메뉴 건너뛰기




Volumn 89, Issue 2, 2013, Pages 181-188

Expression of curcin-transferrin receptor binding peptide fusion protein and its anti-tumor activity

Author keywords

Anti tumor activity; Curcin; Expression; Fusion protein; Transferrin receptor binding peptide

Indexed keywords

ANTINEOPLASTIC AGENT; CURCIN PROTEIN, JATROPHA CURCAS; HYBRID PROTEIN; PEPTIDE; RIBOSOME INACTIVATING PROTEIN 1; TRANSFERRIN RECEPTOR; VEGETABLE PROTEIN;

EID: 84876382662     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2013.03.009     Document Type: Article
Times cited : (16)

References (33)
  • 1
    • 0022489331 scopus 로고
    • Ribosome-inactivating proteins up to date
    • F. Stirpe, and L. Barbieri Ribosome-inactivating proteins up to date FEBS Lett. 195 1986 1 8
    • (1986) FEBS Lett. , vol.195 , pp. 1-8
    • Stirpe, F.1    Barbieri, L.2
  • 2
    • 0034924485 scopus 로고    scopus 로고
    • Ribosome-inactivating proteins from plants: More than RNA N-glycosidases?
    • W.J. Peumans, Q. Hao, and E.J. Van Damme Ribosome-inactivating proteins from plants: more than RNA N-glycosidases? FASEB J. 15 2001 1493 1506
    • (2001) FASEB J. , vol.15 , pp. 1493-1506
    • Peumans, W.J.1    Hao, Q.2    Van Damme, E.J.3
  • 3
    • 0025936547 scopus 로고
    • Minireview: Enzymatic properties of ribosome-inactivating proteins (RIPs) and related toxins
    • W.P. Fong, R.N. Wong, T.T. Go, and H.W. Yeung Minireview: enzymatic properties of ribosome-inactivating proteins (RIPs) and related toxins Life Sci. 49 1991 1859 1869
    • (1991) Life Sci. , vol.49 , pp. 1859-1869
    • Fong, W.P.1    Wong, R.N.2    Go, T.T.3    Yeung, H.W.4
  • 4
    • 14744291476 scopus 로고
    • Ribosome-inactivating proteins from plants: Present status and future prospects
    • F. Stirpe, L. Barbieri, M.G. Battelli, M. Soria, and D.A. Lappi Ribosome-inactivating proteins from plants: present status and future prospects Biotechnology (NY) 10 1992 405 412
    • (1992) Biotechnology (NY) , vol.10 , pp. 405-412
    • Stirpe, F.1    Barbieri, L.2    Battelli, M.G.3    Soria, M.4    Lappi, D.A.5
  • 5
    • 0028098025 scopus 로고
    • Ricin: Structure, mode of action, and some current applications
    • J.M. Lord, L.M. Roberts, and J.D. Robertus Ricin: structure, mode of action, and some current applications FASEB J. 8 1994 201 208
    • (1994) FASEB J. , vol.8 , pp. 201-208
    • Lord, J.M.1    Roberts, L.M.2    Robertus, J.D.3
  • 6
    • 0015781481 scopus 로고
    • Different biological properties of the two constituent peptide chains of ricin, a toxic protein inhibiting protein synthesis
    • S. Olsnes, and A. Pihl Different biological properties of the two constituent peptide chains of ricin, a toxic protein inhibiting protein synthesis Biochemistry 12 1973 3121 3126
    • (1973) Biochemistry , vol.12 , pp. 3121-3126
    • Olsnes, S.1    Pihl, A.2
  • 7
    • 0030881586 scopus 로고    scopus 로고
    • Plant resistance to fungal infection induced by nontoxic pokeweed antiviral protein mutants
    • O. Zoubenko, F. Uckun, Y. Hur, I. Chet, and N. Tumer Plant resistance to fungal infection induced by nontoxic pokeweed antiviral protein mutants Nat. Biotechnol. 15 1997 992 996
    • (1997) Nat. Biotechnol. , vol.15 , pp. 992-996
    • Zoubenko, O.1    Uckun, F.2    Hur, Y.3    Chet, I.4    Tumer, N.5
  • 9
    • 0030994026 scopus 로고    scopus 로고
    • C-terminal deletion mutant of pokeweed antiviral protein inhibits viral infection but does not depurinate host ribosomes
    • N.E. Tumer, D.J. Hwang, and M. Bonness C-terminal deletion mutant of pokeweed antiviral protein inhibits viral infection but does not depurinate host ribosomes Proc. Natl. Acad. Sci. U.S.A. 94 1997 3866 3871
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 3866-3871
    • Tumer, N.E.1    Hwang, D.J.2    Bonness, M.3
  • 12
    • 0017253038 scopus 로고
    • Studies on the proteins from the seeds of Croton tiglium and of Jatropha curcas. Toxic properties and inhibition of protein synthesis in vitro
    • F. Stirpe, A. Pession-Brizzi, E. Lorenzoni, P. Strocchi, L. Montanaro, and S. Sperti Studies on the proteins from the seeds of Croton tiglium and of Jatropha curcas. Toxic properties and inhibition of protein synthesis in vitro Biochem. J. 156 1976 1 6
    • (1976) Biochem. J. , vol.156 , pp. 1-6
    • Stirpe, F.1    Pession-Brizzi, A.2    Lorenzoni, E.3    Strocchi, P.4    Montanaro, L.5    Sperti, S.6
  • 13
    • 84888881790 scopus 로고    scopus 로고
    • Expression of recombinant curcin in Jatropha curcas L. and its antitumor activity in vitro
    • D.D. Xu, B. Zhang, Y.D. Huang, Q.H. Zhang, Z.J. Su, H. Xu, and Q. Zheng Expression of recombinant curcin in Jatropha curcas L. and its antitumor activity in vitro J. Anhui Agric. Sci. 12 2012 7079 7082
    • (2012) J. Anhui Agric. Sci. , vol.12 , pp. 7079-7082
    • Xu, D.D.1    Zhang, B.2    Huang, Y.D.3    Zhang, Q.H.4    Su, Z.J.5    Xu, H.6    Zheng, Q.7
  • 14
    • 0141760478 scopus 로고    scopus 로고
    • Cloning and expression of curcin, a ribosome-inactivating protein from the seeds of Jatropha curcas
    • J. Lin, Y. Chen, Y. Xu, F. Yan, L. Tang, and F. Chen Cloning and expression of curcin, a ribosome-inactivating protein from the seeds of Jatropha curcas Acta Bot. Sin. 7 2003 858 863
    • (2003) Acta Bot. Sin. , vol.7 , pp. 858-863
    • Lin, J.1    Chen, Y.2    Xu, Y.3    Yan, F.4    Tang, L.5    Chen, F.6
  • 17
    • 77749304317 scopus 로고    scopus 로고
    • Purification and characterization of curcin, a toxic lectin from the seed of Jatropha curcas
    • J. Lin, X. Zhou, J.Y. Wang, P.H. Jiang, and K.X. Tang Purification and characterization of curcin, a toxic lectin from the seed of Jatropha curcas Prep. Biochem. Biotechnol. 40 2010 107 118
    • (2010) Prep. Biochem. Biotechnol. , vol.40 , pp. 107-118
    • Lin, J.1    Zhou, X.2    Wang, J.Y.3    Jiang, P.H.4    Tang, K.X.5
  • 18
    • 84861607615 scopus 로고    scopus 로고
    • The effect of curcin from Jatropha curcas on apoptosis of mouse sarcoma-180 cells
    • Q. Zhao, W.G. Wang, Y.H. Wang, Y. Xu, and F. Chen The effect of curcin from Jatropha curcas on apoptosis of mouse sarcoma-180 cells Fitoterapia 83 2012 849 852
    • (2012) Fitoterapia , vol.83 , pp. 849-852
    • Zhao, Q.1    Wang, W.G.2    Wang, Y.H.3    Xu, Y.4    Chen, F.5
  • 19
    • 4043133131 scopus 로고    scopus 로고
    • Ribosome-inactivating proteins
    • F. Stirpe Ribosome-inactivating proteins Toxicon 44 2004 371 383
    • (2004) Toxicon , vol.44 , pp. 371-383
    • Stirpe, F.1
  • 22
    • 0027368441 scopus 로고
    • Eradication of large solid tumors in mice with an immunotoxin directed against tumor vasculature
    • F.J. Burrows, and P.E. Thorpe Eradication of large solid tumors in mice with an immunotoxin directed against tumor vasculature Proc. Natl. Acad. Sci. U.S.A. 90 1993 8996 9000
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 8996-9000
    • Burrows, F.J.1    Thorpe, P.E.2
  • 24
    • 0033961913 scopus 로고    scopus 로고
    • Transferrin and transferrin receptor function in brain barrier systems
    • T. Moos, and E.H. Morgan Transferrin and transferrin receptor function in brain barrier systems Cell. Mol. Neurobiol. 20 2000 77 95
    • (2000) Cell. Mol. Neurobiol. , vol.20 , pp. 77-95
    • Moos, T.1    Morgan, E.H.2
  • 26
    • 0025057114 scopus 로고
    • Elevated transferrin receptor content in human prostate cancer cell lines assessed in vitro and in vivo
    • H.N. Keer, J.M. Kozlowski, Y.C. Tsai, C. Lee, R.N. McEwan, and J.T. Grayhack Elevated transferrin receptor content in human prostate cancer cell lines assessed in vitro and in vivo J. Urol. 143 1990 381 385
    • (1990) J. Urol. , vol.143 , pp. 381-385
    • Keer, H.N.1    Kozlowski, J.M.2    Tsai, Y.C.3    Lee, C.4    McEwan, R.N.5    Grayhack, J.T.6
  • 27
    • 0020597630 scopus 로고
    • Transferrin receptors in human tissues: Their distribution and possible clinical relevance
    • K.C. Gatter, G. Brown, I.S. Trowbridge, R.E. Woolston, and D.Y. Mason Transferrin receptors in human tissues: their distribution and possible clinical relevance J. Clin. Pathol. 36 1983 539 545
    • (1983) J. Clin. Pathol. , vol.36 , pp. 539-545
    • Gatter, K.C.1    Brown, G.2    Trowbridge, I.S.3    Woolston, R.E.4    Mason, D.Y.5
  • 29
    • 19644389665 scopus 로고    scopus 로고
    • Solubilization and refolding of bacterial inclusion body proteins
    • S.M. Singh, and A.K. Panda Solubilization and refolding of bacterial inclusion body proteins J. Biosci. Bioeng. 99 2005 303 310
    • (2005) J. Biosci. Bioeng. , vol.99 , pp. 303-310
    • Singh, S.M.1    Panda, A.K.2
  • 30
    • 0032190686 scopus 로고    scopus 로고
    • Advances in refolding of proteins produced in E. coli
    • H. Lilie, E. Schwarz, and R. Rudolph Advances in refolding of proteins produced in E. coli Curr. Opin. Biotechnol. 9 1998 497 501
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 497-501
    • Lilie, H.1    Schwarz, E.2    Rudolph, R.3
  • 31
    • 0006454079 scopus 로고
    • Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli
    • J. Buchner, and R. Rudolph Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli Biotechnology (NY) 9 1991 157 162
    • (1991) Biotechnology (NY) , vol.9 , pp. 157-162
    • Buchner, J.1    Rudolph, R.2
  • 32
    • 0027618513 scopus 로고
    • Renaturation of casein kinase II from recombinant subunits produced in Escherichia coli: Purification and characterization of the reconstituted holoenzyme
    • W.J. Lin, and J.A. Traugh Renaturation of casein kinase II from recombinant subunits produced in Escherichia coli: purification and characterization of the reconstituted holoenzyme Protein Expr. Purif. 4 1993 256 264
    • (1993) Protein Expr. Purif. , vol.4 , pp. 256-264
    • Lin, W.J.1    Traugh, J.A.2
  • 33
    • 0030792301 scopus 로고    scopus 로고
    • Optimization of the solubilization and renaturation of fish growth hormone produced by Escherichia coli
    • M.H. Hsih, J.C. Kuo, and H.J. Tsai Optimization of the solubilization and renaturation of fish growth hormone produced by Escherichia coli Appl. Microbiol. Biotechnol. 48 1997 66 72
    • (1997) Appl. Microbiol. Biotechnol. , vol.48 , pp. 66-72
    • Hsih, M.H.1    Kuo, J.C.2    Tsai, H.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.