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Volumn 14, Issue 11, 2005, Pages 811-818

Role of Apaf-1, a key regulator of apoptosis, in melanoma progression and chemoresistance

Author keywords

Apaf 1; Apoptosis; Chemoresistance; Melanoma progression

Indexed keywords

APOPTOTIC PROTEASE ACTIVATING FACTOR 1; CASPASE 9; CYTOCHROME C; PROTEIN PRECURSOR;

EID: 27744591569     PISSN: 09066705     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1600-0625.2005.00360.x     Document Type: Review
Times cited : (53)

References (77)
  • 1
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
    • Zou H, Henzel W J, Liu X et al. Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell 1997: 90: 405-413.
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3
  • 2
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P, Nijhawan D, Budihardjo I et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 1997: 91: 479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3
  • 3
    • 0034192467 scopus 로고    scopus 로고
    • Proapoptotic apoptosis protease-activating factor 1 (Apaf-1) has a cytoplasmic localization distinct from Bcl-2 or Bcl-x (L)
    • Hausmann G, O'Reilly L A, van Driel R et al. Proapoptotic apoptosis protease-activating factor 1 (Apaf-1) has a cytoplasmic localization distinct from Bcl-2 or Bcl-x (L). J Cell Biol 2000: 149: 623-634.
    • (2000) J. Cell Biol. , vol.149 , pp. 623-634
    • Hausmann, G.1    O'Reilly, L.A.2    van Driel, R.3
  • 4
    • 0034708504 scopus 로고    scopus 로고
    • Expression and functional analysis of Apaf-1 isoforms
    • Benedict M A, Hu Y, Inohara N et al. Expression and functional analysis of Apaf-1 isoforms. J Biol Chem 2000: 275: 8461-8468.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8461-8468
    • Benedict, M.A.1    Hu, Y.2    Inohara, N.3
  • 5
    • 0035409448 scopus 로고    scopus 로고
    • Programmed cell death and apoptosis: Origins of the theory
    • Lockshin R A, Zakeri Z. Programmed cell death and apoptosis: origins of the theory. Nat Rev Mol Cell Biol 2001: 2: 545-550.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 545-550
    • Lockshin, R.A.1    Zakeri, Z.2
  • 6
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson C B. Apoptosis in the pathogenesis and treatment of disease. Science 1995: 267: 1456-1462.
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 7
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry N A, Lazebnik Y. Caspases: enemies within. Science 1998: 281: 1312-1316.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 8
    • 0032544268 scopus 로고    scopus 로고
    • Apoptotic pathways: The roads to ruin
    • Green D R. Apoptotic pathways: the roads to ruin. Cell 1998: 94: 695-698.
    • (1998) Cell , vol.94 , pp. 695-698
    • Green, D.R.1
  • 9
    • 0036187036 scopus 로고    scopus 로고
    • Three-dimensional structure of the apoptosome: Implications for assembly, procaspase-9 binding, and activation
    • Acehan D, Jiang X, Morgan D G et al. Three-dimensional structure of the apoptosome: implications for assembly, procaspase-9 binding, and activation. Mol Cell 2002: 9: 423-432.
    • (2002) Mol. Cell , vol.9 , pp. 423-432
    • Acehan, D.1    Jiang, X.2    Morgan, D.G.3
  • 10
    • 0032085941 scopus 로고    scopus 로고
    • Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization
    • Srinivasula S M, Ahmad M, Fernandes-Alnemri T et al. Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization. Mol Cell 1998: 1: 949-957.
    • (1998) Mol. Cell , vol.1 , pp. 949-957
    • Srinivasula, S.M.1    Ahmad, M.2    Fernandes-Alnemri, T.3
  • 11
    • 0032404536 scopus 로고    scopus 로고
    • The central executioners of apoptosis: Caspases or mitochondria?
    • Green D, Kroemer G. The central executioners of apoptosis: caspases or mitochondria? Trends Cell Biol 1998: 8: 267-271.
    • (1998) Trends Cell Biol. , vol.8 , pp. 267-271
    • Green, D.1    Kroemer, G.2
  • 12
    • 0032509354 scopus 로고    scopus 로고
    • WD-40 repeat region regulates Apaf-1 self association and procaspase-9 activation
    • Hu Y, Ding L, Spencer D M et al. WD-40 repeat region regulates Apaf-1 self association and procaspase-9 activation. J Biol Chem 1998: 273: 33489-33494.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33489-33494
    • Hu, Y.1    Ding, L.2    Spencer, D.M.3
  • 13
    • 0033529634 scopus 로고    scopus 로고
    • Caspase activation involves the formation of the aposome, a large (approximately 700 kDa) caspase-activating complex
    • Cain K, Brown D G, Langlais C et al. Caspase activation involves the formation of the aposome, a large (approximately 700 kDa) caspase-activating complex. J Biol Chem 1999: 274: 22686-22692.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22686-22692
    • Cain, K.1    Brown, D.G.2    Langlais, C.3
  • 14
    • 0033580926 scopus 로고    scopus 로고
    • Cytochrome c and dATP-mediated oligomerization of Apaf-1 is a prerequisite for procaspase-9 activation
    • Saleh A, Srinivasula S M, Acharya S et al. Cytochrome c and dATP-mediated oligomerization of Apaf-1 is a prerequisite for procaspase-9 activation. J Biol Chem 1999: 274: 17941-17945.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17941-17945
    • Saleh, A.1    Srinivasula, S.M.2    Acharya, S.3
  • 15
    • 0344348821 scopus 로고    scopus 로고
    • Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis
    • Hu Y, Benedict M A, Ding L et al. Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis. EMBO J 1999: 18: 3586-3595.
    • (1999) EMBO J. , vol.18 , pp. 3586-3595
    • Hu, Y.1    Benedict, M.A.2    Ding, L.3
  • 16
    • 0033573020 scopus 로고    scopus 로고
    • Caspase-9 and APAF-1 form an active holoenzyme
    • Rodriguez J, Lazebnik Y. Caspase-9 and APAF-1 form an active holoenzyme. Genes Dev 1999: 13: 3179-3184.
    • (1999) Genes Dev. , vol.13 , pp. 3179-3184
    • Rodriguez, J.1    Lazebnik, Y.2
  • 17
    • 0036204110 scopus 로고    scopus 로고
    • The regulation of APAF1 expression during development and tumourigenesis
    • Hickman E S, Helin K. The regulation of APAF1 expression during development and tumourigenesis. Apoptosis 2002: 7: 167-171.
    • (2002) Apoptosis , vol.7 , pp. 167-171
    • Hickman, E.S.1    Helin, K.2
  • 18
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo X, Budihardjo I, Zou H et al. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 1998: 94: 481-490.
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3
  • 19
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H, Zhu H, Xu C J et al. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 1998: 94: 491-501.
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, J.3
  • 20
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked
    • Yang J, Liu X, Bhalla K et al. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. Science 1997: 275: 1129-1132.
    • (1997) Science , vol.275 , pp. 1129-1132
    • Yang, J.1    Liu, X.2    Bhalla, K.3
  • 21
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck R M, Bossy-Wetzel E, Green D R et al. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science 1997: 275: 1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3
  • 22
    • 0032575688 scopus 로고    scopus 로고
    • The Bcl-2 protein family: Arbiters of cell survival
    • Adams J M, Cory S. The Bcl-2 protein family: arbiters of cell survival. Science 1998: 281: 1322-1326.
    • (1998) Science , vol.281 , pp. 1322-1326
    • Adams, J.M.1    Cory, S.2
  • 23
    • 0034640281 scopus 로고    scopus 로고
    • Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis
    • Oda E, Ohki R, Murasawa H et al. Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis. Science 2000: 288: 1053-1058.
    • (2000) Science , vol.288 , pp. 1053-1058
    • Oda, E.1    Ohki, R.2    Murasawa, H.3
  • 24
    • 0032518787 scopus 로고    scopus 로고
    • Bim: A novel member of the Bcl-2 family that promotes apoptosis
    • O'Connor L, Strasser A, O'Reilly L A et al. Bim: a novel member of the Bcl-2 family that promotes apoptosis. EMBO J 1998: 17: 384-395.
    • (1998) EMBO J. , vol.17 , pp. 384-395
    • O'Connor, L.1    Strasser, A.2    O'Reilly, L.A.3
  • 25
    • 0033607506 scopus 로고    scopus 로고
    • Proapoptotic Bcl-2 relative Bim required for certain apoptotic responses, leukocyte homeostasis, and to preclude autoimmunity
    • Bouillet P, Metcalf D, Huang D C et al. Proapoptotic Bcl-2 relative Bim required for certain apoptotic responses, leukocyte homeostasis, and to preclude autoimmunity. Science 1999: 286: 1735-17388.
    • (1999) Science , vol.286 , pp. 1735-17388
    • Bouillet, P.1    Metcalf, D.2    Huang, D.C.3
  • 28
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • Wang X. The expanding role of mitochondria in apoptosis. Genes Dev 2001: 15: 2922-2933.
    • (2001) Genes Dev. , vol.15 , pp. 2922-2933
    • Wang, X.1
  • 29
    • 0035859915 scopus 로고    scopus 로고
    • Apaf-1 deficiency and neural tube closure defects are found in fog mice
    • Honarpour N, Gilbert S L, Lahn B T et al. Apaf-1 deficiency and neural tube closure defects are found in fog mice. Proc Natl Acad Sci USA 2001: 98: 9683-9687.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9683-9687
    • Honarpour, N.1    Gilbert, S.L.2    Lahn, B.T.3
  • 31
    • 0035821652 scopus 로고    scopus 로고
    • DANN microarray analysis of genes involved in p53 mediated apoptosis: Activation of Apaf-1
    • Kannan K, Kaminski N, Rechavi G et al. DANN microarray analysis of genes involved in p53 mediated apoptosis: activation of Apaf-1. Oncogene 2001: 20: 3449-3455.
    • (2001) Oncogene , vol.20 , pp. 3449-3455
    • Kannan, K.1    Kaminski, N.2    Rechavi, G.3
  • 32
    • 0035884191 scopus 로고    scopus 로고
    • APAF-1 is a transcriptional target of p53 in DNA damage-induced apoptosis
    • Robles A I, Bemmels N A, Foraker A B et al. APAF-1 is a transcriptional target of p53 in DNA damage-induced apoptosis. Cancer Res 2001: 61: 6660-6664.
    • (2001) Cancer Res. , vol.61 , pp. 6660-6664
    • Robles, A.I.1    Bemmels, N.A.2    Foraker, A.B.3
  • 33
    • 0026849821 scopus 로고
    • Definition of a consensus binding site for p53
    • El-Deiry W S, Kern S E, Pietenpol J A et al. Definition of a consensus binding site for p53. Nat Genet 1992: 1: 45-49.
    • (1992) Nat. Genet. , vol.1 , pp. 45-49
    • El-Deiry, W.S.1    Kern, S.E.2    Pietenpol, J.A.3
  • 34
    • 18644381327 scopus 로고    scopus 로고
    • Apaf-1 is a mediator of E2F-1 induced apoptosis
    • Furukawa Y, Nishimura N, Furukawa Y et al. Apaf-1 is a mediator of E2F-1 induced apoptosis. J Biol Chem 2002: 277: 39760-39768.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39760-39768
    • Furukawa, Y.1    Nishimura, N.2    Furukawa, Y.3
  • 35
    • 0035252592 scopus 로고    scopus 로고
    • E2Fs regulate the expression of genes involved in differentiation, development, proliferation, and apoptosis
    • Muller H, Bracken A P, Vernell R et al. E2Fs regulate the expression of genes involved in differentiation, development, proliferation, and apoptosis. Genes Dev 2001: 15: 267-285.
    • (2001) Genes Dev. , vol.15 , pp. 267-285
    • Muller, H.1    Bracken, A.P.2    Vernell, R.3
  • 36
    • 0034703742 scopus 로고    scopus 로고
    • P53: Death star
    • Vousden K H. p53: death star. Cell 2000: 103: 691-694.
    • (2000) Cell , vol.103 , pp. 691-694
    • Vousden, K.H.1
  • 37
    • 0030930366 scopus 로고    scopus 로고
    • A model for p53-induced apoptosis
    • Polyak K, Xia Y, Zweier J L et al. A model for p53-induced apoptosis. Nature 1997: 389: 300-305.
    • (1997) Nature , vol.389 , pp. 300-305
    • Polyak, K.1    Xia, Y.2    Zweier, J.L.3
  • 38
    • 0034677589 scopus 로고    scopus 로고
    • Initiation of Apaf-1 translation by internal ribosome entry
    • Coldwell M J, Mitchell S A, Stoneley M et al. Initiation of Apaf-1 translation by internal ribosome entry. Oncogene 2000: 19: 899-905.
    • (2000) Oncogene , vol.19 , pp. 899-905
    • Coldwell, M.J.1    Mitchell, S.A.2    Stoneley, M.3
  • 39
    • 0035027806 scopus 로고    scopus 로고
    • Protein factor requirements of the Apaf-1 internal ribosome entry segment: Roles of polypyrimidine tract binding protein and upstream of N-ras
    • Mitchell S A, Brown E C, Coldwell M J et al. Protein factor requirements of the Apaf-1 internal ribosome entry segment: roles of polypyrimidine tract binding protein and upstream of N-ras. Mol Cell Biol 2001: 21: 3364-3374.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 3364-3374
    • Mitchell, S.A.1    Brown, E.C.2    Coldwell, M.J.3
  • 40
    • 0035839575 scopus 로고    scopus 로고
    • The adapter protein apoptotic protease-activating factor-1 (Apaf-1) is proteolytically processed during apoptosis
    • Lauber K, Appel H A, Schlosser S F et al. The adapter protein apoptotic protease-activating factor-1 (Apaf-1) is proteolytically processed during apoptosis. J Biol Chem 2001: 276: 29772-29781.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29772-29781
    • Lauber, K.1    Appel, H.A.2    Schlosser, S.F.3
  • 41
    • 0035881074 scopus 로고    scopus 로고
    • Final version of the American Joint Committee on Cancer staging system for cutaneous melanoma
    • Balch C M, Buzaid A C, Soong S J et al. Final version of the American Joint Committee on Cancer staging system for cutaneous melanoma. J Clin Oncol 2001: 19: 3635-3648.
    • (2001) J. Clin. Oncol. , vol.19 , pp. 3635-3648
    • Balch, C.M.1    Buzaid, A.C.2    Soong, S.J.3
  • 44
    • 0038793948 scopus 로고    scopus 로고
    • Apoptosis and melanoma chemoresistance
    • Soengas M S, Lowe S W. Apoptosis and melanoma chemoresistance. Oncogene 2003: 22: 3138-3151.
    • (2003) Oncogene , vol.22 , pp. 3138-3151
    • Soengas, M.S.1    Lowe, S.W.2
  • 45
    • 0032962588 scopus 로고    scopus 로고
    • Apoptosis and therapy
    • Schmitt C A, Lowe S W. Apoptosis and therapy. J Pathol 1999: 187: 127-137.
    • (1999) J. Pathol. , vol.187 , pp. 127-137
    • Schmitt, C.A.1    Lowe, S.W.2
  • 47
    • 20944435524 scopus 로고    scopus 로고
    • Ferritin contributes to melanoma progression by modulating cell growth and sensitivity to oxidative stress
    • Baldi A, Lombardi D, Russo P et al. Ferritin contributes to melanoma progression by modulating cell growth and sensitivity to oxidative stress. Clin Cancer Res 2005: 11: 3175-3183.
    • (2005) Clin. Cancer Res. , vol.11 , pp. 3175-3183
    • Baldi, A.1    Lombardi, D.2    Russo, P.3
  • 48
    • 0038460957 scopus 로고    scopus 로고
    • cDNA array technology in melanoma: An overview
    • Baldi A, Santini D, De Luca A et al. cDNA array technology in melanoma: an overview. J Cell Physiol 2003: 196: 219-223.
    • (2003) J. Cell Physiol. , vol.196 , pp. 219-223
    • Baldi, A.1    Santini, D.2    De Luca, A.3
  • 49
    • 0029852580 scopus 로고    scopus 로고
    • Use of cDNA microarray to analyze gene expression patterns in human cancer
    • DeRisi J, Penland L, Brown P O et al. Use of cDNA microarray to analyze gene expression patterns in human cancer. Nat Genet 1996: 14: 457-460.
    • (1996) Nat. Genet. , vol.14 , pp. 457-460
    • DeRisi, J.1    Penland, L.2    Brown, P.O.3
  • 50
    • 0034601487 scopus 로고    scopus 로고
    • Genomic analysis of metastasis reveals an essential role for RhoC
    • Clark E A, Golub T R, Landser E S, Hynes R O. Genomic analysis of metastasis reveals an essential role for RhoC. Nature 2000: 406: 532-535.
    • (2000) Nature , vol.406 , pp. 532-535
    • Clark, E.A.1    Golub, T.R.2    Landser, E.S.3    Hynes, R.O.4
  • 51
    • 0034601455 scopus 로고    scopus 로고
    • Molecular classification of cutaneous malignant melanoma by gene expression profilings
    • Bittner M, Meltzer P, Chen Y et al. Molecular classification of cutaneous malignant melanoma by gene expression profilings. Nature 2000: 406: 536-540.
    • (2000) Nature , vol.406 , pp. 536-540
    • Bittner, M.1    Meltzer, P.2    Chen, Y.3
  • 52
    • 0028596185 scopus 로고
    • Sunburn and p53 in the onset of skin cancer
    • Ziegler A, Jonason A S, Leffell D J et al. Sunburn and p53 in the onset of skin cancer. Nature 1994: 372: 773-776.
    • (1994) Nature , vol.372 , pp. 773-776
    • Ziegler, A.1    Jonason, A.S.2    Leffell, D.J.3
  • 53
    • 0033614447 scopus 로고    scopus 로고
    • The pathogenesis of melanoma induced by ultraviolet radiation
    • Gilchrest B A, Eller M S, Geller A C et al. The pathogenesis of melanoma induced by ultraviolet radiation. N Engl J Med 1999: 340: 1341-1348.
    • (1999) N. Engl. J. Med. , vol.340 , pp. 1341-1348
    • Gilchrest, B.A.1    Eller, M.S.2    Geller, A.C.3
  • 54
    • 19644365303 scopus 로고    scopus 로고
    • Nonlesional vitiliginous melanocytes are not characterized by an increased proneness to nitric oxide-induced apoptosis
    • Ivanova K, van den Wijngaard R, Gerzer R et al. Nonlesional vitiliginous melanocytes are not characterized by an increased proneness to nitric oxide-induced apoptosis. Exp Dermatol 2005: 14: 445-453.
    • (2005) Exp. Dermatol. , vol.14 , pp. 445-453
    • Ivanova, K.1    van den Wijngaard, R.2    Gerzer, R.3
  • 55
    • 0037372013 scopus 로고    scopus 로고
    • Apoptosis and melanoma: Molecular mechanisms
    • Hussein R M, Haemel A K, Wood G S. Apoptosis and melanoma: molecular mechanisms. J Pathol 2003: 1299: 275-288.
    • (2003) J. Pathol. , vol.1299 , pp. 275-288
    • Hussein, R.M.1    Haemel, A.K.2    Wood, G.S.3
  • 56
    • 0037244772 scopus 로고    scopus 로고
    • Apoptosis regulators and responses in human melanocytic and keratinocytic cells
    • Bowen A R, Hanks A N, Allen S M et al. Apoptosis regulators and responses in human melanocytic and keratinocytic cells. J Invest Dermatol 2003: 120: 48-55.
    • (2003) J. Invest. Dermatol. , vol.120 , pp. 48-55
    • Bowen, A.R.1    Hanks, A.N.2    Allen, S.M.3
  • 57
    • 0032517341 scopus 로고    scopus 로고
    • The p16INK4a/CDKN2A tumor suppressor and its relatives
    • Ruas M, Peters G. The p16INK4a/CDKN2A tumor suppressor and its relatives. Biochim Biophys Acta 1998: 1378: F115-17177.
    • (1998) Biochim. Biophys. Acta , vol.1378
    • Ruas, M.1    Peters, G.2
  • 59
    • 0038457477 scopus 로고    scopus 로고
    • Hunam melanocyte senescence and melanoma susceptibility genes
    • Bennet D C. Hunam melanocyte senescence and melanoma susceptibility genes. Oncogene 2003: 22: 3063-3069.
    • (2003) Oncogene , vol.22 , pp. 3063-3069
    • Bennet, D.C.1
  • 60
    • 22344444821 scopus 로고    scopus 로고
    • Apoptosis of lymphocytes in peripheral blood of patients with melanoma
    • Tas F, Duranyildiz D, Argon A et al. Apoptosis of lymphocytes in peripheral blood of patients with melanoma. Med Oncol 2005: 22: 177-182.
    • (2005) Med. Oncol. , vol.22 , pp. 177-182
    • Tas, F.1    Duranyildiz, D.2    Argon, A.3
  • 61
    • 0032506524 scopus 로고    scopus 로고
    • Control of apoptosis and mitotic spindle checkpoint by survivin
    • Li F, Ambrosini G, Chu E Y et al. Control of apoptosis and mitotic spindle checkpoint by survivin. Nature 1998: 396: 580-584.
    • (1998) Nature , vol.396 , pp. 580-584
    • Li, F.1    Ambrosini, G.2    Chu, E.Y.3
  • 62
    • 0028348001 scopus 로고
    • Mutation and expression of the p53 gene in human malignant melanoma
    • Albino A P, Vidal M J, McNutt N S et al. Mutation and expression of the p53 gene in human malignant melanoma. Melanoma Res 1994: 4: 35-45.
    • (1994) Melanoma. Res. , vol.4 , pp. 35-45
    • Albino, A.P.1    Vidal, M.J.2    McNutt, N.S.3
  • 63
    • 0028197011 scopus 로고
    • Analysis of p53 in human cutaneous melanoma cell lines
    • Montano X, Shamsher M, Whitehead P et al. Analysis of p53 in human cutaneous melanoma cell lines. Oncogene 1994: 9: 1455-1459.
    • (1994) Oncogene , vol.9 , pp. 1455-1459
    • Montano, X.1    Shamsher, M.2    Whitehead, P.3
  • 64
    • 0036753482 scopus 로고    scopus 로고
    • Mutations in the TP53 gene in human malignant melanomas derived from sun-exposed skin and unexposed mucosal membranes
    • Ragnarsson-Olding B K, Karsberg S, Platz A et al. Mutations in the TP53 gene in human malignant melanomas derived from sun-exposed skin and unexposed mucosal membranes. Melanoma Res 2002: 12: 453-463.
    • (2002) Melanoma Res. , vol.12 , pp. 453-463
    • Ragnarsson-Olding, B.K.1    Karsberg, S.2    Platz, A.3
  • 65
    • 0033515883 scopus 로고    scopus 로고
    • Apaf-1 and caspase-9 in p53-dependent apoptosis and tumor inhibition
    • Soengas M S, Alarcon R M, Yoshida H et al. Apaf-1 and caspase-9 in p53-dependent apoptosis and tumor inhibition. Science 1999: 284: 156-159.
    • (1999) Science , vol.284 , pp. 156-159
    • Soengas, M.S.1    Alarcon, R.M.2    Yoshida, H.3
  • 66
    • 0035821652 scopus 로고    scopus 로고
    • DNA microarray analysis of genes involved in p53 mediated apoptosis: Activation of Apaf-1
    • Kannan K, Kaminski N, Rechavi G et al. DNA microarray analysis of genes involved in p53 mediated apoptosis: activation of Apaf-1. Oncogene 2001: 20: 3449-3455.
    • (2001) Oncogene , vol.20 , pp. 3449-3455
    • Kannan, K.1    Kaminski, N.2    Rechavi, G.3
  • 67
    • 0035843169 scopus 로고    scopus 로고
    • Inactivation of the apoptosis effector Apaf-1 in malignant melanoma
    • Soengas M S, Capodieci P, Polsky D et al. Inactivation of the apoptosis effector Apaf-1 in malignant melanoma. Nature 2001: 409: 207-211.
    • (2001) Nature , vol.409 , pp. 207-211
    • Soengas, M.S.1    Capodieci, P.2    Polsky, D.3
  • 68
    • 0033601073 scopus 로고    scopus 로고
    • Methylation-induced repression - Belts, braces, and chromatin
    • Bird A P, Wolffe A P. Methylation-induced repression - belts, braces, and chromatin. Cell 1999: 99: 451-454.
    • (1999) Cell , vol.99 , pp. 451-454
    • Bird, A.P.1    Wolffe, A.P.2
  • 69
    • 10744220426 scopus 로고    scopus 로고
    • Analysis of APAF-1 expression in human cutaneous melanoma progression
    • Baldi A, Santini D, Russo P et al. Analysis of APAF-1 expression in human cutaneous melanoma progression. Exp Dermatol 2004: 13: 93-97.
    • (2004) Exp. Dermatol. , vol.13 , pp. 93-97
    • Baldi, A.1    Santini, D.2    Russo, P.3
  • 70
    • 5644293078 scopus 로고    scopus 로고
    • Apoptosis protease activator protein-1 expression is dispensable for response of human melanoma cells to distinct proapoptotic agents
    • Zanon M, Piris A, Bersani I et al. Apoptosis protease activator protein-1 expression is dispensable for response of human melanoma cells to distinct proapoptotic agents. Cancer Res 2004: 64: 7386-7394.
    • (2004) Cancer Res. , vol.64 , pp. 7386-7394
    • Zanon, M.1    Piris, A.2    Bersani, I.3
  • 71
    • 0345830385 scopus 로고    scopus 로고
    • Role of caspases-3 and - 7 in Apaf-1 proteolytic cleavage and degradation events during cisplatin-induced apoptosis in melanoma cells
    • Del Bello B, Valentini M A, Mangiavacchi P et al. Role of caspases-3 and - 7 in Apaf-1 proteolytic cleavage and degradation events during cisplatin-induced apoptosis in melanoma cells. Exp Cell Res 2004: 293: 302-310.
    • (2004) Exp. Cell Res. , vol.293 , pp. 302-310
    • Del Bello, B.1    Valentini, M.A.2    Mangiavacchi, P.3
  • 72
    • 5044237664 scopus 로고    scopus 로고
    • Reduced Apaf-1 expression in human cutaneous melanomas
    • Dai D L, Martinka M, Bush J A et al. Reduced Apaf-1 expression in human cutaneous melanomas. Br J Cancer 2004: 91: 1089-1095.
    • (2004) Br. J. Cancer , vol.91 , pp. 1089-1095
    • Dai, D.L.1    Martinka, M.2    Bush, J.A.3
  • 73
    • 1542510618 scopus 로고    scopus 로고
    • Allelic imbalance of 12q22-23 associated with APAF-1 locus correlates with poor disease outcome in cutaneous melanoma
    • Fujimoto A, Takeuchi H, Taback B et al. Allelic imbalance of 12q22-23 associated with APAF-1 locus correlates with poor disease outcome in cutaneous melanoma. Cancer Res 2004: 64: 2245-2250.
    • (2004) Cancer Res. , vol.64 , pp. 2245-2250
    • Fujimoto, A.1    Takeuchi, H.2    Taback, B.3
  • 74
    • 12844255773 scopus 로고    scopus 로고
    • Decreased expression of Apaf-1 with progression of melanoma
    • Mustika R, Budiyanto A, Nishigori C et al. Decreased expression of Apaf-1 with progression of melanoma. Pigment Cell Res 2005: 18: 59-62.
    • (2005) Pigment Cell Res. , vol.18 , pp. 59-62
    • Mustika, R.1    Budiyanto, A.2    Nishigori, C.3
  • 75
    • 0031763526 scopus 로고    scopus 로고
    • Downregulation of transcription factor AP-2 predicts poor survival in stage I cutaneous malignant melanoma
    • Karjalainen J M, Kellokoski J K, Eskelinen M J et al. Downregulation of transcription factor AP-2 predicts poor survival in stage I cutaneous malignant melanoma. J Clin Oncol 1998: 16: 3584-3591.
    • (1998) J. Clin. Oncol. , vol.16 , pp. 3584-3591
    • Karjalainen, J.M.1    Kellokoski, J.K.2    Eskelinen, M.J.3
  • 76
    • 0034759481 scopus 로고    scopus 로고
    • Expression of AP-2 transcription factor and of its downstream target genes c-kit, E-cadherin and p-21 in human cutaneous melanoma
    • Baldi A, Santini D, Battista T et al. Expression of AP-2 transcription factor and of its downstream target genes c-kit, E-cadherin and p-21 in human cutaneous melanoma. J Cell Biochem 2001: 83: 364-372.
    • (2001) J. Cell Biochem. , vol.83 , pp. 364-372
    • Baldi, A.1    Santini, D.2    Battista, T.3
  • 77
    • 18944390491 scopus 로고    scopus 로고
    • Regulators of apoptosis: Suitable targets for immune therapy of cancer
    • Andersen Mh, Becker J C, Straten P. Regulators of apoptosis: suitable targets for immune therapy of cancer. Nat Rev Drug Discov 2005: 4: 399-409.
    • (2005) Nat. Rev. Drug Discov. , vol.4 , pp. 399-409
    • Andersen, Mh.1    Becker, J.C.2    Straten, P.3


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