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Volumn 27, Issue 3, 2008, Pages 471-480

Clinical biomarkers and imaging for radiotherapy-induced cell death

Author keywords

Annexin V; Apoptosis; Biomarker; Cell death; Imaging; Radiotherapy

Indexed keywords

BIOLOGICAL MARKER; LIPOCORTIN 5; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLSERINE; SPHINGOMYELIN;

EID: 47949118084     PISSN: 01677659     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10555-008-9131-1     Document Type: Review
Times cited : (73)

References (63)
  • 1
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan, D., & Weinberg, R. A. (2000). The hallmarks of cancer. Cell, 100, 57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 3
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner, M. O. (2000). The biochemistry of apoptosis. Nature, 407, 770-776.
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 4
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • Wang, X. (2001). The expanding role of mitochondria in apoptosis. Genes & Development, 15, 2922-2233.
    • (2001) Genes & Development , vol.15 , pp. 2922-2233
    • Wang, X.1
  • 5
    • 0036097786 scopus 로고    scopus 로고
    • Keeping killers on a tight leash: Transcriptional and post-translational control of the pro-apoptotic activity of BH3-only proteins
    • Puthalakath, H., & Strasser, A. (2002). Keeping killers on a tight leash: Transcriptional and post-translational control of the pro-apoptotic activity of BH3-only proteins. Cell Death and Differentiation, 9, 505-512.
    • (2002) Cell Death and Differentiation , vol.9 , pp. 505-512
    • Puthalakath, H.1    Strasser, A.2
  • 6
    • 0035876483 scopus 로고    scopus 로고
    • BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak
    • Zong, W. X., Lindsten, T., Ross, A. J., MacGregor, G. R., & Thompson, C. B. (2001). BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak. Genes & Development, 15, 1481-1486.
    • (2001) Genes & Development , vol.15 , pp. 1481-1486
    • Zong, W.X.1    Lindsten, T.2    Ross, A.J.3    MacGregor, G.R.4    Thompson, C.B.5
  • 7
    • 0034663829 scopus 로고    scopus 로고
    • TBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c
    • Wei, M. C., Lindsten, T., Mootha, V. K., Weiler, S., Gross, A., Ashiya, M., et al. (2000). tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c. Genes & Development, 14, 2060-2071.
    • (2000) Genes & Development , vol.14 , pp. 2060-2071
    • Wei, M.C.1    Lindsten, T.2    Mootha, V.K.3    Weiler, S.4    Gross, A.5    Ashiya, M.6
  • 8
    • 0033535350 scopus 로고    scopus 로고
    • Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis
    • Desagher, S., Osen-Sand, A., Nichols, A., Eskes, R., Montessuit, S., Lauper, S., et al. (1999). Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis. Journal of Cell Biology, 144, 891-901.
    • (1999) Journal of Cell Biology , vol.144 , pp. 891-901
    • Desagher, S.1    Osen-Sand, A.2    Nichols, A.3    Eskes, R.4    Montessuit, S.5    Lauper, S.6
  • 9
    • 0035853811 scopus 로고    scopus 로고
    • Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells
    • Antonsson, B., Montessuit, S., Sanchez, B., & Martinou, J. C. (2001). Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells. Journal of Biological Chemistry, 276, 11615-11623.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 11615-11623
    • Antonsson, B.1    Montessuit, S.2    Sanchez, B.3    Martinou, J.C.4
  • 10
    • 0034786019 scopus 로고    scopus 로고
    • BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis
    • Cheng, E. H., Wei, M. C., Weiler, S., Flavell, R. A., Mak, T. W., Lindsten, T., et al. (2001). BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis. Molecular Cell, 8, 705-711.
    • (2001) Molecular Cell , vol.8 , pp. 705-711
    • Cheng, E.H.1    Wei, M.C.2    Weiler, S.3    Flavell, R.A.4    Mak, T.W.5    Lindsten, T.6
  • 11
    • 0036728834 scopus 로고    scopus 로고
    • Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics
    • Letai, A., Bassik, M. C., Walensky, L. D., Sorcinelli, M. D., Weiler, S., & Korsmeyer, S. J. (2002). Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics. Cancer Cell, 2, 183-192.
    • (2002) Cancer Cell , vol.2 , pp. 183-192
    • Letai, A.1    Bassik, M.C.2    Walensky, L.D.3    Sorcinelli, M.D.4    Weiler, S.5    Korsmeyer, S.J.6
  • 12
  • 13
    • 0032532013 scopus 로고    scopus 로고
    • FLIP prevents apoptosis induced by death receptors but not by perforin/granzyme B, chemotherapeutic drugs, and gamma irradiation
    • Kataoka, T., Schröter, M., Hahne, M., Schneider, P., Irmler, M., Thome, M., et al. (1998). FLIP prevents apoptosis induced by death receptors but not by perforin/granzyme B, chemotherapeutic drugs, and gamma irradiation. Journal of Immunology, 161, 3936-3942.
    • (1998) Journal of Immunology , vol.161 , pp. 3936-3942
    • Kataoka, T.1    Schröter, M.2    Hahne, M.3    Schneider, P.4    Irmler, M.5    Thome, M.6
  • 14
    • 0032900335 scopus 로고    scopus 로고
    • Ordering of ceramide formation, caspase activation, and mitochondrial changes during CD95- and DNA damage-induced apoptosis
    • Tepper, A. D., de Vries, E., van Blitterswijk, W. J., & Borst, J. (1999). Ordering of ceramide formation, caspase activation, and mitochondrial changes during CD95- and DNA damage-induced apoptosis. Journal of Clinical Investigation, 103, 971-978.
    • (1999) Journal of Clinical Investigation , vol.103 , pp. 971-978
    • Tepper, A.D.1    De Vries, E.2    Van Blitterswijk, W.J.3    Borst, J.4
  • 15
    • 0025751550 scopus 로고
    • Bcl-2 inhibits multiple forms of apoptosis but not negative selection in thymocytes
    • Sentman, C. L., Shutter, C. L., Hockenberry, D., Kanagaa, O., & Korsmeyer, S. J. (1991). Bcl-2 inhibits multiple forms of apoptosis but not negative selection in thymocytes. Cell, 67, 879-888.
    • (1991) Cell , vol.67 , pp. 879-888
    • Sentman, C.L.1    Shutter, C.L.2    Hockenberry, D.3    Kanagaa, O.4    Korsmeyer, S.J.5
  • 16
    • 0028072523 scopus 로고
    • DNA damage can induce apoptosis in proliferating lymphoid cells via p53-independent mechanisms inhibitable by Bcl-2
    • Strasser, A., Harris, A. W., Jacks, T., & Cory, S. (1994). DNA damage can induce apoptosis in proliferating lymphoid cells via p53-independent mechanisms inhibitable by Bcl-2. Cell, 79, 189-192.
    • (1994) Cell , vol.79 , pp. 189-192
    • Strasser, A.1    Harris, A.W.2    Jacks, T.3    Cory, S.4
  • 17
    • 0028335717 scopus 로고
    • Tumor suppressor p53 is a regulator of bcl-2 and bax gene expression in vitro and in vivo
    • Miyashita, T., Kralewski, S., Krajewska, M., Wang, H. G., Lin, H. K., Liebermann, D. A., et al. (1994). Tumor suppressor p53 is a regulator of bcl-2 and bax gene expression in vitro and in vivo. Oncogene, 9, 1799-1805.
    • (1994) Oncogene , vol.9 , pp. 1799-1805
    • Miyashita, T.1    Kralewski, S.2    Krajewska, M.3    Wang, H.G.4    Lin, H.K.5    Liebermann, D.A.6
  • 18
    • 0028883179 scopus 로고
    • Tumor suppressor p53 is a direct transcriptional activator of the human bax gene
    • Miyashita, T., & Reed, J. C. (1995). Tumor suppressor p53 is a direct transcriptional activator of the human bax gene. Cell, 80, 293-299.
    • (1995) Cell , vol.80 , pp. 293-299
    • Miyashita, T.1    Reed, J.C.2
  • 19
    • 0037115539 scopus 로고    scopus 로고
    • Tissue-specific induction of p53 targets in vivo
    • Fei, P., Bernhard, E. J., & El-Deiry, W. S. (2002). Tissue-specific induction of p53 targets in vivo. Cancer Research, 62, 7316-7327.
    • (2002) Cancer Research , vol.62 , pp. 7316-7327
    • Fei, P.1    Bernhard, E.J.2    El-Deiry, W.S.3
  • 21
    • 0029935682 scopus 로고    scopus 로고
    • Involvement of the CD95 (APO-1/Fas) receptor/ligand system in drug-induced apoptosis in leukemia cells
    • Friesen, C., Herr, I., Krammer, P. H., & Debatin, K. M. (1996). Involvement of the CD95 (APO-1/Fas) receptor/ligand system in drug-induced apoptosis in leukemia cells. Nature Medicine, 2, 574-577.
    • (1996) Nature Medicine , vol.2 , pp. 574-577
    • Friesen, C.1    Herr, I.2    Krammer, P.H.3    Debatin, K.M.4
  • 22
    • 0040419494 scopus 로고    scopus 로고
    • Drug-induced apoptosis in hepatoma cells is mediated by the CD95 (APO-1/Fas) receptor/ligand system and involves activation of wild-type p53
    • Müller, M., Strand, S., Hug, H., Heinemann, E. M., Walczak, H., Hofmann, W. J., et al. (1997). Drug-induced apoptosis in hepatoma cells is mediated by the CD95 (APO-1/Fas) receptor/ligand system and involves activation of wild-type p53. Journal of Clinical Investigation, 99, 403-413.
    • (1997) Journal of Clinical Investigation , vol.99 , pp. 403-413
    • Müller, M.1    Strand, S.2    Hug, H.3    Heinemann, E.M.4    Walczak, H.5    Hofmann, W.J.6
  • 23
    • 0035912109 scopus 로고    scopus 로고
    • Sensitization of resistant lymphoma cells to irradiation-induced apoptosis by the death ligand TRAIL
    • Belka, C., Schmid, B., Marini, P., Durand, E., Rudner, J., Faltin, H., et al. (2001). Sensitization of resistant lymphoma cells to irradiation-induced apoptosis by the death ligand TRAIL. Oncogene, 20, 2190-2196.
    • (2001) Oncogene , vol.20 , pp. 2190-2196
    • Belka, C.1    Schmid, B.2    Marini, P.3    Durand, E.4    Rudner, J.5    Faltin, H.6
  • 24
    • 2642536197 scopus 로고    scopus 로고
    • Alkylating DNA damage stimulates a regulated form of necrotic cell death
    • Zong, W. X., Ditsworth, D., Bauer, D. E., Wang, Z. Q., & Thompson, C. B. (2004). Alkylating DNA damage stimulates a regulated form of necrotic cell death. Genes & Development, 18, 1272-1282.
    • (2004) Genes & Development , vol.18 , pp. 1272-1282
    • Zong, W.X.1    Ditsworth, D.2    Bauer, D.E.3    Wang, Z.Q.4    Thompson, C.B.5
  • 25
    • 33748941408 scopus 로고    scopus 로고
    • Selective induction of necrotic cell death in cancer cells by beta-lapachone through activation of DNA damage response pathway
    • Sun, X., Li, Y., Li, W., Zhang, B., Wang, A. J., Sun, J., et al. (2006). Selective induction of necrotic cell death in cancer cells by beta-lapachone through activation of DNA damage response pathway. Cell Cycle, 5, 2029-2035.
    • (2006) Cell Cycle , vol.5 , pp. 2029-2035
    • Sun, X.1    Li, Y.2    Li, W.3    Zhang, B.4    Wang, A.J.5    Sun, J.6
  • 27
    • 0031850793 scopus 로고    scopus 로고
    • Delayed DNA damage associated with mitotic catastrophe following X-irradiation of HeLa S3 cells
    • Ianzini, F., & Mackey, M. A. (1998). Delayed DNA damage associated with mitotic catastrophe following X-irradiation of HeLa S3 cells. Mutagenesis, 13, 337-344.
    • (1998) Mutagenesis , vol.13 , pp. 337-344
    • Ianzini, F.1    MacKey, M.A.2
  • 28
    • 33746077747 scopus 로고    scopus 로고
    • Condensin I recruitment and uneven chromatin condensation precede mitotic cell death in response to DNA damage
    • Blank, M., Lerenthal, Y., Mittelman, L., & Shiloh, Y. (2006). Condensin I recruitment and uneven chromatin condensation precede mitotic cell death in response to DNA damage. Journal of Cell Biology, 74, 195-206.
    • (2006) Journal of Cell Biology , vol.74 , pp. 195-206
    • Blank, M.1    Lerenthal, Y.2    Mittelman, L.3    Shiloh, Y.4
  • 30
    • 0038309329 scopus 로고    scopus 로고
    • The molecular mechanism of autophagy
    • Wang, C. W., & Klionsky, D. J. (2003). The molecular mechanism of autophagy. Molecular Medicine, 9, 65-76.
    • (2003) Molecular Medicine , vol.9 , pp. 65-76
    • Wang, C.W.1    Klionsky, D.J.2
  • 31
    • 0035863399 scopus 로고    scopus 로고
    • A novel response of cancer cells to radiation involves autophagy and formation of acidic vesicles
    • Paglin, S., Hollister, T., Delohery, T., Hackett, N., McMahill, M., Sphicas, E., et al. (2001). A novel response of cancer cells to radiation involves autophagy and formation of acidic vesicles. Cancer Research, 61, 439-444.
    • (2001) Cancer Research , vol.61 , pp. 439-444
    • Paglin, S.1    Hollister, T.2    Delohery, T.3    Hackett, N.4    McMahill, M.5    Sphicas, E.6
  • 32
    • 33748456755 scopus 로고    scopus 로고
    • Pathways that regulate autophagy and their role in mediating tumor response to treatment
    • Paglin, S., & Yahalom, J. (2006). Pathways that regulate autophagy and their role in mediating tumor response to treatment. Autophagy, 2, 291-293.
    • (2006) Autophagy , vol.2 , pp. 291-293
    • Paglin, S.1    Yahalom, J.2
  • 33
    • 1842583789 scopus 로고    scopus 로고
    • Development by self-digestion: Molecular mechanisms and biological functions of autophagy
    • Levine, B., & Klionsky, D. J. (2004). Development by self-digestion: Molecular mechanisms and biological functions of autophagy. Developmental Cell, 6, 463-747.
    • (2004) Developmental Cell , vol.6 , pp. 463-747
    • Levine, B.1    Klionsky, D.J.2
  • 34
    • 33745713171 scopus 로고    scopus 로고
    • Autophagy promotes tumor cell survival and restricts necrosis, inflammation, and tumorigenesis
    • Degenhardt, K., Mathew, R., Beaudoin, B., Bray, K., Anderson, D., Chen, G., et al. (2006). Autophagy promotes tumor cell survival and restricts necrosis, inflammation, and tumorigenesis. Cancer Cell, 10, 51-64.
    • (2006) Cancer Cell , vol.10 , pp. 51-64
    • Degenhardt, K.1    Mathew, R.2    Beaudoin, B.3    Bray, K.4    Anderson, D.5    Chen, G.6
  • 36
    • 0034069237 scopus 로고    scopus 로고
    • Cancer, aging and cellular senescence
    • Campisi, J. (2000). Cancer, aging and cellular senescence. In Vivo, 14, 183-188.
    • (2000) In Vivo , vol.14 , pp. 183-188
    • Campisi, J.1
  • 37
    • 0038277105 scopus 로고    scopus 로고
    • Tumor cell senescence in cancer treatment
    • Roninson, I. B. (2003). Tumor cell senescence in cancer treatment. Cancer Research, 63, 2705-2715.
    • (2003) Cancer Research , vol.63 , pp. 2705-2715
    • Roninson, I.B.1
  • 38
    • 0031766349 scopus 로고    scopus 로고
    • Radiation-induced apoptosis: The ceramide-SAPK signaling pathway and clinical aspects
    • Verheij, M., van Blitterswijk, W. J., & Bartelink, H. (1998). Radiation-induced apoptosis: The ceramide-SAPK signaling pathway and clinical aspects. Acta Oncológica, 37, 575-581.
    • (1998) Acta Oncológica , vol.37 , pp. 575-581
    • Verheij, M.1    Van Blitterswijk, W.J.2    Bartelink, H.3
  • 40
    • 0034749556 scopus 로고    scopus 로고
    • Prognostic factors in transitional cell cancer of the bladder: An emerging role for Bcl-2 and p53
    • Ong, F., Moonen, L. M. F., Gallee, M. P. W., ten Bosch, C., Zerp, S. F., Hart, A. A. M., et al. (2001). Prognostic factors in transitional cell cancer of the bladder: An emerging role for Bcl-2 and p53. Radiotherapy and Oncology, 61, 169-175.
    • (2001) Radiotherapy and Oncology , vol.61 , pp. 169-175
    • Ong, F.1    Moonen, L.M.F.2    Gallee, M.P.W.3    Ten Bosch, C.4    Zerp, S.F.5    Hart, A.A.M.6
  • 41
    • 0036083696 scopus 로고    scopus 로고
    • Annexins: From structure to function
    • Gerke, V., & Moss, S. E. (2002). Annexins: From structure to function. Physiological Reviews, 82, 331-371.
    • (2002) Physiological Reviews , vol.82 , pp. 331-371
    • Gerke, V.1    Moss, S.E.2
  • 43
    • 0024268328 scopus 로고
    • Sedimentation equilibrium analysis of five lipocortin-related phospholipase A2 inhibitors from human placenta. Evidence against a mechanistically relevant association between enzyme and inhibitor
    • Ahn, N. G., Teller, D. C., Bienkowski, M. J., McMullen, B. A., Lipkin, E. W., & de Haen, C. (1988). Sedimentation equilibrium analysis of five lipocortin-related phospholipase A2 inhibitors from human placenta. Evidence against a mechanistically relevant association between enzyme and inhibitor. Journal of Biological Chemistry, 263, 18657-18663.
    • (1988) Journal of Biological Chemistry , vol.263 , pp. 18657-18663
    • Ahn, N.G.1    Teller, D.C.2    Bienkowski, M.J.3    McMullen, B.A.4    Lipkin, E.W.5    De Haen, C.6
  • 45
    • 0027546634 scopus 로고
    • Interaction of annexin V and platelets: Effects on platelet function and protein S binding
    • Sun, J., Bird, P., & Salem, H. H. (1993). Interaction of annexin V and platelets: Effects on platelet function and protein S binding. Thrombosis Research, 69, 289-296.
    • (1993) Thrombosis Research , vol.69 , pp. 289-296
    • Sun, J.1    Bird, P.2    Salem, H.H.3
  • 46
    • 0028200038 scopus 로고
    • Annexin V as a probe of the contribution of anionic phospholipids to the procoagulant activity of tumour cell surfaces
    • Sugimura, M., Donato, R., Kakkar, V. V., & Scully, M. F. (1994). Annexin V as a probe of the contribution of anionic phospholipids to the procoagulant activity of tumour cell surfaces. Blood Coagulation & Fibrinolysis, 5, 365-373.
    • (1994) Blood Coagulation & Fibrinolysis , vol.5 , pp. 365-373
    • Sugimura, M.1    Donato, R.2    Kakkar, V.V.3    Scully, M.F.4
  • 48
    • 0034661803 scopus 로고    scopus 로고
    • Visualisation of cell death in vivo in patients with acute myocardial infarction
    • Hofstra, L., Liem, I. H., Dumont, E. A., Boersma, H. H., van Heerde, W. L., Doevendans, P. A., et al. (2000). Visualisation of cell death in vivo in patients with acute myocardial infarction. Lancet, 356, 209-212.
    • (2000) Lancet , vol.356 , pp. 209-212
    • Hofstra, L.1    Liem, I.H.2    Dumont, E.A.3    Boersma, H.H.4    Van Heerde, W.L.5    Doevendans, P.A.6
  • 49
    • 0034019978 scopus 로고    scopus 로고
    • Radionuclide imaging of acute lung transplant rejection with annexin V
    • Blankenberg, F. G., Robbins, R. C., Stoot, J. H., Vriens, P. W., Berry, G. J., Tait, J. F., et al. (2000). Radionuclide imaging of acute lung transplant rejection with annexin V. Chest, 117, 834-840.
    • (2000) Chest , vol.117 , pp. 834-840
    • Blankenberg, F.G.1    Robbins, R.C.2    Stoot, J.H.3    Vriens, P.W.4    Berry, G.J.5    Tait, J.F.6
  • 50
    • 33746094672 scopus 로고    scopus 로고
    • In vivo imaging of apoptosis in patients with acute stroke: Correlation with blood-brain barrier permeability
    • Lorberboym, M., Blankenberg, F. G., Sadeh, M., & Lampl, Y. (2006). In vivo imaging of apoptosis in patients with acute stroke: Correlation with blood-brain barrier permeability. Brain Research, 1103, 13-19.
    • (2006) Brain Research , vol.1103 , pp. 13-19
    • Lorberboym, M.1    Blankenberg, F.G.2    Sadeh, M.3    Lampl, Y.4
  • 51
    • 0036717347 scopus 로고    scopus 로고
    • Increased uptake of the apoptosis-imaging agent (99m)Tc recombinant human Annexin V in human tumors after one course of chemotherapy as a predictor of tumor response and patient prognosis
    • Belhocine, T., Steinmetz, N., Hustinx, R., Bartsch, P., Jerusalem, G., Seidel, L., et al. (2002). Increased uptake of the apoptosis-imaging agent (99m)Tc recombinant human Annexin V in human tumors after one course of chemotherapy as a predictor of tumor response and patient prognosis. Clinical Cancer Research, 8, 2766-2774.
    • (2002) Clinical Cancer Research , vol.8 , pp. 2766-2774
    • Belhocine, T.1    Steinmetz, N.2    Hustinx, R.3    Bartsch, P.4    Jerusalem, G.5    Seidel, L.6
  • 53
    • 0031298054 scopus 로고    scopus 로고
    • In vitro radiation-induced apoptosis and tumour response to radiotherapy: A prospective study in patients with non-Hodgkin lymphomas treated by low-dose irradiation
    • Dubray, B., Breton, C., Delic, J., Klijanienko, J., Maciorowski, Z., Vielh, P., et al. (1997). In vitro radiation-induced apoptosis and tumour response to radiotherapy: A prospective study in patients with non-Hodgkin lymphomas treated by low-dose irradiation. International Journal of Radiation Biology, 72, 759-760.
    • (1997) International Journal of Radiation Biology , vol.72 , pp. 759-760
    • Dubray, B.1    Breton, C.2    Delic, J.3    Klijanienko, J.4    MacIorowski, Z.5    Vielh, P.6
  • 57
    • 47949102750 scopus 로고    scopus 로고
    • Methodological aspects and applications of in vivo imaging of apoptosis in oncology: An illustrative review
    • Kartachova, M., Verheij, M., van Eck, B., Hoefnagel, K., & Valdés Olmos, R. (2005). Methodological aspects and applications of in vivo imaging of apoptosis in oncology: An illustrative review. Current Medical Imaging Review, 1, 221-228.
    • (2005) Current Medical Imaging Review , vol.1 , pp. 221-228
    • Kartachova, M.1    Verheij, M.2    Van Eck, B.3    Hoefnagel, K.4    Valdés Olmos, R.5
  • 59
    • 34249719936 scopus 로고    scopus 로고
    • The nonpeptidyl caspase binding radioligand (S)-1-(4-(2-[18F] fluoroethoxy)-benzyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin [18F]CbR) as potential positron emission tomography-compatible apoptosis imaging agent
    • Faust, A., Wagner, S., Law, M. P., Hermann, S., Schnockel, U., Keul, P., et al. (2007). The nonpeptidyl caspase binding radioligand (S)-1-(4-(2-[18F] fluoroethoxy)-benzyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin [18F]CbR) as potential positron emission tomography-compatible apoptosis imaging agent. Quarterly Journal of Nuclear Medicine and Molecular Imaging, 51, 67-73.
    • (2007) Quarterly Journal of Nuclear Medicine and Molecular Imaging , vol.51 , pp. 67-73
    • Faust, A.1    Wagner, S.2    Law, M.P.3    Hermann, S.4    Schnockel, U.5    Keul, P.6
  • 62
    • 33644606050 scopus 로고    scopus 로고
    • Detection of autophagy in tissue by standard immunohistochemistry: Possibilities and limitations
    • Martinet, W., De Meyer, G. R., Andries, L., Herman, A. G., & Kockx, M. M. (2006). Detection of autophagy in tissue by standard immunohistochemistry: Possibilities and limitations. Autophagy, 2, 55-57.
    • (2006) Autophagy , vol.2 , pp. 55-57
    • Martinet, W.1    De Meyer, G.R.2    Andries, L.3    Herman, A.G.4    Kockx, M.M.5
  • 63
    • 34548799705 scopus 로고    scopus 로고
    • Methods to detect biomarkers of cellular senescence: The senescence-associated beta-galactosidase assay
    • Itahana, K., Campisi, J., & Dimri, G. P. (2007). Methods to detect biomarkers of cellular senescence: The senescence-associated beta-galactosidase assay. Methods in Molecular Biology, 371, 21-31.
    • (2007) Methods in Molecular Biology , vol.371 , pp. 21-31
    • Itahana, K.1    Campisi, J.2    Dimri, G.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.