density of Escherichia coli BL21(DE3)[pET-3aT2M2]. Biotechnol. Progr. 13 (1997) 249-257
    • (1997) Biotechnol. Progr. , vol.13 , pp. 249-257
    • Shin, C.S.1    Hong, M.S.2    Bae, C.S.3    Lee, J.4
  • 25
    • 0019212385 scopus 로고
    • Gelonin, a new inhibitor of protein synthesis, nontoxic to intact cells. Isolation, characterization, and preparation of cytotoxic complexes with concanavalin A
    • Stirpe F., Olsnes S., and Pihl A. Gelonin, a new inhibitor of protein synthesis, nontoxic to intact cells. Isolation, characterization, and preparation of cytotoxic complexes with concanavalin A. J. Biol. Chem. 255 (1980) 6947-6953
    • (1980) J. Biol. Chem. , vol.255 , pp. 6947-6953
    • Stirpe, F.1    Olsnes, S.2    Pihl, A.3
  • 27
    • 3543050105 scopus 로고    scopus 로고
    • His tag effect on solubility of human proteins produced in Escherichia coli: a comparison between four expression vectors
    • Woestenenk E.A., Hammarström M., Berg S., Härd T., and Berglund H. His tag effect on solubility of human proteins produced in Escherichia coli: a comparison between four expression vectors. J. Struct. Funct. Genom. 5 (2004) 217-229
    • (2004) J. Struct. Funct. Genom. , vol.5 , pp. 217-229
    • Woestenenk, E.A.1    Hammarström, M.2    Berg, S.3    Härd, T.4    Berglund, H.5
  • 28
    • 0036425999 scopus 로고    scopus 로고
    • Expression, purification, and characterization of a biologically active bovine enterokinase catalytic subunit in Escherichia coli
    • Yuan L.-D., and Hua Z.-C. Expression, purification, and characterization of a biologically active bovine enterokinase catalytic subunit in Escherichia coli. Protein Express. Purif. 25 (2002) 300-304
    • (2002) Protein Express. Purif. , vol.25 , pp. 300-304
    • Yuan, L.-D.1    Hua, Z.-C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.