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Volumn 27, Issue 1, 2013, Pages 220-231

Insights into the mechanism of cell death induced by saporin delivered into cancer cells by an antibody fusion protein targeting the transferrin receptor 1

Author keywords

Immunotoxin; Oxidative stress; Ribosome inactivating protein; Saporin; Transferrin receptor 1

Indexed keywords

ACETYLCYSTEINE; ANTIBODY AVIDIN FUSION PROTEIN; CASPASE; CD71 ANTIGEN; DNA; HYBRID PROTEIN; SAPORIN; UNCLASSIFIED DRUG;

EID: 84869427890     PISSN: 08872333     EISSN: 18793177     Source Type: Journal    
DOI: 10.1016/j.tiv.2012.10.006     Document Type: Article
Times cited : (26)

References (67)
  • 1
    • 0035312922 scopus 로고    scopus 로고
    • THUMP-a predicted RNA-binding domain shared by 4-thiouridine, pseudouridine synthases and RNA methylases
    • Aravind L., Koonin E.V. THUMP-a predicted RNA-binding domain shared by 4-thiouridine, pseudouridine synthases and RNA methylases. Trends Biochem. Sci. 2001, 26:215-217.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 215-217
    • Aravind, L.1    Koonin, E.V.2
  • 2
    • 0013001418 scopus 로고    scopus 로고
    • The cytotoxic activity of ribosome-inactivating protein saporin-6 is attributed to its rRNA N-glycosidase and internucleosomal DNA fragmentation activities
    • Bagga S., Seth D., Batra J.K. The cytotoxic activity of ribosome-inactivating protein saporin-6 is attributed to its rRNA N-glycosidase and internucleosomal DNA fragmentation activities. J. Biol. Chem. 2003, 278:4813-4820.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4813-4820
    • Bagga, S.1    Seth, D.2    Batra, J.K.3
  • 3
    • 36148945617 scopus 로고    scopus 로고
    • R4 RGS proteins: regulation of G-protein signaling and beyond
    • Bansal G., Druey K.M., Xie Z. R4 RGS proteins: regulation of G-protein signaling and beyond. Pharmacol. Ther. 2007, 116:473-495.
    • (2007) Pharmacol. Ther. , vol.116 , pp. 473-495
    • Bansal, G.1    Druey, K.M.2    Xie, Z.3
  • 8
    • 84954358196 scopus 로고    scopus 로고
    • Abrin induced oxidative stress mediated DNA damage in human leukemic cells and its reversal by N-acetylcysteine
    • Bhaskar A.S., Deb U., Kumar O., Lakshmana Rao P.V. Abrin induced oxidative stress mediated DNA damage in human leukemic cells and its reversal by N-acetylcysteine. Toxicol. In Vitro 2008, 22:1902-1908.
    • (2008) Toxicol. In Vitro , vol.22 , pp. 1902-1908
    • Bhaskar, A.S.1    Deb, U.2    Kumar, O.3    Lakshmana Rao, P.V.4
  • 9
    • 27944476715 scopus 로고    scopus 로고
    • Escherichia coli verotoxin 1 mediates apoptosis in human HCT116 colon cancer cells by inducing overexpression of the GADD family of genes and S phase arrest
    • Bhattacharjee R.N., Park K.S., Uematsu S., Okada K., Hoshino K., Takeda K., Takeuchi O., Akira S., Iida T., Honda T. Escherichia coli verotoxin 1 mediates apoptosis in human HCT116 colon cancer cells by inducing overexpression of the GADD family of genes and S phase arrest. FEBS Lett. 2005, 579:6604-6610.
    • (2005) FEBS Lett. , vol.579 , pp. 6604-6610
    • Bhattacharjee, R.N.1    Park, K.S.2    Uematsu, S.3    Okada, K.4    Hoshino, K.5    Takeda, K.6    Takeuchi, O.7    Akira, S.8    Iida, T.9    Honda, T.10
  • 11
    • 84857999640 scopus 로고    scopus 로고
    • Minimal influence of G-protein null mutations on ozone-induced changes in gene expression, foliar injury, gas exchange and peroxidase activity in Arabidopsis thaliana L
    • Booker F., Burkey K., Morgan P., Fiscus E., Jones A. Minimal influence of G-protein null mutations on ozone-induced changes in gene expression, foliar injury, gas exchange and peroxidase activity in Arabidopsis thaliana L. Plant Cell Environ. 2012, 35:668-681.
    • (2012) Plant Cell Environ. , vol.35 , pp. 668-681
    • Booker, F.1    Burkey, K.2    Morgan, P.3    Fiscus, E.4    Jones, A.5
  • 13
    • 33750471197 scopus 로고    scopus 로고
    • Mutual cross-talk between reactive oxygen species and nuclear factor-kappa B: molecular basis and biological significance
    • Bubici C., Papa S., Dean K., Franzoso G. Mutual cross-talk between reactive oxygen species and nuclear factor-kappa B: molecular basis and biological significance. Oncogene 2006, 25:6731-6748.
    • (2006) Oncogene , vol.25 , pp. 6731-6748
    • Bubici, C.1    Papa, S.2    Dean, K.3    Franzoso, G.4
  • 15
    • 35648981177 scopus 로고    scopus 로고
    • Mapping of oxidative stress responses of human tumor cells following photodynamic therapy using hexaminolevulinate
    • Cekaite L., Peng Q., Reiner A., Shahzidi S., Tveito S., Furre I.E., Hovig E. Mapping of oxidative stress responses of human tumor cells following photodynamic therapy using hexaminolevulinate. BMC Genomics 2007, 8:273.
    • (2007) BMC Genomics , vol.8 , pp. 273
    • Cekaite, L.1    Peng, Q.2    Reiner, A.3    Shahzidi, S.4    Tveito, S.5    Furre, I.E.6    Hovig, E.7
  • 17
    • 67549107386 scopus 로고    scopus 로고
    • Caspase activation pathways: some recent progress
    • Cullen S.P., Martin S.J. Caspase activation pathways: some recent progress. Cell Death Differ. 2009, 16:935-938.
    • (2009) Cell Death Differ. , vol.16 , pp. 935-938
    • Cullen, S.P.1    Martin, S.J.2
  • 18
    • 43549107895 scopus 로고    scopus 로고
    • Differential regulation of Kruppel-like factor family transcription factor expression in neonatal rat cardiac myocytes: effects of endothelin-1, oxidative stress and cytokines
    • Cullingford T.E., Butler M.J., Marshall A.K., Tham el L., Sugden P.H., Clerk A. Differential regulation of Kruppel-like factor family transcription factor expression in neonatal rat cardiac myocytes: effects of endothelin-1, oxidative stress and cytokines. Biochim. Biophys. Acta 2008, 1783:1229-1236.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 1229-1236
    • Cullingford, T.E.1    Butler, M.J.2    Marshall, A.K.3    Tham el, L.4    Sugden, P.H.5    Clerk, A.6
  • 20
    • 33750019824 scopus 로고    scopus 로고
    • The transferrin receptor part II: targeted delivery of therapeutic agents into cancer cells
    • Daniels T.R., Delgado T., Helguera G., Penichet M.L. The transferrin receptor part II: targeted delivery of therapeutic agents into cancer cells. Clin. Immunol. 2006, 121:159-176.
    • (2006) Clin. Immunol. , vol.121 , pp. 159-176
    • Daniels, T.R.1    Delgado, T.2    Helguera, G.3    Penichet, M.L.4
  • 21
    • 33750008791 scopus 로고    scopus 로고
    • The transferrin receptor part I: biology and targeting with cytotoxic antibodies for the treatment of cancer
    • Daniels T.R., Delgado T., Rodríguez J.A., Helguera G., Penichet M.L. The transferrin receptor part I: biology and targeting with cytotoxic antibodies for the treatment of cancer. Clin. Immunol. 2006, 121:144-158.
    • (2006) Clin. Immunol. , vol.121 , pp. 144-158
    • Daniels, T.R.1    Delgado, T.2    Rodríguez, J.A.3    Helguera, G.4    Penichet, M.L.5
  • 22
    • 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
    • Daniels T.R., Ng P.P., Delgado T., Lynch M.R., Schiller G., Helguera G., Penichet M.L. 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. 2007, 6:2995-3008.
    • (2007) Mol. Cancer Ther. , vol.6 , pp. 2995-3008
    • Daniels, T.R.1    Ng, P.P.2    Delgado, T.3    Lynch, M.R.4    Schiller, G.5    Helguera, G.6    Penichet, M.L.7
  • 25
  • 27
    • 80051778368 scopus 로고    scopus 로고
    • Mitochondria in cancer: at the crossroads of life and death
    • Fogg V.C., Lanning N.J., Mackeigan J.P. Mitochondria in cancer: at the crossroads of life and death. Chin. J. Cancer 2011, 30:526-539.
    • (2011) Chin. J. Cancer , vol.30 , pp. 526-539
    • Fogg, V.C.1    Lanning, N.J.2    Mackeigan, J.P.3
  • 29
    • 13944280312 scopus 로고    scopus 로고
    • Mitochondrial DNA D-loop as a new target of saporin 6 nuclease activity
    • Gasperi-Campani A., Brognara I., Baiocchi D., Roncuzzi L. Mitochondrial DNA D-loop as a new target of saporin 6 nuclease activity. Toxicon 2005, 45:475-480.
    • (2005) Toxicon , vol.45 , pp. 475-480
    • Gasperi-Campani, A.1    Brognara, I.2    Baiocchi, D.3    Roncuzzi, L.4
  • 30
    • 62049086099 scopus 로고    scopus 로고
    • The pathobiology of kruppel-like factors in colorectal cancer
    • Ghaleb A.M., Yang V.W. The pathobiology of kruppel-like factors in colorectal cancer. Curr. Colorectal Cancer Rep. 2008, 4:59-64.
    • (2008) Curr. Colorectal Cancer Rep. , vol.4 , pp. 59-64
    • Ghaleb, A.M.1    Yang, V.W.2
  • 31
    • 0030781105 scopus 로고    scopus 로고
    • Characterization and phenotypic analysis of differentiating CD34+ human bone marrow cells in liquid culture
    • Gross S., Helm K., Gruntmeir J.J., Stillman W.S., Pyatt D.W., Irons R.D. Characterization and phenotypic analysis of differentiating CD34+ human bone marrow cells in liquid culture. Eur. J. Haematol. 1997, 59:318-326.
    • (1997) Eur. J. Haematol. , vol.59 , pp. 318-326
    • Gross, S.1    Helm, K.2    Gruntmeir, J.J.3    Stillman, W.S.4    Pyatt, D.W.5    Irons, R.D.6
  • 32
    • 44949178277 scopus 로고    scopus 로고
    • Dual regulation of glucocorticoid-induced leucine zipper (GILZ) by the glucocorticoid receptor and the PI3-kinase/AKT pathways in multiple myeloma
    • Grugan K.D., Ma C., Singhal S., Krett N.L., Rosen S.T. Dual regulation of glucocorticoid-induced leucine zipper (GILZ) by the glucocorticoid receptor and the PI3-kinase/AKT pathways in multiple myeloma. J. Steroid Biochem. Mol. Biol. 2008, 110:244-254.
    • (2008) J. Steroid Biochem. Mol. Biol. , vol.110 , pp. 244-254
    • Grugan, K.D.1    Ma, C.2    Singhal, S.3    Krett, N.L.4    Rosen, S.T.5
  • 35
    • 11144247941 scopus 로고    scopus 로고
    • Administration of ricin induces a severe inflammatory response via nonredundant stimulation of ERK, JNK, and P38 MAPK and provides a mouse model of hemolytic uremic syndrome
    • Korcheva V., Wong J., Corless C., Iordanov M., Magun B. Administration of ricin induces a severe inflammatory response via nonredundant stimulation of ERK, JNK, and P38 MAPK and provides a mouse model of hemolytic uremic syndrome. Am. J. Pathol. 2005, 166:323-339.
    • (2005) Am. J. Pathol. , vol.166 , pp. 323-339
    • Korcheva, V.1    Wong, J.2    Corless, C.3    Iordanov, M.4    Magun, B.5
  • 37
    • 51849151811 scopus 로고    scopus 로고
    • Enhanced cytotoxicity of saporin by polyamidoamine dendrimer conjugation and photochemical internalization
    • Lai P.S., Pai C.L., Peng C.L., Shieh M.J., Berg K., Lou P.J. Enhanced cytotoxicity of saporin by polyamidoamine dendrimer conjugation and photochemical internalization. J. Biomed. Mater. Res. A 2008, 87:147-155.
    • (2008) J. Biomed. Mater. Res. A , vol.87 , pp. 147-155
    • Lai, P.S.1    Pai, C.L.2    Peng, C.L.3    Shieh, M.J.4    Berg, K.5    Lou, P.J.6
  • 38
    • 0026505736 scopus 로고
    • Long-term erythropoiesis from constant numbers of CD34+ cells in serum-free cultures initiated with highly purified progenitor cells from human bone marrow
    • Lansdorp P.M., Dragowska W. Long-term erythropoiesis from constant numbers of CD34+ cells in serum-free cultures initiated with highly purified progenitor cells from human bone marrow. J. Exp. Med. 1992, 175:1501-1509.
    • (1992) J. Exp. Med. , vol.175 , pp. 1501-1509
    • Lansdorp, P.M.1    Dragowska, W.2
  • 39
    • 0030756303 scopus 로고    scopus 로고
    • A new member of the I kappaB protein family, I kappaB epsilon, inhibits RelA (p65)-mediated NF-kappaB transcription
    • Li Z., Nabel G.J. A new member of the I kappaB protein family, I kappaB epsilon, inhibits RelA (p65)-mediated NF-kappaB transcription. Mol. Cell. Biol. 1997, 17:6184-6190.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6184-6190
    • Li, Z.1    Nabel, G.J.2
  • 40
    • 78651384731 scopus 로고    scopus 로고
    • Type I ribosome-inactivating proteins from Saponaria officinialis
    • Springer-Verlag, Berlin Heidelberg, Germany, J.M. Lord, M.R. Hartley (Eds.)
    • Lombardi A., Marshall R.S., Savino C., Serena Fabrini M., Ceriotti A. Type I ribosome-inactivating proteins from Saponaria officinialis. Toxic Plant Proteins 2010, 55-78. Springer-Verlag, Berlin Heidelberg, Germany. J.M. Lord, M.R. Hartley (Eds.).
    • (2010) Toxic Plant Proteins , pp. 55-78
    • Lombardi, A.1    Marshall, R.S.2    Savino, C.3    Serena Fabrini, M.4    Ceriotti, A.5
  • 41
    • 84871232740 scopus 로고    scopus 로고
    • Oxidative stress in apoptosis and cancer: an update
    • (Epub ahead of print)
    • Mates J.M., Segura J.A., Alonso F.J., Marquez J. Oxidative stress in apoptosis and cancer: an update. Arch. Toxicol. 2012, 19-25. (Epub ahead of print).
    • (2012) Arch. Toxicol. , pp. 19-25
    • Mates, J.M.1    Segura, J.A.2    Alonso, F.J.3    Marquez, J.4
  • 43
    • 0036678172 scopus 로고    scopus 로고
    • An anti-transferrin receptor-avidin fusion protein exhibits both strong proapoptotic activity and the ability to deliver various molecules into cancer cells
    • Ng P.P., Dela Cruz J.S., Sorour D.N., Stinebaugh J.M., Shin S.U., Shin D.S., Morrison S.L., Penichet M.L. An anti-transferrin receptor-avidin fusion protein exhibits both strong proapoptotic activity and the ability to deliver various molecules into cancer cells. Proc. Natl. Acad. Sci. USA 2002, 99:10706-10711.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10706-10711
    • Ng, P.P.1    Dela Cruz, J.S.2    Sorour, D.N.3    Stinebaugh, J.M.4    Shin, S.U.5    Shin, D.S.6    Morrison, S.L.7    Penichet, M.L.8
  • 44
    • 33750631022 scopus 로고    scopus 로고
    • Molecular events contributing to cell death in malignant human hematopoietic cells elicited by an IgG3-avidin fusion protein targeting the transferrin receptor
    • Ng P.P., Helguera G., Daniels T.R., Lomas S.Z., Rodríguez J.A., Schiller G., Bonavida B., Morrison S.L., Penichet M.L. Molecular events contributing to cell death in malignant human hematopoietic cells elicited by an IgG3-avidin fusion protein targeting the transferrin receptor. Blood 2006, 108:2745-2754.
    • (2006) Blood , vol.108 , pp. 2745-2754
    • Ng, P.P.1    Helguera, G.2    Daniels, T.R.3    Lomas, S.Z.4    Rodríguez, J.A.5    Schiller, G.6    Bonavida, B.7    Morrison, S.L.8    Penichet, M.L.9
  • 45
    • 58249123414 scopus 로고    scopus 로고
    • Enhanced cytotoxicity of an anti-transferrin receptor IgG3-avidin fusion protein in combination with gambogic acid against human malignant hematopoietic cells: functional relevance of iron, the receptor, and reactive oxygen species
    • Ortiz-Sánchez E., Daniels T.R., Helguera G., Martinez-Maza O., Bonavida B., Penichet M.L. Enhanced cytotoxicity of an anti-transferrin receptor IgG3-avidin fusion protein in combination with gambogic acid against human malignant hematopoietic cells: functional relevance of iron, the receptor, and reactive oxygen species. Leukemia 2009, 23:59-70.
    • (2009) Leukemia , vol.23 , pp. 59-70
    • Ortiz-Sánchez, E.1    Daniels, T.R.2    Helguera, G.3    Martinez-Maza, O.4    Bonavida, B.5    Penichet, M.L.6
  • 46
    • 78549234756 scopus 로고    scopus 로고
    • Induction of DNA damage-inducible gene GADD45beta contributes to sorafenib-induced apoptosis in hepatocellular carcinoma cells
    • Ou D.L., Shen Y.C., Yu S.L., Chen K.F., Yeh P.Y., Fan H.H., Feng W.C., Wang C.T., Lin L.I., Hsu C., Cheng A.L. Induction of DNA damage-inducible gene GADD45beta contributes to sorafenib-induced apoptosis in hepatocellular carcinoma cells. Cancer Res. 2010, 70:9309-9318.
    • (2010) Cancer Res. , vol.70 , pp. 9309-9318
    • Ou, D.L.1    Shen, Y.C.2    Yu, S.L.3    Chen, K.F.4    Yeh, P.Y.5    Fan, H.H.6    Feng, W.C.7    Wang, C.T.8    Lin, L.I.9    Hsu, C.10    Cheng, A.L.11
  • 48
    • 84857116578 scopus 로고    scopus 로고
    • Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling
    • Ray P.D., Huang B.W., Tsuji Y. Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling. Cell. Signal. 2012, 24:981-990.
    • (2012) Cell. Signal. , vol.24 , pp. 981-990
    • Ray, P.D.1    Huang, B.W.2    Tsuji, Y.3
  • 51
    • 0030593702 scopus 로고    scopus 로고
    • DNA-nuclease activity of the single-chain ribosome-inactivating proteins dianthin 30, saporin 6 and gelonin
    • Roncuzzi L., Gasperi-Campani A. DNA-nuclease activity of the single-chain ribosome-inactivating proteins dianthin 30, saporin 6 and gelonin. FEBS Lett. 1996, 392:16-20.
    • (1996) FEBS Lett. , vol.392 , pp. 16-20
    • Roncuzzi, L.1    Gasperi-Campani, A.2
  • 52
    • 0030906975 scopus 로고    scopus 로고
    • The unusual stability of saporin, a candidate for the synthesis of immunotoxins
    • Santanche S., Bellelli A., Brunori M. The unusual stability of saporin, a candidate for the synthesis of immunotoxins. Biochem. Biophys. Res. Commun. 1997, 234:129-132.
    • (1997) Biochem. Biophys. Res. Commun. , vol.234 , pp. 129-132
    • Santanche, S.1    Bellelli, A.2    Brunori, M.3
  • 53
    • 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. 2008, 40:2880-2888.
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 2880-2888
    • Sikriwal, D.1    Ghosh, P.2    Batra, J.K.3
  • 54
    • 33845800913 scopus 로고    scopus 로고
    • Gene-expression profiling during curcumin-induced apoptosis reveals downregulation of CXCR4
    • Skommer J., Wlodkowic D., Pelkonen J. Gene-expression profiling during curcumin-induced apoptosis reveals downregulation of CXCR4. Exp. Hematol. 2007, 35:84-95.
    • (2007) Exp. Hematol. , vol.35 , pp. 84-95
    • Skommer, J.1    Wlodkowic, D.2    Pelkonen, J.3
  • 55
  • 56
    • 34047158745 scopus 로고    scopus 로고
    • Stra13 is induced by genotoxic stress and regulates ionizing-radiation-induced apoptosis
    • Thin T.H., Li L., Chung T.K., Sun H., Taneja R. Stra13 is induced by genotoxic stress and regulates ionizing-radiation-induced apoptosis. EMBO Rep. 2007, 8:401-407.
    • (2007) EMBO Rep. , vol.8 , pp. 401-407
    • Thin, T.H.1    Li, L.2    Chung, T.K.3    Sun, H.4    Taneja, R.5
  • 57
    • 13244265558 scopus 로고    scopus 로고
    • NF-kappaB/Egr-1/Gadd45 are sequentially activated upon UVB irradiation to mediate epidermal cell death
    • Thyss R., Virolle V., Imbert V., Peyron J.F., Aberdam D., Virolle T. NF-kappaB/Egr-1/Gadd45 are sequentially activated upon UVB irradiation to mediate epidermal cell death. EMBO J. 2005, 24:128-137.
    • (2005) EMBO J. , vol.24 , pp. 128-137
    • Thyss, R.1    Virolle, V.2    Imbert, V.3    Peyron, J.F.4    Aberdam, D.5    Virolle, T.6
  • 59
    • 13744259293 scopus 로고    scopus 로고
    • Myeloma cell contamination of peripheral blood stem-cell grafts can predict the outcome in multiple myeloma patients after high-dose chemotherapy and autologous stem-cell transplantation
    • Vogel W., Kopp H.G., Kanz L., Einsele H. Myeloma cell contamination of peripheral blood stem-cell grafts can predict the outcome in multiple myeloma patients after high-dose chemotherapy and autologous stem-cell transplantation. J. Cancer Res. Clin. Oncol. 2005, 131:214-218.
    • (2005) J. Cancer Res. Clin. Oncol. , vol.131 , pp. 214-218
    • Vogel, W.1    Kopp, H.G.2    Kanz, L.3    Einsele, H.4
  • 61
    • 0030899121 scopus 로고    scopus 로고
    • I kappa B epsilon, a novel member of the I kappa B family, controls RelA and cRel NF-kappa B activity
    • Whiteside S.T., Epinat J.C., Rice N.R., Israel A. I kappa B epsilon, a novel member of the I kappa B family, controls RelA and cRel NF-kappa B activity. EMBO J. 1997, 16:1413-1426.
    • (1997) EMBO J. , vol.16 , pp. 1413-1426
    • Whiteside, S.T.1    Epinat, J.C.2    Rice, N.R.3    Israel, A.4
  • 62
    • 37149013733 scopus 로고    scopus 로고
    • Proinflammatory responses of human airway cells to ricin involve stress-activated protein kinases and NF-kappaB
    • Wong J., Korcheva V., Jacoby D.B., Magun B.E. Proinflammatory responses of human airway cells to ricin involve stress-activated protein kinases and NF-kappaB. Am. J. Physiol. Lung Cell. Mol. Physiol. 2007, 293:L1385-L1394.
    • (2007) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.293
    • Wong, J.1    Korcheva, V.2    Jacoby, D.B.3    Magun, B.E.4
  • 63
    • 21344471947 scopus 로고    scopus 로고
    • Basic helix-loop-helix transcription factors, BHLHB2 and BHLHB3; their gene expressions are regulated by multiple extracellular stimuli
    • Yamada K., Miyamoto K. Basic helix-loop-helix transcription factors, BHLHB2 and BHLHB3; their gene expressions are regulated by multiple extracellular stimuli. Front. Biosci. 2005, 10:3151-3171.
    • (2005) Front. Biosci. , vol.10 , pp. 3151-3171
    • Yamada, K.1    Miyamoto, K.2
  • 64
    • 33750904465 scopus 로고    scopus 로고
    • Role of thioredoxin in cell growth through interactions with signaling molecules
    • Yoshioka J., Schreiter E.R., Lee R.T. Role of thioredoxin in cell growth through interactions with signaling molecules. Antioxid. Redox Signal. 2006, 8:2143-2151.
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 2143-2151
    • Yoshioka, J.1    Schreiter, E.R.2    Lee, R.T.3
  • 66
    • 84892512827 scopus 로고    scopus 로고
    • Roles of thioredoxin binding protein (TXNIP) in oxidative stress apoptosis and cancer
    • (Epub ahead of print)
    • Zhou J., Chng W.J. Roles of thioredoxin binding protein (TXNIP) in oxidative stress apoptosis and cancer. Mitochondrion 2012, (Epub ahead of print).
    • (2012) Mitochondrion
    • Zhou, J.1    Chng, W.J.2
  • 67
    • 72449146886 scopus 로고    scopus 로고
    • Distinct mechanisms are utilized to induce stress sensor gadd45b by different stress stimuli
    • Zumbrun S.D., Hoffman B., Liebermann D.A. Distinct mechanisms are utilized to induce stress sensor gadd45b by different stress stimuli. J. Cell. Biochem. 2009, 108:1220-1231.
    • (2009) J. Cell. Biochem. , vol.108 , pp. 1220-1231
    • Zumbrun, S.D.1    Hoffman, B.2    Liebermann, D.A.3


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