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Volumn 4, Issue , 2014, Pages

Cytological and Subcellular Response of Cells Exposed to the Type-1 RIP Curcin and its Hemocompatibility Analysis

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EID: 84926340225     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep05747     Document Type: Article
Times cited : (10)

References (57)
  • 1
    • 14744291476 scopus 로고
    • Ribosome- Inactivating Proteins from Plants: Present Status and Future Prospects
    • Stirpe, F., Barbieri, L., Battelli, M. G., Soria, M. & Lappi, D. A. Ribosome- Inactivating Proteins from Plants: Present Status and Future Prospects. Nat. Biotechnol. 10, 405-412 (1992).
    • (1992) Nat. Biotechnol. , vol.10 , pp. 405-412
    • Stirpe, F.1    Barbieri, L.2    Battelli, M.G.3    Soria, M.4    Lappi, D.A.5
  • 2
    • 84875259702 scopus 로고    scopus 로고
    • Ribosome-inactivating proteins: From toxins to useful proteins
    • Stripe, F. Ribosome-inactivating proteins: From toxins to useful proteins. Toxicon 67, 12-16 (2013).
    • (2013) Toxicon , vol.67 , pp. 12-16
    • Stripe, F.1
  • 4
    • 0023664263 scopus 로고
    • Themechanism of action of ricin and related toxic lectins on eukaryotic ribosomes
    • Endo, Y., Mitsui, K., Motizuki, M. & Tsurugi, K. Themechanism of action of ricin and related toxic lectins on eukaryotic ribosomes. J. Biol. Chem. 262, 5908-5912 (1978).
    • (1978) J. Biol. Chem. , vol.262 , pp. 5908-5912
    • Endo, Y.1    Mitsui, K.2    Motizuki, M.3    Tsurugi, K.4
  • 5
    • 0023219950 scopus 로고
    • RNA N-glycosidase activity of ricin A-chain, mechanism of action of the toxic lectin on eukaryotic ribosomes
    • Endo, Y. & Tsurugi, K. RNA N-glycosidase activity of ricin A-chain, mechanism of action of the toxic lectin on eukaryotic ribosomes. J. Biol. Chem. 262, 8128-8130 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 8128-8130
    • Endo, Y.1    Tsurugi, K.2
  • 6
    • 4043133131 scopus 로고    scopus 로고
    • Ribosome-inactivating proteins
    • Stripe, F. Ribosome-inactivating proteins. Toxicon 44, 371-383 (2004).
    • (2004) Toxicon , vol.44 , pp. 371-383
    • Stripe, F.1
  • 7
    • 0026660286 scopus 로고
    • Some ribosome-inactivating proteins depurinate ribosomal RNA at multiple sites
    • Barbieri, L., Ferreras, J. M., Barraco, A., Ricci, P. & Stirpe, F. Some ribosome-inactivating proteins depurinate ribosomal RNA at multiple sites. Biochem. J. 286, 1-4 (1992).
    • (1992) Biochem. J. , vol.286 , pp. 1-4
    • Barbieri, L.1    Ferreras, J.M.2    Barraco, A.3    Ricci, P.4    Stirpe, F.5
  • 8
    • 33747229123 scopus 로고    scopus 로고
    • Ribosome-inactivating proteins: Progress and problems
    • Stirpe, F. & Battelli, M. G. Ribosome-inactivating proteins: progress and problems. Cell. Mol. Life Sci. 63, 1850-1866 (2006).
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 1850-1866
    • Stirpe, F.1    Battelli, M.G.2
  • 9
    • 0026720825 scopus 로고
    • Proteins with abortifacient, ribosome inactivating, immunomodulatory, antitumor and anti-AIDS activities from cucurbitaceae plants
    • Ng, T. B., Chan, W. Y. & Yeung, H. W. Proteins with abortifacient, ribosome inactivating, immunomodulatory, antitumor and anti-AIDS activities from cucurbitaceae plants. Gen. Pharmac. 23, 575-590 (1992).
    • (1992) Gen. Pharmac. , vol.23 , pp. 575-590
    • Ng, T.B.1    Chan, W.Y.2    Yeung, H.W.3
  • 10
    • 0014954212 scopus 로고
    • Abrin and ricin: New anti-tumour substances
    • Lin, J. Y., Tserng, K. Y., Chen, C. C., Lin, L. T. & Tung, T. C. Abrin and ricin: new anti-tumour substances. Nature 227, 292-293 (1970).
    • (1970) Nature , vol.227 , pp. 292-293
    • Lin, J.Y.1    Tserng, K.Y.2    Chen, C.C.3    Lin, L.T.4    Tung, T.C.5
  • 11
    • 0024347707 scopus 로고
    • Intratumour therapy of solid tumours with ricin-antibody conjugates
    • Kanellos, J., McKenzie, I. F. & Pietersz, G. A. Intratumour therapy of solid tumours with ricin-antibody conjugates. Immunol. Cell Biol. 67, 89-99 (1989).
    • (1989) Immunol. Cell Biol. , vol.67 , pp. 89-99
    • Kanellos, J.1    McKenzie, I.F.2    Pietersz, G.A.3
  • 13
    • 4043112821 scopus 로고    scopus 로고
    • Purification and characterization of Moschatin, a novel type I ribosome-inactivating protein from the mature seeds of pumpkin (Cucurbita moschata), and preparation of its immunotoxin against human melanoma cells
    • Xia, H. C., Li, F., Li, Z. & Zhang, Z. C. Purification and characterization of Moschatin, a novel type I ribosome-inactivating protein from the mature seeds of pumpkin (Cucurbita moschata), and preparation of its immunotoxin against human melanoma cells. Cell Research 13, 369-374 (2003).
    • (2003) Cell Research , vol.13 , pp. 369-374
    • Xia, H.C.1    Li, F.2    Li, Z.3    Zhang, Z.C.4
  • 14
    • 36749004368 scopus 로고    scopus 로고
    • Conjugation of an anti-transferrin receptor IgG3-avidin fusion protein with biotinylated saporin results in significant enhancement of its cytotoxicity against malignant hematopoietic cells
    • 1
    • Daniels1, T. R. et al. Conjugation of an anti-transferrin receptor IgG3-avidin fusion protein with biotinylated saporin results in significant enhancement of its cytotoxicity against malignant hematopoietic cells. Mol. Cancer Ther. 6, 2995-3008 (2007).
    • (2007) Mol. Cancer Ther. , vol.6 , pp. 2995-3008
    • Daniels, T.R.1
  • 15
    • 84884524144 scopus 로고    scopus 로고
    • Targeted cytolysins synergistically potentiate cytoplasmic delivery of gelonin immunotoxin
    • Pirie, C. M., Liu, D. V. & Wittrup, K. D. Targeted cytolysins synergistically potentiate cytoplasmic delivery of gelonin immunotoxin. Mol. Cancer Ther. 12, 1774-82 (2013).
    • (2013) Mol. Cancer Ther. , vol.12 , pp. 1774-1782
    • Pirie, C.M.1    Liu, D.V.2    Wittrup, K.D.3
  • 16
    • 0028148350 scopus 로고
    • Recent developments in immunotoxin therapy
    • Ghetie, M. A.&Vitetta, E. S. Recent developments in immunotoxin therapy. Curr. Opin. Immunol. 6, 707-714 (1994).
    • (1994) Curr. Opin. Immunol. , vol.6 , pp. 707-714
    • Ghetie, M.A.1    Vitetta, E.S.2
  • 18
    • 0029806274 scopus 로고    scopus 로고
    • Induction of apoptosis by ribosome-inactivating proteins and related immunotoxins
    • Bolognesi, A.et al. Induction of apoptosis by ribosome-inactivating proteins and related immunotoxins. Int. J. Cancer 68, 349-355 (1996).
    • (1996) Int. J. Cancer , vol.68 , pp. 349-355
    • Bolognesi, A.1
  • 19
    • 51249107532 scopus 로고    scopus 로고
    • Ribosome inactivating protein saporin induces apoptosis through mitochondrial cascade, independent of translation inhibition
    • Sikriwal, D., Ghosh, P. & Batra, J. K. Ribosome inactivating protein saporin induces apoptosis through mitochondrial cascade, independent of translation inhibition. Int. J. Biochem. Cell Biol. 40, 2880-2888 (2008).
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 2880-2888
    • Sikriwal, D.1    Ghosh, P.2    Batra, J.K.3
  • 20
    • 77649129744 scopus 로고    scopus 로고
    • An evolved ribosome-inactivating protein targets and kills human melanoma cells in vitro and in vivo
    • Cheung, M. C. et al. An evolved ribosome-inactivating protein targets and kills human melanoma cells in vitro and in vivo. Molecular Cancer 9, 28 (2010).
    • (2010) Molecular Cancer , vol.9 , pp. 28
    • Cheung, M.C.1
  • 21
    • 67650097017 scopus 로고    scopus 로고
    • Ribosome-inactivating proteins isolated from dietary bitter melon induce apoptosis and inhibit histone deacetylase-1 selectively in premalignant and malignant prostate cancer cells
    • Xiong, S. D. et al. Ribosome-inactivating proteins isolated from dietary bitter melon induce apoptosis and inhibit histone deacetylase-1 selectively in premalignant and malignant prostate cancer cells. Int. J. Cancer 125, 774-782 (2009).
    • (2009) Int. J. Cancer , vol.125 , pp. 774-782
    • Xiong, S.D.1
  • 22
    • 53249109668 scopus 로고    scopus 로고
    • Therapeutic biology of Jatropha curcas: A mini review
    • Thomas, R., Sah, N. K. & Sharma, P. B. Therapeutic biology of Jatropha curcas: a mini review. Curr. Pharm. Biotechnol. 9, 315-24 (2008).
    • (2008) Curr. Pharm. Biotechnol. , vol.9 , pp. 315-324
    • Thomas, R.1    Sah, N.K.2    Sharma, P.B.3
  • 23
    • 84858709993 scopus 로고    scopus 로고
    • Jatropha curcas: A potential biofuel plant for sustainable environmental development
    • Pandey, V. C. et al. Jatropha curcas: A potential biofuel plant for sustainable environmental development. Renewable and Sustainable Energy Reviews 16, 2870-2883 (2012).
    • (2012) Renewable and Sustainable Energy Reviews , vol.16 , pp. 2870-2883
    • Pandey, V.C.1
  • 24
    • 53249119524 scopus 로고    scopus 로고
    • Jatropha curcas L., amultipurpose stress resistant plant with a potential for ethnomedicine and renewable energy
    • Debnath, M. & Bisen, P. S. Jatropha curcas L., amultipurpose stress resistant plant with a potential for ethnomedicine and renewable energy. Curr. Pharm. Biotechnol. 9, 288-306 (2008).
    • (2008) Curr. Pharm. Biotechnol. , vol.9 , pp. 288-306
    • Debnath, M.1    Bisen, P.S.2
  • 25
    • 0012271650 scopus 로고
    • The poisonous principles of the seeds of Jatropha curcas Linn
    • Felke, J. The poisonous principles of the seeds of Jatropha curcas Linn. Landw. Versuchsw. 82, 427-430 (1914).
    • (1914) Landw. Versuchsw. , vol.82 , pp. 427-430
    • Felke, J.1
  • 26
    • 0037336184 scopus 로고    scopus 로고
    • Antitumor effects of curcin from seeds of Jatropha curcas
    • Juan, L., Fang, Y., Lin, T. & Fang, C. Antitumor effects of curcin from seeds of Jatropha curcas. Acta Pharmacol. Sin. 24, 241-246 (2003).
    • (2003) Acta Pharmacol. Sin. , vol.24 , pp. 241-246
    • Juan, L.1    Fang, Y.2    Lin, T.3    Fang, C.4
  • 27
    • 0141760478 scopus 로고    scopus 로고
    • Cloning and expression of curcin, a ribosome-inactivating protein from the seeds of Jatropha curcas
    • Lin, J. et al. Cloning and expression of curcin, a ribosome-inactivating protein from the seeds of Jatropha curcas. Acta Bot. Sin. 45, 858-863 (2003).
    • (2003) Acta Bot. Sin. , vol.45 , pp. 858-863
    • Lin, J.1
  • 28
    • 22244437941 scopus 로고    scopus 로고
    • Expression of a ribosome inactivating protein (curcin 2) in Jatropha curcas is induced by stress
    • Qin, W., Ming-Xing, H., Ying, X., Xin-Shen, Z. & Fang, C. Expression of a ribosome inactivating protein (curcin 2) in Jatropha curcas is induced by stress. J. Biosci. 30, 351-357 (2005).
    • (2005) J. Biosci. , vol.30 , pp. 351-357
    • Qin, W.1    Ming-Xing, H.2    Ying, X.3    Xin-Shen, Z.4    Fang, C.5
  • 29
    • 84876382662 scopus 로고    scopus 로고
    • Expression of curcin-transferrin receptor binding peptide fusion protein and its anti-tumor activity
    • Zheng, Q. et al. Expression of curcin-transferrin receptor binding peptide fusion protein and its anti-tumor activity. Protein Expr Purif. 89, 181-188 (2013).
    • (2013) Protein Expr Purif. , vol.89 , pp. 181-188
    • Zheng, Q.1
  • 30
    • 84897824713 scopus 로고    scopus 로고
    • Type 1 ribotoxin-curcin conjugated biogenic gold nanoparticles for a multimodal therapeutic approach towards brain cancer
    • Mohamed, M. S. et al. Type 1 ribotoxin-curcin conjugated biogenic gold nanoparticles for a multimodal therapeutic approach towards brain cancer. Biochim Biophys Acta. (2013) http://dx.doi.org/10.1016/j.bbagen.2013.12.020.
    • (2013) Biochim Biophys Acta.
    • Mohamed, M.S.1
  • 31
    • 80053203292 scopus 로고    scopus 로고
    • Natural products: An evolving role in future drug discovery
    • Mishra, B. B. & Tiwari, V. K. Natural products: an evolving role in future drug discovery. Eur. J. Med. Chem. 46, 4769-807 (2011).
    • (2011) Eur. J. Med. Chem. , vol.46 , pp. 4769-4807
    • Mishra, B.B.1    Tiwari, V.K.2
  • 32
    • 84855281811 scopus 로고    scopus 로고
    • Natural products: Promising resources for cancer drug discovery
    • Mondal, S. et al. Natural products: promising resources for cancer drug discovery. Anticancer Agents Med Chem. 12, 49-75 (2012).
    • (2012) Anticancer Agents Med Chem. , vol.12 , pp. 49-75
    • Mondal, S.1
  • 33
    • 33748686346 scopus 로고    scopus 로고
    • Expression, purification and anti-tumor activity of curcin
    • Luo, M. J. et al. Expression, purification and anti-tumor activity of curcin. Acta Biochim. Biophys. Sin. (Shanghai). 38, 663-668 (2006).
    • (2006) Acta Biochim. Biophys. Sin. (Shanghai) , vol.38 , pp. 663-668
    • Luo, M.J.1
  • 34
    • 84861607615 scopus 로고    scopus 로고
    • The effect of curcin from Jatropha curcas on apoptosis of mouse sarcoma-180 cells
    • Zhao, Q., Wang, W., Wang, Y., Xu, Y. & Chen, F. The effect of curcin from Jatropha curcas on apoptosis of mouse sarcoma-180 cells. Fitoterapia 83, 849-852 (2012).
    • (2012) Fitoterapia , vol.83 , pp. 849-852
    • Zhao, Q.1    Wang, W.2    Wang, Y.3    Xu, Y.4    Chen, F.5
  • 35
    • 0037336184 scopus 로고    scopus 로고
    • Antitumor effects of curcin from seeds of Jatropha curcas
    • Lin, J., Yan, F., Tang, L. & Chen, F. Antitumor effects of curcin from seeds of Jatropha curcas. Acta Pharmacol. Sin. 24, 241-246 (2003).
    • (2003) Acta Pharmacol. Sin. , vol.24 , pp. 241-246
    • Lin, J.1    Yan, F.2    Tang, L.3    Chen, F.4
  • 36
    • 84876382662 scopus 로고    scopus 로고
    • Expression of curcin-transferrin receptor binding peptide fusion protein and its anti-tumor activity
    • Zheng, Q. et al. Expression of curcin-transferrin receptor binding peptide fusion protein and its anti-tumor activity. Protein Expr. Purif. 89, 181-188 (2013).
    • (2013) Protein Expr. Purif. , vol.89 , pp. 181-188
    • Zheng, Q.1
  • 37
    • 57649149333 scopus 로고    scopus 로고
    • Classification of cell death: Recommendations of the nomenclature committee on cell death
    • Kroemer, G. et al. Classification of cell death: recommendations of the nomenclature committee on cell death. Cell. Death Differ. 16, 3-11 (2009).
    • (2009) Cell. Death Differ. , vol.16 , pp. 3-11
    • Kroemer, G.1
  • 38
    • 2342481172 scopus 로고    scopus 로고
    • Programmed cell deaths. Apoptosis and alternative deathstyles
    • Guimarães, C. A. & Linden, R. Programmed cell deaths. Apoptosis and alternative deathstyles. Eur. J. Biochem. 271, 1638-1650 (2004).
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1638-1650
    • Guimarães, C.A.1    Linden, R.2
  • 39
    • 33745226982 scopus 로고    scopus 로고
    • Downregulation of survivin expression and concomitant induction of apoptosis by celecoxib and its non-cyclooxygenase-2-inhibitory analog, dimethyl-celecoxib (DMC), in tumor cells in vitro and in vivo
    • Pyrko, P. et al. Downregulation of survivin expression and concomitant induction of apoptosis by celecoxib and its non-cyclooxygenase-2-inhibitory analog, dimethyl-celecoxib (DMC), in tumor cells in vitro and in vivo. Mol. Cancer 5, 19 (2006).
    • (2006) Mol. Cancer , vol.5 , pp. 19
    • Pyrko, P.1
  • 40
    • 0346250160 scopus 로고    scopus 로고
    • Survivin, versatile modulation of cell division and apoptosis in cancer
    • Altieri, D. C. et al. Survivin, versatile modulation of cell division and apoptosis in cancer. Oncogene, 22, 8581-8589 (2003).
    • (2003) Oncogene , vol.22 , pp. 8581-8589
    • Altieri, D.C.1
  • 41
    • 3042552397 scopus 로고    scopus 로고
    • Ribozyme-mediated down-regula-tion of survivin expression sensitizes human melanoma cells to topotecan in vitro and in vivo
    • Pennati, M. et al. Ribozyme-mediated down-regula-tion of survivin expression sensitizes human melanoma cells to topotecan in vitro and in vivo. Carcinogenesis 25, 1129-1136 (2004).
    • (2004) Carcinogenesis , vol.25 , pp. 1129-1136
    • Pennati, M.1
  • 42
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • Green, D. R. & Kroemer, G. The pathophysiology of mitochondrial cell death. Science 305, 626-629 (2004).
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 43
    • 84900551341 scopus 로고    scopus 로고
    • Morphological Features of Organelles during Apoptosis: An Overview
    • Bottone, M. G. et al. Morphological Features of Organelles during Apoptosis: An Overview. Cells 2, 294-305 (2013).
    • (2013) Cells , vol.2 , pp. 294-305
    • Bottone, M.G.1
  • 44
    • 78650894319 scopus 로고    scopus 로고
    • Crosstalk of reactive oxygen species and NF-κB signaling
    • Morgan, M. J. & Liu, Z. Crosstalk of reactive oxygen species and NF-κB signaling. Cell Research 21, 103-115 (2011).
    • (2011) Cell Research , vol.21 , pp. 103-115
    • Morgan, M.J.1    Liu, Z.2
  • 45
    • 84859897794 scopus 로고    scopus 로고
    • Regulation of reactive oxygen species generation incell signaling
    • Bae, Y. S., Oh, H., Rhee, S. G. & Do, Y. Y. Regulation of reactive oxygen species generation incell signaling. Molecules and Cells 32, 491-509 (2011).
    • (2011) Molecules and Cells , vol.32 , pp. 491-509
    • Bae, Y.S.1    Oh, H.2    Rhee, S.G.3    Do, Y.Y.4
  • 46
    • 73849095427 scopus 로고    scopus 로고
    • The nuclear signaling of NF-kappaB: Current knowledge, new insights, and future perspectives
    • Wan, F. & Lenardo, M. J. The nuclear signaling of NF-kappaB: current knowledge, new insights, and future perspectives. Cell Research 20, 24-33 (2010).
    • (2010) Cell Research , vol.20 , pp. 24-33
    • Wan, F.1    Lenardo, M.J.2
  • 47
    • 84858957528 scopus 로고    scopus 로고
    • Nuclear PARP-1 protein overexpression is associated with poor overall survival in early breast cancer
    • Rojo, F. et al. Nuclear PARP-1 protein overexpression is associated with poor overall survival in early breast cancer. Ann. Oncol. 23, 1156-1164 (2012).
    • (2012) Ann. Oncol. , vol.23 , pp. 1156-1164
    • Rojo, F.1
  • 48
    • 84857936584 scopus 로고    scopus 로고
    • Advances in using PARP inhibitors to treat cancer
    • Kummar, S. et al. Advances in using PARP inhibitors to treat cancer. BMC Med. 10, 25 (2012).
    • (2012) BMC Med. , vol.10 , pp. 25
    • Kummar, S.1
  • 49
    • 77957842603 scopus 로고    scopus 로고
    • Apoptotic volume decrease as a geometric determinant for cell dismantling into apoptotic bodies
    • Núñez, R., Sancho-Martínez, S. M., Novoa, J. M. & López-Hernández, F. J. Apoptotic volume decrease as a geometric determinant for cell dismantling into apoptotic bodies. Cell Death Differ. 17, 1665-1671 (2010).
    • (2010) Cell Death Differ. , vol.17 , pp. 1665-1671
    • Núñez, R.1    Sancho-Martínez, S.M.2    Novoa, J.M.3    López-Hernández, F.J.4
  • 50
    • 33847295719 scopus 로고    scopus 로고
    • Mechanism of depolymerization and severing of actin filaments and its significance in cytoskeletal dynamics
    • Ono, S. Mechanism of depolymerization and severing of actin filaments and its significance in cytoskeletal dynamics. Int. Rev. Cytol. 258, 1-82 (2007).
    • (2007) Int. Rev. Cytol. , vol.258 , pp. 1-82
    • Ono, S.1
  • 51
    • 77954486800 scopus 로고    scopus 로고
    • Measuring mechanical tension across vinculin reveals regula-tion of focal adhesion dynamics
    • Grashoff, C. Measuring mechanical tension across vinculin reveals regula-tion of focal adhesion dynamics. Nature 466, 263-266 (2010).
    • (2010) Nature , vol.466 , pp. 263-266
    • Grashoff, C.1
  • 52
    • 84880642716 scopus 로고    scopus 로고
    • Vinculin-actin interaction couples actin retrograde flow to focal adhesions, but is dispensable for focal adhesion growth
    • Thievessen, I. et al. Vinculin-actin interaction couples actin retrograde flow to focal adhesions, but is dispensable for focal adhesion growth. J Cell Biol. 202, 163-177 (2013).
    • (2013) J Cell Biol. , vol.202 , pp. 163-177
    • Thievessen, I.1
  • 53
    • 0028345285 scopus 로고
    • Lipoic and dihydrolipoic acids as antioxidants. A critical evaluation
    • Scott, B. C. et al. Lipoic and dihydrolipoic acids as antioxidants. A critical evaluation. Free Radic. Res. 20, 119-133 (1994).
    • (1994) Free Radic. Res. , vol.20 , pp. 119-133
    • Scott, B.C.1
  • 54
    • 0023855455 scopus 로고
    • Action mechanism of amphipathic peptides gramicidin S and melittin on erythrocyte membrane
    • Katsu, T., Ninomiya, C. & Kuroko, M. Action mechanism of amphipathic peptides gramicidin S and melittin on erythrocyte membrane. Biochim. Biophys. Acta 939, 57-63 (1988).
    • (1988) Biochim. Biophys. Acta , vol.939 , pp. 57-63
    • Katsu, T.1    Ninomiya, C.2    Kuroko, M.3
  • 55
    • 0032531290 scopus 로고    scopus 로고
    • Hemocompatibility of treated polystyrene substrates: Contact activation, platelet adhesion, and procoagulant activity of adherent platelets
    • Grunkemeier, J. M., Tsai, W. B. & Horbett, T. A. Hemocompatibility of treated polystyrene substrates: contact activation, platelet adhesion, and procoagulant activity of adherent platelets. J. Biomed. Mater. Res. 41, 657-670 (1998).
    • (1998) J. Biomed. Mater. Res. , vol.41 , pp. 657-670
    • Grunkemeier, J.M.1    Tsai, W.B.2    Horbett, T.A.3
  • 56
    • 33646345346 scopus 로고    scopus 로고
    • Hemocompatibility evaluation of poly(glycerol-sebacate) in vitro for vascular tissue engineering
    • Motlagh, D., Yang, J., Lui, K. Y., Webb, A. R. & Ameer, G. A. Hemocompatibility evaluation of poly(glycerol-sebacate) in vitro for vascular tissue engineering. Biomaterials 24, 4315-4324 (2006).
    • (2006) Biomaterials , vol.24 , pp. 4315-4324
    • Motlagh, D.1    Yang, J.2    Lui, K.Y.3    Webb, A.R.4    Ameer, G.A.5
  • 57
    • 0029239613 scopus 로고
    • Simple method for platelet counting
    • Tamada, Y., Kulik, E. A. & Ikada, Y. Simple method for platelet counting. Biomaterials 16, 259-261 (1995).
    • (1995) Biomaterials , vol.16 , pp. 259-261
    • Tamada, Y.1    Kulik, E.A.2    Ikada, Y.3


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