메뉴 건너뛰기




Volumn 109, Issue 9, 2007, Pages 4045-4054

Iron chelation regulates cyclin D1 expression via the proteasome: A link to iron deficiency-mediated growth suppression

Author keywords

[No Author keywords available]

Indexed keywords

2 HYDROXY 1 NAPHTHYLALDEHYDE ISONICOTINOYL HYDRAZONE; CYCLIN D1; DEFEROXAMINE; GLYCOGEN SYNTHASE KINASE 3BETA; HYDRAZONE DERIVATIVE; PROTEASOME; PROTEASOME INHIBITOR; UBIQUITIN; UNCLASSIFIED DRUG; VON HIPPEL LINDAU PROTEIN;

EID: 34247373460     PISSN: 00064971     EISSN: 00064971     Source Type: Journal    
DOI: 10.1182/blood-2006-10-047753     Document Type: Article
Times cited : (133)

References (71)
  • 1
    • 0028586693 scopus 로고
    • Control of disease by selective iron depletion: A novel therapeutic strategy utilizing iron chelators
    • Hershko C. Control of disease by selective iron depletion: a novel therapeutic strategy utilizing iron chelators. Baillieres Clin Haematol. 1994;7:965-1000.
    • (1994) Baillieres Clin Haematol , vol.7 , pp. 965-1000
    • Hershko, C.1
  • 2
    • 0038324398 scopus 로고    scopus 로고
    • The role of iron chelation in cancer therapy
    • Buss JL, Torti FM, Torti SV. The role of iron chelation in cancer therapy. Curr Med Chem. 2003;10:1021-1034.
    • (2003) Curr Med Chem , vol.10 , pp. 1021-1034
    • Buss, J.L.1    Torti, F.M.2    Torti, S.V.3
  • 3
    • 29844457587 scopus 로고    scopus 로고
    • The evolution of iron chelators for the treatment of iron overload disease and cancer
    • Kalinowski DS, Richardson DR. The evolution of iron chelators for the treatment of iron overload disease and cancer. Pharmacol Rev. 2005;57:547-583.
    • (2005) Pharmacol Rev , vol.57 , pp. 547-583
    • Kalinowski, D.S.1    Richardson, D.R.2
  • 4
    • 0033599057 scopus 로고    scopus 로고
    • Disorders of iron metabolism
    • Andrews NC. Disorders of iron metabolism. New England J Med 1999;341:1986-1995.
    • (1999) New England J Med , vol.341 , pp. 1986-1995
    • Andrews, N.C.1
  • 5
    • 0018337084 scopus 로고
    • The reduction of ribonucleotides
    • Thelander L, Reichard, P. The reduction of ribonucleotides. Annu Rev Biochem. 1979;48:133-158.
    • (1979) Annu Rev Biochem , vol.48 , pp. 133-158
    • Thelander, L.1    Reichard, P.2
  • 6
    • 0035181433 scopus 로고    scopus 로고
    • Ribonucleotide reductase as a preferential target for the inhibition of leukemic cell growth by 311, a novel iron chelator of the pyridoxal isonicotinoyl hydrazone class
    • Green DA, Antholine WE, Wong SJ, Richardson DR, Chitambar CR. Ribonucleotide reductase as a preferential target for the inhibition of leukemic cell growth by 311, a novel iron chelator of the pyridoxal isonicotinoyl hydrazone class. Clin Cancer Res 2001;7:3574-3579.
    • (2001) Clin Cancer Res , vol.7 , pp. 3574-3579
    • Green, D.A.1    Antholine, W.E.2    Wong, S.J.3    Richardson, D.R.4    Chitambar, C.R.5
  • 7
    • 0037009846 scopus 로고    scopus 로고
    • The role of iron in cell cycle progression and the proliferation of neoplastic cells
    • Le NTV, Richardson, DR. The role of iron in cell cycle progression and the proliferation of neoplastic cells. Biochim Biophys Acta. 2002;1603:31-46.
    • (2002) Biochim Biophys Acta , vol.1603 , pp. 31-46
    • Le, N.T.V.1    Richardson, D.R.2
  • 8
    • 0028171292 scopus 로고
    • G1 phase progression: Cycling on cue
    • Sherr CJ. G1 phase progression: cycling on cue. Cell. 1994;79:551-555.
    • (1994) Cell , vol.79 , pp. 551-555
    • Sherr, C.J.1
  • 9
    • 0030601987 scopus 로고    scopus 로고
    • Iron deprivation inhibits cyclin-dependent kinase activity and decreases cyclin D/CDK4 protein levels in asynchronous MDA-MB-453 human breast cancer cells
    • Kulp KS, Green SL, Vulliet PR. Iron deprivation inhibits cyclin-dependent kinase activity and decreases cyclin D/CDK4 protein levels in asynchronous MDA-MB-453 human breast cancer cells. Exp Cell Res. 1996;229:60-68.
    • (1996) Exp Cell Res , vol.229 , pp. 60-68
    • Kulp, K.S.1    Green, S.L.2    Vulliet, P.R.3
  • 10
    • 0035437183 scopus 로고    scopus 로고
    • Gao J, Richardson DR. The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective anti-proliferative agents, IV: the mechanisms involved in inhibiting cell-cycle progression. Blood. 2001;98:842-850.
    • Gao J, Richardson DR. The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective anti-proliferative agents, IV: the mechanisms involved in inhibiting cell-cycle progression. Blood. 2001;98:842-850.
  • 11
    • 0031895560 scopus 로고    scopus 로고
    • Cyclin D1 and human neoplasia
    • Donnellan R, Chetty, R. Cyclin D1 and human neoplasia. Mol Pathol. 1998;51:1-7.
    • (1998) Mol Pathol , vol.51 , pp. 1-7
    • Donnellan, R.1    Chetty, R.2
  • 12
    • 33746524819 scopus 로고    scopus 로고
    • Gain of 11q/cyclin D1 overexpression is an essential early step in skin cancer development and causes abnormal tissue organization and differentiation
    • Burnworth B, Popp S, Stark HJ, et al. Gain of 11q/cyclin D1 overexpression is an essential early step in skin cancer development and causes abnormal tissue organization and differentiation. Oncogene. 2006;25:4399-4412.
    • (2006) Oncogene , vol.25 , pp. 4399-4412
    • Burnworth, B.1    Popp, S.2    Stark, H.J.3
  • 13
    • 0030101829 scopus 로고    scopus 로고
    • Inhibition of lung cancer proliferation by antisense cyclin D
    • Schrump DS, Chen A, Consoli U. Inhibition of lung cancer proliferation by antisense cyclin D. Cancer Gene Ther. 1996;3:131-135.
    • (1996) Cancer Gene Ther , vol.3 , pp. 131-135
    • Schrump, D.S.1    Chen, A.2    Consoli, U.3
  • 14
    • 0032533225 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3β regulates cyclin D1 proteolysis and subcellular localization
    • Diehl JA, Cheng M, Roussenl MF, Sherr CJ. Glycogen synthase kinase-3β regulates cyclin D1 proteolysis and subcellular localization. Genes Dev. 1998;12:3499-3511.
    • (1998) Genes Dev , vol.12 , pp. 3499-3511
    • Diehl, J.A.1    Cheng, M.2    Roussenl, M.F.3    Sherr, C.J.4
  • 15
    • 0034595423 scopus 로고    scopus 로고
    • Cell cycle-dependent variations in c-Jun and JunB phosphorylation: A role in the control of cyclin D1 expression
    • Bakiri L, Lallemand D, Bossy-Wetzel E, Yaniv M. Cell cycle-dependent variations in c-Jun and JunB phosphorylation: a role in the control of cyclin D1 expression. EMBO J. 2000;19:2056-2068.
    • (2000) EMBO J , vol.19 , pp. 2056-2068
    • Bakiri, L.1    Lallemand, D.2    Bossy-Wetzel, E.3    Yaniv, M.4
  • 16
    • 0030916209 scopus 로고    scopus 로고
    • Inhibition of cyclin D1 phosphorylation on threonine-286 prevents its rapid degradation by the ubiquitin-proteasome pathway
    • Diehl JA, Zindy F, Sherr CJ. Inhibition of cyclin D1 phosphorylation on threonine-286 prevents its rapid degradation by the ubiquitin-proteasome pathway. Genes Dev. 1997;11:957-972.
    • (1997) Genes Dev , vol.11 , pp. 957-972
    • Diehl, J.A.1    Zindy, F.2    Sherr, C.J.3
  • 17
    • 0037213921 scopus 로고    scopus 로고
    • Ubiquitin-dependent proteolysis of cyclin D1 is associated with coxsackievirus-induced cell growth arrest
    • Luo H, Zhang J, Dastvan F, et al. Ubiquitin-dependent proteolysis of cyclin D1 is associated with coxsackievirus-induced cell growth arrest. J Virol. 2003;77:1-9.
    • (2003) J Virol , vol.77 , pp. 1-9
    • Luo, H.1    Zhang, J.2    Dastvan, F.3
  • 18
  • 19
    • 0029166967 scopus 로고
    • Eukaryotic translation initiation factor 4E regulates expression of cyclin D1 at transcriptional and post-transcriptional levels
    • Rosenwald IB, Kaspar R, Rousseau D, et al. Eukaryotic translation initiation factor 4E regulates expression of cyclin D1 at transcriptional and post-transcriptional levels. J Biol Chem. 1995;270:21176-21180.
    • (1995) J Biol Chem , vol.270 , pp. 21176-21180
    • Rosenwald, I.B.1    Kaspar, R.2    Rousseau, D.3
  • 20
    • 0030691026 scopus 로고    scopus 로고
    • Post-translational regulation of cyclin D1 by retinoic acid: A chemoprevention mechanism
    • Langenfeld J, Kiyokawa H, Sekula D, Boyle J, Dmitrovsky E. Post-translational regulation of cyclin D1 by retinoic acid: a chemoprevention mechanism. Proc Natl Acad Sci U S A. 1997;94:12070-12074.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 12070-12074
    • Langenfeld, J.1    Kiyokawa, H.2    Sekula, D.3    Boyle, J.4    Dmitrovsky, E.5
  • 21
    • 4744339875 scopus 로고    scopus 로고
    • Antizyme targets cyclin D1 for degradation
    • Newman R, Mobascher A, Mangold U, et al. Antizyme targets cyclin D1 for degradation. J Biol Chem. 2004;279:41504-41511.
    • (2004) J Biol Chem , vol.279 , pp. 41504-41511
    • Newman, R.1    Mobascher, A.2    Mangold, U.3
  • 23
    • 0036645091 scopus 로고    scopus 로고
    • Identification of cyclin D1 and other novel targets for the von Hippel-Lindau tumor suppressor gene by expression of array analysis and investigation of cyclin D1 genotype as a modifier in von Hippel-Lindau disease
    • Zatyka M, da Silva NF, Clifford SC, et al. Identification of cyclin D1 and other novel targets for the von Hippel-Lindau tumor suppressor gene by expression of array analysis and investigation of cyclin D1 genotype as a modifier in von Hippel-Lindau disease. Cancer Res. 2002;62:3803-38011.
    • (2002) Cancer Res , vol.62 , pp. 3803-38011
    • Zatyka, M.1    da Silva, N.F.2    Clifford, S.C.3
  • 24
    • 0037617447 scopus 로고    scopus 로고
    • Loss of von Hippel-Lindau protein causes cell density dependent deregulation of cyclin D1 expression through hypoxia-inducible factor
    • Baba M, Hirai S, Yamada-Okabe H, et al. Loss of von Hippel-Lindau protein causes cell density dependent deregulation of cyclin D1 expression through hypoxia-inducible factor. Oncogene. 2003;22:2728-2738.
    • (2003) Oncogene , vol.22 , pp. 2728-2738
    • Baba, M.1    Hirai, S.2    Yamada-Okabe, H.3
  • 25
    • 0022425793 scopus 로고
    • Role of antizyme in degradation of ornithine decarboxylase in HTC cells
    • Murakami Y, Hayashi S. Role of antizyme in degradation of ornithine decarboxylase in HTC cells. Biochem J. 1985;226:893-896.
    • (1985) Biochem J , vol.226 , pp. 893-896
    • Murakami, Y.1    Hayashi, S.2
  • 26
    • 0026714435 scopus 로고
    • Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination
    • Murakami Y, Matsufuji S, Kameji T, et al. Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination. Nature. 1992;360:597-599.
    • (1992) Nature , vol.360 , pp. 597-599
    • Murakami, Y.1    Matsufuji, S.2    Kameji, T.3
  • 27
    • 17244378011 scopus 로고    scopus 로고
    • Inhibition of NAD(P)H:quinone oxidoreductase 1 activity and induction of p53 degradation by the natural phenolic compound curcumin
    • Tsvetkov P, Asher G, Reiss V, Shaul Y, Sachs L, Lotem J. Inhibition of NAD(P)H:quinone oxidoreductase 1 activity and induction of p53 degradation by the natural phenolic compound curcumin. Proc Natl Acad Sci U S A. 2005;102:5535-5540.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 5535-5540
    • Tsvetkov, P.1    Asher, G.2    Reiss, V.3    Shaul, Y.4    Sachs, L.5    Lotem, J.6
  • 28
    • 14644446056 scopus 로고    scopus 로고
    • 20S proteasomal degradation of ornithine decarboxylase is regulated by NQO1
    • Asher G, Bercovich Z, Tsvetkov P, Shaul Y, Kahana C. 20S proteasomal degradation of ornithine decarboxylase is regulated by NQO1. Mol Cell. 2005;17:645-655.
    • (2005) Mol Cell , vol.17 , pp. 645-655
    • Asher, G.1    Bercovich, Z.2    Tsvetkov, P.3    Shaul, Y.4    Kahana, C.5
  • 29
    • 0032771646 scopus 로고    scopus 로고
    • Crystal and molecular structure of 2-hydroxy-1-naphthaldehyde isonicotinoyl hydrazone (NIH) and its iron(III) complex: An iron chelator with anti-tumour activity
    • Richardson DR, Bernhardt PV. Crystal and molecular structure of 2-hydroxy-1-naphthaldehyde isonicotinoyl hydrazone (NIH) and its iron(III) complex: an iron chelator with anti-tumour activity. J Biol Inorg Chem. 1999;4:266-273.
    • (1999) J Biol Inorg Chem , vol.4 , pp. 266-273
    • Richardson, D.R.1    Bernhardt, P.V.2
  • 30
    • 0028205667 scopus 로고
    • Accumulation of p53 in a mutant cell line defective in the ubiquitin pathway
    • Chowdary DR, Dermody JJ, Jha KK, Ozer HL. Accumulation of p53 in a mutant cell line defective in the ubiquitin pathway. Mol Cell Biol. 1994;14:1997-2003.
    • (1994) Mol Cell Biol , vol.14 , pp. 1997-2003
    • Chowdary, D.R.1    Dermody, J.J.2    Jha, K.K.3    Ozer, H.L.4
  • 31
    • 7244239197 scopus 로고    scopus 로고
    • Iron chelators with high anti-proliferative activity up-regulate the expression of a growth inhibitory and metastasis supressor gene: A novel link between iron metabolism and proliferation
    • Le NTV, Richardson, DR. Iron chelators with high anti-proliferative activity up-regulate the expression of a growth inhibitory and metastasis supressor gene: a novel link between iron metabolism and proliferation. Blood. 2004;104:2967-2975.
    • (2004) Blood , vol.104 , pp. 2967-2975
    • Le, N.T.V.1    Richardson, D.R.2
  • 32
    • 33749515083 scopus 로고    scopus 로고
    • A class of iron chelators with a wide spectrum of potent anti-tumor activity: Agents that overcome resistance to chemotherapeutics
    • Whitnall M, Howard J, Ponka P, Richardson DR. A class of iron chelators with a wide spectrum of potent anti-tumor activity: agents that overcome resistance to chemotherapeutics. Proc Natl Acad Sci U S A. 2006;103:14901-14906.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 14901-14906
    • Whitnall, M.1    Howard, J.2    Ponka, P.3    Richardson, D.R.4
  • 33
    • 15744368845 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor g-independent ablation of cyclin D1 by thiazolidinediones and their derivatives in breast cancer cells
    • Huang JW, Shiau CW, Yang YT, et al. Peroxisome proliferator-activated receptor g-independent ablation of cyclin D1 by thiazolidinediones and their derivatives in breast cancer cells. Mol Pharmacol. 2005;67:1342-1348.
    • (2005) Mol Pharmacol , vol.67 , pp. 1342-1348
    • Huang, J.W.1    Shiau, C.W.2    Yang, Y.T.3
  • 34
    • 0030894798 scopus 로고    scopus 로고
    • Richardson DR, Milnes, K. The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective antiproliferative agents, II: the mechanism of action of ligands derived from salicylaldehyde benzoyl hydrazone and 2-hydroxy-1-naphthylaldehyde benzoyl hydrazone. Blood. 1997;89:3025-3038.
    • Richardson DR, Milnes, K. The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective antiproliferative agents, II: the mechanism of action of ligands derived from salicylaldehyde benzoyl hydrazone and 2-hydroxy-1-naphthylaldehyde benzoyl hydrazone. Blood. 1997;89:3025-3038.
  • 35
    • 0033566305 scopus 로고    scopus 로고
    • The potential of analogues of the pyridoxal isonicotinoyl hydrazone class as effective anti-proliferative agents, III: The effect of the ligands on molecular targets involved in proliferation
    • Darnell G, Richardson DR. The potential of analogues of the pyridoxal isonicotinoyl hydrazone class as effective anti-proliferative agents, III: the effect of the ligands on molecular targets involved in proliferation. Blood. 1999;94:781-792.
    • (1999) Blood , vol.94 , pp. 781-792
    • Darnell, G.1    Richardson, D.R.2
  • 36
    • 0028891974 scopus 로고
    • The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective anti-proliferative agents
    • Richardson DR, Tran EH, Ponka P. The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective anti-proliferative agents. Blood. 1995;86:4295-4306.
    • (1995) Blood , vol.86 , pp. 4295-4306
    • Richardson, D.R.1    Tran, E.H.2    Ponka, P.3
  • 37
    • 0142154312 scopus 로고    scopus 로고
    • The effect of potent iron chelators on the regulation of p53: Examination of the expression, localization and DNA-binding activity of p53 and the transactivation of WAF1
    • Liang S, Richardson DR. The effect of potent iron chelators on the regulation of p53: examination of the expression, localization and DNA-binding activity of p53 and the transactivation of WAF1. Carcinogenesis. 2003;24:1601-1614.
    • (2003) Carcinogenesis , vol.24 , pp. 1601-1614
    • Liang, S.1    Richardson, D.R.2
  • 38
    • 0037100453 scopus 로고    scopus 로고
    • Novel "hybrid" iron chelators derived from aroylhydrazones and thiosemicarbazones demonstrate high anti-proliferative activity that is selective for tumor cells
    • Lovejoy DB, Richardson DR. Novel "hybrid" iron chelators derived from aroylhydrazones and thiosemicarbazones demonstrate high anti-proliferative activity that is selective for tumor cells. Blood. 2002;100:666-676.
    • (2002) Blood , vol.100 , pp. 666-676
    • Lovejoy, D.B.1    Richardson, D.R.2
  • 39
    • 0038687772 scopus 로고    scopus 로고
    • Potent iron chelators increase the mRNA levels of the universal cyclin-dependent kinase inhibitor, p21WAF1/CIP1, but paradoxically inhibits translation: A potential mechanism of cell cycle dysregulation
    • Le NTV, Richardson DR. Potent iron chelators increase the mRNA levels of the universal cyclin-dependent kinase inhibitor, p21WAF1/CIP1, but paradoxically inhibits translation: a potential mechanism of cell cycle dysregulation. Carcinogenesis. 2003;24:1045-1058.
    • (2003) Carcinogenesis , vol.24 , pp. 1045-1058
    • Le, N.T.V.1    Richardson, D.R.2
  • 40
    • 0034003005 scopus 로고    scopus 로고
    • Stress signals utilize multiple pathways to stabilize p53
    • Ashcroft M, Taya Y, Vousden KH. Stress signals utilize multiple pathways to stabilize p53. Mol Cell Biol. 2000;20:3224-3233.
    • (2000) Mol Cell Biol , vol.20 , pp. 3224-3233
    • Ashcroft, M.1    Taya, Y.2    Vousden, K.H.3
  • 41
    • 0035149526 scopus 로고    scopus 로고
    • Synergistic enhancement of apoptosis by DNAand cytoskeleton-damaging agents: A basis for combination chemotherapy of cancer
    • Shang X, Shiono Y, Fujita Y, Oka S, Yamazaki Y. Synergistic enhancement of apoptosis by DNAand cytoskeleton-damaging agents: a basis for combination chemotherapy of cancer. Anticancer Res. 2001;21:2585-2589.
    • (2001) Anticancer Res , vol.21 , pp. 2585-2589
    • Shang, X.1    Shiono, Y.2    Fujita, Y.3    Oka, S.4    Yamazaki, Y.5
  • 42
    • 0027521831 scopus 로고
    • Role of ribonucleotide reductase in inhibition of mammalian cell growth by potent iron chelators
    • Nyholm S, Mann GJ, Johansson AG, Bergeron RJ, Graslund A, Thelander L. Role of ribonucleotide reductase in inhibition of mammalian cell growth by potent iron chelators. J Biol Chem. 1993;268:26200-26205.
    • (1993) J Biol Chem , vol.268 , pp. 26200-26205
    • Nyholm, S.1    Mann, G.J.2    Johansson, A.G.3    Bergeron, R.J.4    Graslund, A.5    Thelander, L.6
  • 43
    • 0029833706 scopus 로고    scopus 로고
    • The relationship of intracellular iron chelation to the inhibition and regeneration of human ribonucleotide reductase
    • Cooper CE, Lynagh GR, Hoyes KP, Hider RC, Cammack R, Porter JB. The relationship of intracellular iron chelation to the inhibition and regeneration of human ribonucleotide reductase. J Biol Chem. 1996;271:20291-20299.
    • (1996) J Biol Chem , vol.271 , pp. 20291-20299
    • Cooper, C.E.1    Lynagh, G.R.2    Hoyes, K.P.3    Hider, R.C.4    Cammack, R.5    Porter, J.B.6
  • 44
    • 0026690909 scopus 로고
    • Two mechanisms of iron uptake from transferrin by melanoma cells: The effect of desferrioxamine and ferric ammonium citrate
    • Richardson DR, Baker E. Two mechanisms of iron uptake from transferrin by melanoma cells: the effect of desferrioxamine and ferric ammonium citrate. J Biol Chem. 1992;267:13972-13979.
    • (1992) J Biol Chem , vol.267 , pp. 13972-13979
    • Richardson, D.R.1    Baker, E.2
  • 45
    • 0027938207 scopus 로고    scopus 로고
    • Nurse P. Ordering S phase and M phase in the cell cycle. Cell. 1994;79:547-550.
    • Nurse P. Ordering S phase and M phase in the cell cycle. Cell. 1994;79:547-550.
  • 46
    • 0028173667 scopus 로고
    • Acceleration of the G1/S phase transition by expression of cyclin D1 and E with an inducible system
    • Resnitzky D, Gossen M, Bujard H, Reed SI. Acceleration of the G1/S phase transition by expression of cyclin D1 and E with an inducible system. Mol Cell Biol. 1994;14:1669-1679.
    • (1994) Mol Cell Biol , vol.14 , pp. 1669-1679
    • Resnitzky, D.1    Gossen, M.2    Bujard, H.3    Reed, S.I.4
  • 47
    • 0029807526 scopus 로고    scopus 로고
    • Viewpoint: Putting the cell cycle in order
    • Nasmyth K. Viewpoint: putting the cell cycle in order. Science. 1996;274:1643-1645.
    • (1996) Science , vol.274 , pp. 1643-1645
    • Nasmyth, K.1
  • 49
    • 13944249549 scopus 로고    scopus 로고
    • Destabilization of cyclin D1 message plays a critical role in cell cycle exit upon mitogen withdrawal
    • Guo Y, Harwalkar J, Stacey DW, Hitomi M. Destabilization of cyclin D1 message plays a critical role in cell cycle exit upon mitogen withdrawal. Oncogene. 2005;24:1032-1042.
    • (2005) Oncogene , vol.24 , pp. 1032-1042
    • Guo, Y.1    Harwalkar, J.2    Stacey, D.W.3    Hitomi, M.4
  • 50
    • 0027201502 scopus 로고
    • Neuroblastoma sensitivity to growth inhibition by deferrioxamine: Evidence for a block in G1 phase of the cell cycle
    • Brodie C, Siriwardana G, Lucas J, et al. Neuroblastoma sensitivity to growth inhibition by deferrioxamine: evidence for a block in G1 phase of the cell cycle. Cancer Res. 1993;53:3968-3975.
    • (1993) Cancer Res , vol.53 , pp. 3968-3975
    • Brodie, C.1    Siriwardana, G.2    Lucas, J.3
  • 51
    • 0021259518 scopus 로고
    • Deferoxamine: A reversible S-phase inhibitor of human lymphocyte proliferation
    • Lederman HM, Cohen A, Lee JW, Freedman MH, Gelfand EW. Deferoxamine: a reversible S-phase inhibitor of human lymphocyte proliferation. Blood. 1984;64:748-753.
    • (1984) Blood , vol.64 , pp. 748-753
    • Lederman, H.M.1    Cohen, A.2    Lee, J.W.3    Freedman, M.H.4    Gelfand, E.W.5
  • 53
    • 0033568521 scopus 로고    scopus 로고
    • Down-regulation of cyclin D1 by transcriptional repression in MCF-7 human breast carcinoma cells induced by flavopiridol
    • Carlson B, Lahusenm T, Singh S, et al. Down-regulation of cyclin D1 by transcriptional repression in MCF-7 human breast carcinoma cells induced by flavopiridol. Cancer Res. 1999;59:4634-4641.
    • (1999) Cancer Res , vol.59 , pp. 4634-4641
    • Carlson, B.1    Lahusenm, T.2    Singh, S.3
  • 54
    • 3042684281 scopus 로고    scopus 로고
    • Mirk/dyrk1B kinase destabilizes cyclin D1 by phosphorylation at threonine 288
    • Zou Y, Ewton DZ, Deng X, Mercer SE, Friedman E. Mirk/dyrk1B kinase destabilizes cyclin D1 by phosphorylation at threonine 288. J Biol Chem. 2004;279:27790-27798.
    • (2004) J Biol Chem , vol.279 , pp. 27790-27798
    • Zou, Y.1    Ewton, D.Z.2    Deng, X.3    Mercer, S.E.4    Friedman, E.5
  • 55
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: Valuable new tools for cell biologist
    • Lee DH, Goldberg, AL. Proteasome inhibitors: valuable new tools for cell biologist. Trends Cell Biol. 1998;8:397-403.
    • (1998) Trends Cell Biol , vol.8 , pp. 397-403
    • Lee, D.H.1    Goldberg, A.L.2
  • 56
    • 33644958956 scopus 로고    scopus 로고
    • Proteasome inhibitor-induced apoptosis in human monocyte-derived dendritic cells
    • Nencioni A, Garuti A, Schwarzenberg K, et al. Proteasome inhibitor-induced apoptosis in human monocyte-derived dendritic cells. Eur J Immunol. 2006;36:681-689.
    • (2006) Eur J Immunol , vol.36 , pp. 681-689
    • Nencioni, A.1    Garuti, A.2    Schwarzenberg, K.3
  • 57
    • 2342667387 scopus 로고    scopus 로고
    • The development of proteasome inhibitors as anticancer drugs
    • Adams J. The development of proteasome inhibitors as anticancer drugs. Cancer Cell. 2004;5:417-421.
    • (2004) Cancer Cell , vol.5 , pp. 417-421
    • Adams, J.1
  • 58
    • 0030449964 scopus 로고    scopus 로고
    • Lithium inhibits glycogen synthase kinase-3 activity and mimics wingless signalling in intact cells
    • Stambolic V, Ruel L, Woodgett JR. Lithium inhibits glycogen synthase kinase-3 activity and mimics wingless signalling in intact cells. Curr Biol. 1996;6:1664-1668.
    • (1996) Curr Biol , vol.6 , pp. 1664-1668
    • Stambolic, V.1    Ruel, L.2    Woodgett, J.R.3
  • 61
    • 0034697022 scopus 로고    scopus 로고
    • Ubiquitination of free cyclin D1 is independent of phosphorylation on threonine 286
    • Germain D, Russell A, Thompson A, Hendley J. Ubiquitination of free cyclin D1 is independent of phosphorylation on threonine 286. J Biol Chem. 2000;275:12074-12079.
    • (2000) J Biol Chem , vol.275 , pp. 12074-12079
    • Germain, D.1    Russell, A.2    Thompson, A.3    Hendley, J.4
  • 62
    • 9444236895 scopus 로고    scopus 로고
    • Minireview: Cyclin D1: normal and abnormal functions
    • Fu M, Wang C, Li Z, Sakamaki T, Pestell RG. Minireview: cyclin D1: normal and abnormal functions. Endocrinology. 2004;145:5439-5447.
    • (2004) Endocrinology , vol.145 , pp. 5439-5447
    • Fu, M.1    Wang, C.2    Li, Z.3    Sakamaki, T.4    Pestell, R.G.5
  • 63
    • 0029849620 scopus 로고    scopus 로고
    • Cancer cell cycles
    • Sherr CJ. Cancer cell cycles. Science. 1996;274:1672-1677.
    • (1996) Science , vol.274 , pp. 1672-1677
    • Sherr, C.J.1
  • 64
    • 33746746418 scopus 로고    scopus 로고
    • Development of small-molecule cyclin D1-ablative agents
    • Huang JW, Shiau CW, Yang J, et al. Development of small-molecule cyclin D1-ablative agents. J Med Chem. 2006;49:4684-4689.
    • (2006) J Med Chem , vol.49 , pp. 4684-4689
    • Huang, J.W.1    Shiau, C.W.2    Yang, J.3
  • 65
    • 0034787555 scopus 로고    scopus 로고
    • p53-independent apoptosis mediated by tachpyridine, an anti-cancer iron chelator
    • Abeysinghe RD, Greene BT, Haynes R, et al. p53-independent apoptosis mediated by tachpyridine, an anti-cancer iron chelator. Carcinogenesis. 2001;22:1607-1614.
    • (2001) Carcinogenesis , vol.22 , pp. 1607-1614
    • Abeysinghe, R.D.1    Greene, B.T.2    Haynes, R.3
  • 67
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman MH, Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev. 2002;82:373-428.
    • (2002) Physiol Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 69
    • 0037069939 scopus 로고    scopus 로고
    • Curcumin-induced suppression of cell proliferation correlates with down-regulation of cyclin D1 expression and CDK4-mediated retinoblastoma protein phosphorylation
    • Mukhopadhyay A, Banerjee S, Stafford LJ, Xia C, Liu M, Aggarwal BB. Curcumin-induced suppression of cell proliferation correlates with down-regulation of cyclin D1 expression and CDK4-mediated retinoblastoma protein phosphorylation. Oncogene. 2002;21:8852-8861.
    • (2002) Oncogene , vol.21 , pp. 8852-8861
    • Mukhopadhyay, A.1    Banerjee, S.2    Stafford, L.J.3    Xia, C.4    Liu, M.5    Aggarwal, B.B.6
  • 71
    • 23044508946 scopus 로고    scopus 로고
    • Cyclin D1 in breast cancer pathogenesis
    • Arnold M, Papanikolaou, A. Cyclin D1 in breast cancer pathogenesis. J Clin Oncol. 2005;23:4215-4224.
    • (2005) J Clin Oncol , vol.23 , pp. 4215-4224
    • Arnold, M.1    Papanikolaou, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.