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Volumn 45, Issue 12, 2004, Pages 4583-4591

Involvement of protein kinase CK2 in angiogenesis and retinal neovascularization

Author keywords

[No Author keywords available]

Indexed keywords

1 (5 ISOQUINOLINESULFONYL) 2 METHYLPIPERAZINE; 2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 2 MORPHOLINO 8 PHENYLCHROMONE; 4 (4 FLUOROPHENYL) 2 (4 HYDROXYPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; 4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; 4 ETHYL 2 (4 METHOXYPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; 4,5,6,7 TETRABROMOBENZOTRIAZOLE; 5,6 DICHLOROBENZIMIDAZOLE RIBOSIDE; APIGENIN; CALPHOSTIN C; CASEIN KINASE II; CHRYSIN; CKI 7; DACTINOMYCIN; EMODIN; GROWTH FACTOR; ILOMASTAT; LY 379196; MITOGEN ACTIVATED PROTEIN KINASE P38; N [2 (4 BROMOCINNAMYLAMINO)ETHYL] 5 ISOQUINOLINESULFONAMIDE; N [2 [[N [3 (4 CHLOROPHENYL) 2 PROPENYL] N METHYLAMINO]METHYL]PHENYL] N (2 HYDROXYETHYL) 4 METHOXYBENZENESULFONAMIDE; OXYGEN; PROTEIN KINASE INHIBITOR; QUERCETIN; UNCLASSIFIED DRUG; WORTMANNIN;

EID: 9444245342     PISSN: 01460404     EISSN: None     Source Type: Journal    
DOI: 10.1167/iovs.04-0686     Document Type: Article
Times cited : (80)

References (87)
  • 1
    • 0030712335 scopus 로고    scopus 로고
    • Ischemia-driven angiogenesis
    • Dor Y, Eli K. Ischemia-driven angiogenesis. Trends Cardiovasc Med. 1997;7:289-294.
    • (1997) Trends Cardiovasc Med , vol.7 , pp. 289-294
    • Dor, Y.1    Eli, K.2
  • 2
    • 0348048874 scopus 로고    scopus 로고
    • Diabetic retinopathy
    • Frank RN. Diabetic retinopathy. N Engl J Med. 2004;350:48-58.
    • (2004) N Engl J Med , vol.350 , pp. 48-58
    • Frank, R.N.1
  • 3
    • 0002800936 scopus 로고
    • Basement membrane morphology in diabetes mellitus
    • Rifkin H, Porte D Jr, eds. New York: Elsevier;
    • østerby R. Basement membrane morphology in diabetes mellitus. In: Rifkin H, Porte D Jr, eds. Diabetes Mellitus. Theory and Practice. 4th ed. New York: Elsevier; 1990:220-233.
    • (1990) Diabetes Mellitus. Theory and Practice. 4th Ed. , pp. 220-233
    • Østerby, R.1
  • 4
    • 0033937497 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor (PAI)-1 overexpression in retinal microvessels of PAI-1 transgenic mice
    • Grant MB, Spoerri PE, Player DW, et al. Plasminogen activator inhibitor (PAI)-1 overexpression in retinal microvessels of PAI-1 transgenic mice. Invest Ophthalmol Vis Sci. 2000;41:2296-2302.
    • (2000) Invest Ophthalmol Vis Sci , vol.41 , pp. 2296-2302
    • Grant, M.B.1    Spoerri, P.E.2    Player, D.W.3
  • 5
    • 0030987103 scopus 로고    scopus 로고
    • Growth factors and diabetic retinopathy
    • Paques M, Massin O, Gaudric A. Growth factors and diabetic retinopathy. Diabetes Metab. 1997;23:125-130.
    • (1997) Diabetes Metab , vol.23 , pp. 125-130
    • Paques, M.1    Massin, O.2    Gaudric, A.3
  • 6
    • 0032968550 scopus 로고    scopus 로고
    • Molecular mechanisms of growth factor action in diabetic retinopathy
    • Aiello LP, Hata Y. Molecular mechanisms of growth factor action in diabetic retinopathy. Curr Opin Endocrinol Diabetes. 1999;6: 146-156.
    • (1999) Curr Opin Endocrinol Diabetes , vol.6 , pp. 146-156
    • Aiello, L.P.1    Hata, Y.2
  • 7
    • 0033852483 scopus 로고    scopus 로고
    • Role of vascular endothelial growth factor in diabetic vascular complications
    • Aiello LP, Wong JS. Role of vascular endothelial growth factor in diabetic vascular complications. Kidney Int. 2000;58(suppl 77): 113-119.
    • (2000) Kidney Int , vol.58 , Issue.SUPPL. 77 , pp. 113-119
    • Aiello, L.P.1    Wong, J.S.2
  • 8
    • 0030893294 scopus 로고    scopus 로고
    • Intravitreal growth factors in proliferative diabetic retinopathy: Correlation with neovascular activity and glycaemic management
    • Boulton M, Gregor Z, McLeod D, et al. Intravitreal growth factors in proliferative diabetic retinopathy: correlation with neovascular activity and glycaemic management. Br J Ophthalmol. 1997;81: 228-233.
    • (1997) Br J Ophthalmol , vol.81 , pp. 228-233
    • Boulton, M.1    Gregor, Z.2    McLeod, D.3
  • 9
    • 0022539028 scopus 로고
    • Insulin-like growth factors in vitreous: Studies in control and diabetic subjects with neovascularization
    • Grant M, Russell B, Fitzgerald C, Merimee TJ. Insulin-like growth factors in vitreous: studies in control and diabetic subjects with neovascularization. Diabetes. 1986;35:416-420.
    • (1986) Diabetes , vol.35 , pp. 416-420
    • Grant, M.1    Russell, B.2    Fitzgerald, C.3    Merimee, T.J.4
  • 10
    • 0025294817 scopus 로고
    • Basic fibroblast growth factor levels in the vitreous of patients with proliferative diabetic retinopathy
    • Sivalingam A, Kenney J, Brown GC, Benson WE, Donoso L. Basic fibroblast growth factor levels in the vitreous of patients with proliferative diabetic retinopathy. Arch Ophthalmol. 1990;108: 869-872.
    • (1990) Arch Ophthalmol , vol.108 , pp. 869-872
    • Sivalingam, A.1    Kenney, J.2    Brown, G.C.3    Benson, W.E.4    Donoso, L.5
  • 11
    • 0030963671 scopus 로고    scopus 로고
    • Growth factor alterations in advanced diabetic retinopathy: A possible role of blood retina barrier breakdown
    • Pfeiffer A, Spranger J, Meyer-Schwickerath R, Schatz H. Growth factor alterations in advanced diabetic retinopathy: a possible role of blood retina barrier breakdown. Diabetes. 1997;46(suppl 2): S26-S30.
    • (1997) Diabetes , vol.46 , Issue.SUPPL. 2
    • Pfeiffer, A.1    Spranger, J.2    Meyer-Schwickerath, R.3    Schatz, H.4
  • 12
    • 0033932964 scopus 로고    scopus 로고
    • Hepatocyte growth factor in vitreous and serum from patients with proliferative diabetic retinopathy
    • Canton A, Burgos R, Hernandez C, et al. Hepatocyte growth factor in vitreous and serum from patients with proliferative diabetic retinopathy. Br J Ophthalmol. 2000;84:732-735.
    • (2000) Br J Ophthalmol , vol.84 , pp. 732-735
    • Canton, A.1    Burgos, R.2    Hernandez, C.3
  • 14
    • 0034093621 scopus 로고    scopus 로고
    • Increased levels of platelet-derived growth factor in vitreous fluid of patients with proliferative diabetic retinopathy
    • Freyberger H, Brocker M, Yakut H, et al. Increased levels of platelet-derived growth factor in vitreous fluid of patients with proliferative diabetic retinopathy. Exp Clin Endocrinol Diabetes. 2000;108:106-109.
    • (2000) Exp Clin Endocrinol Diabetes , vol.108 , pp. 106-109
    • Freyberger, H.1    Brocker, M.2    Yakut, H.3
  • 15
    • 0032758384 scopus 로고    scopus 로고
    • Regulation of vascular endothelial growth factor-dependent retinal neovascularizatlon by insulin-like growth factor-1 receptor
    • Smith LE, Shen W, Perruzzi C, et al. Regulation of vascular endothelial growth factor-dependent retinal neovascularizatlon by insulin-like growth factor-1 receptor. Nat Med. 1999;5:1390-1395.
    • (1999) Nat Med , vol.5 , pp. 1390-1395
    • Smith, L.E.1    Shen, W.2    Perruzzi, C.3
  • 17
    • 1142287447 scopus 로고    scopus 로고
    • Role of growth factors and the wound healing response in age-related macular degeneration
    • Schlingemann RO. Role of growth factors and the wound healing response in age-related macular degeneration. Graefes Arch Clin Exp Ophthalmol. 2004;242:91-101.
    • (2004) Graefes Arch Clin Exp Ophthalmol , vol.242 , pp. 91-101
    • Schlingemann, R.O.1
  • 18
    • 0033882794 scopus 로고    scopus 로고
    • Blockade of vascular endothelial cell growth factor receptor signaling is sufficient to completely prevent retinal neovascularization
    • Ozaki H, Seo MS, Ozaki K, et al. Blockade of vascular endothelial cell growth factor receptor signaling is sufficient to completely prevent retinal neovascularization. Am J Pathol. 2000;156:697-707.
    • (2000) Am J Pathol , vol.156 , pp. 697-707
    • Ozaki, H.1    Seo, M.S.2    Ozaki, K.3
  • 19
    • 0030758411 scopus 로고    scopus 로고
    • Vascular endothelial growth factor and the eye: Biochemical mechanisms of action and implications for novel therapies
    • Aiello LP. Vascular endothelial growth factor and the eye: biochemical mechanisms of action and implications for novel therapies. Ophthalmic Res. 1997;29:354-362.
    • (1997) Ophthalmic Res , vol.29 , pp. 354-362
    • Aiello, L.P.1
  • 20
    • 0031006861 scopus 로고    scopus 로고
    • Vascular endothelial growth factor in ocular neovascularization and proliferative diabetic retinopathy
    • Miller JW, Adamis AP, Aiello LP. Vascular endothelial growth factor in ocular neovascularization and proliferative diabetic retinopathy. Diabetes Metab Rev. 1997;13:37-50.
    • (1997) Diabetes Metab Rev , vol.13 , pp. 37-50
    • Miller, J.W.1    Adamis, A.P.2    Aiello, L.P.3
  • 22
    • 0037721109 scopus 로고    scopus 로고
    • Synergistic effect of angiopoietin-1 and vascular endothelial growth factor on neoangiogenesis in hypercholesterolemic rabbit model with acute hindlimb ischemia
    • Shyu KG, Chang H, Isner JM. Synergistic effect of angiopoietin-1 and vascular endothelial growth factor on neoangiogenesis in hypercholesterolemic rabbit model with acute hindlimb ischemia. Life Sci. 2003;73:563-579.
    • (2003) Life Sci , vol.73 , pp. 563-579
    • Shyu, K.G.1    Chang, H.2    Isner, J.M.3
  • 23
    • 0029072011 scopus 로고
    • Basic fibroblast growth factor upregulates the expression of vascular endothelial growth factor in vascular smooth muscle cells: Synergistic interaction with hypoxia
    • Stavri GT, Zachary IC, Baskerville PA, Martin JF, Erusalimsky JD. Basic fibroblast growth factor upregulates the expression of vascular endothelial growth factor in vascular smooth muscle cells: synergistic interaction with hypoxia. Circulation. 1995;92:11-14.
    • (1995) Circulation , vol.92 , pp. 11-14
    • Stavri, G.T.1    Zachary, I.C.2    Baskerville, P.A.3    Martin, J.F.4    Erusalimsky, J.D.5
  • 24
    • 0242492548 scopus 로고    scopus 로고
    • Using gene expression profiling to identify the molecular basis of the synergistic actions of hepatocyte growth factor and vascular endothelial growth factor in human endothelial cells
    • Gerritsen ME, Tomlinson JE, Zlot C, Ziman M, Hwang S. Using gene expression profiling to identify the molecular basis of the synergistic actions of hepatocyte growth factor and vascular endothelial growth factor in human endothelial cells. Br J Pharmacol. 2003;140:595-610.
    • (2003) Br J Pharmacol , vol.140 , pp. 595-610
    • Gerritsen, M.E.1    Tomlinson, J.E.2    Zlot, C.3    Ziman, M.4    Hwang, S.5
  • 25
    • 0033934848 scopus 로고    scopus 로고
    • The platelet-derived growth factor receptor stimulation of p42/p44 mitogen-activated protein kinase in airway smooth muscle involves a G-protein-mediated tyrosine phosphorylation of Gab1
    • Rakhit S, Pyne S, Pyne NJ. The platelet-derived growth factor receptor stimulation of p42/p44 mitogen-activated protein kinase in airway smooth muscle involves a G-protein-mediated tyrosine phosphorylation of Gab1. Mol Pharmacol. 2000;58:413-420.
    • (2000) Mol Pharmacol , vol.58 , pp. 413-420
    • Rakhit, S.1    Pyne, S.2    Pyne, N.J.3
  • 26
    • 0034638844 scopus 로고    scopus 로고
    • Coordinate control of muscle cell survival by distinct insulin-like growth factor activated signaling pathways
    • Lawlor MA, Rotwein P. Coordinate control of muscle cell survival by distinct insulin-like growth factor activated signaling pathways. J Cell Biol. 2000;151:1131-1140.
    • (2000) J Cell Biol , vol.151 , pp. 1131-1140
    • Lawlor, M.A.1    Rotwein, P.2
  • 27
    • 0026027581 scopus 로고
    • Plasminogen activator production by human retinal endothelial cells of nondiabetic and diabetic origin
    • Grant MB, Guay C. Plasminogen activator production by human retinal endothelial cells of nondiabetic and diabetic origin. Invest Ophthalmol Vis Sci. 1991;32:53-64.
    • (1991) Invest Ophthalmol Vis Sci , vol.32 , pp. 53-64
    • Grant, M.B.1    Guay, C.2
  • 28
    • 0036325335 scopus 로고    scopus 로고
    • Effects of tenascin-C on normal and diabetic retinal endothelial cells in culture
    • Castellon R, Caballero S, Hamdi HK, et al. Effects of tenascin-C on normal and diabetic retinal endothelial cells in culture. Invest Ophthalmol Vis Sci. 2002;43:2758-2766.
    • (2002) Invest Ophthalmol Vis Sci , vol.43 , pp. 2758-2766
    • Castellon, R.1    Caballero, S.2    Hamdi, H.K.3
  • 29
    • 0032746494 scopus 로고    scopus 로고
    • Casein kinase II activity is required for transferrin receptor endocytosis
    • Cotlin LF, Siddiqui MA, Simpson F, Collawn JF. Casein kinase II activity is required for transferrin receptor endocytosis. J Biol Chem. 1999;274:30550-30556.
    • (1999) J Biol Chem , vol.274 , pp. 30550-30556
    • Cotlin, L.F.1    Siddiqui, M.A.2    Simpson, F.3    Collawn, J.F.4
  • 30
    • 0014854403 scopus 로고
    • Inhibitors of photosynthesis. VI. Syntheses of electronegatively substituting benzimidazoles
    • Büchel KH. Inhibitors of photosynthesis. VI. Syntheses of electronegatively substituting benzimidazoles (in German). Z Naturforsch B. 1970;25:945-953.
    • (1970) Z Naturforsch B , vol.25 , pp. 945-953
    • Büchel, K.H.1
  • 31
    • 0036433260 scopus 로고    scopus 로고
    • Estradiol reverses TGF-β1-induced mesangial cell apoptosis by a casein kinase 2-dependent mechanism
    • Negulescu O, Bognar I, Lei J, Devarajan P, Silbiger S, Neugarten J. Estradiol reverses TGF-β1-induced mesangial cell apoptosis by a casein kinase 2-dependent mechanism. Kidney Int. 2002;62: 1989-1998.
    • (2002) Kidney Int , vol.62 , pp. 1989-1998
    • Negulescu, O.1    Bognar, I.2    Lei, J.3    Devarajan, P.4    Silbiger, S.5    Neugarten, J.6
  • 32
    • 0036024242 scopus 로고    scopus 로고
    • Inhibition of LPS-stimulated pathways in macrophages by the flavonoid luteolin
    • Xagorari A, Roussos C, Papapetropoulos A. Inhibition of LPS-stimulated pathways in macrophages by the flavonoid luteolin. Br J Pharmacol. 2002;136:1058-1064.
    • (2002) Br J Pharmacol , vol.136 , pp. 1058-1064
    • Xagorari, A.1    Roussos, C.2    Papapetropoulos, A.3
  • 33
    • 0033060267 scopus 로고    scopus 로고
    • Emodin, an anthraquinone derivative isolated from the rhizomes of Rheum palmatum, selectively inhibits the activity of casein kinase II as a competitive inhibitor
    • Yim H, Lee YH, Lee CH, Lee SK. Emodin, an anthraquinone derivative isolated from the rhizomes of Rheum palmatum, selectively inhibits the activity of casein kinase II as a competitive inhibitor. Planta Med. 1999;65:9-13.
    • (1999) Planta Med , vol.65 , pp. 9-13
    • Yim, H.1    Lee, Y.H.2    Lee, C.H.3    Lee, S.K.4
  • 34
    • 0037043777 scopus 로고    scopus 로고
    • Functional interaction of protein kinase CK2 and c-Myc in lymphomagenesis
    • Channavajhala P, Seldin DC. Functional interaction of protein kinase CK2 and c-Myc in lymphomagenesis. Oncogene. 2002;21: 5280-5288.
    • (2002) Oncogene , vol.21 , pp. 5280-5288
    • Channavajhala, P.1    Seldin, D.C.2
  • 35
    • 0035805108 scopus 로고    scopus 로고
    • Selectivity of 4,5,6,7-tetrabromobenzotriazole, an ATP site-directed inhibitor of protein kinase CK2 (casein kinase-2)
    • Sarno S, Reddy H, Meggio F, et al. Selectivity of 4,5,6,7- tetrabromobenzotriazole, an ATP site-directed inhibitor of protein kinase CK2 (casein kinase-2). FEBS Lett. 2001;496:44-48.
    • (2001) FEBS Lett , vol.496 , pp. 44-48
    • Sarno, S.1    Reddy, H.2    Meggio, F.3
  • 36
    • 0034775155 scopus 로고    scopus 로고
    • Structural features underlying selective inhibition of protein kinase CK2 by ATP site-directed tetrabromo-2-benzotriazole
    • Battistutta R, De Moliner E, Sarno S, Zanotti G, Pinna LA. Structural features underlying selective inhibition of protein kinase CK2 by ATP site-directed tetrabromo-2-benzotriazole. Protein Sci. 2001; 10:2200-2206.
    • (2001) Protein Sci , vol.10 , pp. 2200-2206
    • Battistutta, R.1    De Moliner, E.2    Sarno, S.3    Zanotti, G.4    Pinna, L.A.5
  • 37
    • 0034487992 scopus 로고    scopus 로고
    • Effects of daily oral administration of quercetin chalcone and modified citrus pectin
    • Hayashi A, Gillen AC, Lott JR. Effects of daily oral administration of quercetin chalcone and modified citrus pectin. Altern Med Rev. 2000;5:546-552.
    • (2000) Altern Med Rev , vol.5 , pp. 546-552
    • Hayashi, A.1    Gillen, A.C.2    Lott, J.R.3
  • 38
    • 0036400016 scopus 로고    scopus 로고
    • Dietary flavonoids: Bioavailability, metabolic effects, and safety
    • Ross JA, Kasum CM. Dietary flavonoids: bioavailability, metabolic effects, and safety. Annu Rev Nutr. 2002;22:19-34.
    • (2002) Annu Rev Nutr , vol.22 , pp. 19-34
    • Ross, J.A.1    Kasum, C.M.2
  • 39
    • 0028815295 scopus 로고
    • Vascular endothelial growth factor/vascular permeability factor expression in a mouse model of retinal neovascularization
    • Pierce EA, Avery RL, Foley ED, Aiello LP, Smith LE. Vascular endothelial growth factor/vascular permeability factor expression in a mouse model of retinal neovascularization. Proc Natl Acad Sci USA. 1995;92:905-909.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 905-909
    • Pierce, E.A.1    Avery, R.L.2    Foley, E.D.3    Aiello, L.P.4    Smith, L.E.5
  • 40
    • 0035653641 scopus 로고    scopus 로고
    • Adenosine receptor antagonists and retinal neovascularization in vivo
    • Mino RP, Spoerri PE, Caballero S, et al. Adenosine receptor antagonists and retinal neovascularization in vivo. Invest Ophthalmol Vis Sci. 2001;42:3320-3324.
    • (2001) Invest Ophthalmol Vis Sci , vol.42 , pp. 3320-3324
    • Mino, R.P.1    Spoerri, P.E.2    Caballero, S.3
  • 41
    • 0033873786 scopus 로고    scopus 로고
    • Flavonoids apigenin and quercetin inhibit melanoma growth and metastatic potential
    • Caltagirone S, Rossi C, Poggi A, et al. Flavonoids apigenin and quercetin inhibit melanoma growth and metastatic potential. Int J Cancer. 2000;87:595-600.
    • (2000) Int J Cancer , vol.87 , pp. 595-600
    • Caltagirone, S.1    Rossi, C.2    Poggi, A.3
  • 42
    • 0019391447 scopus 로고
    • Metabolism of [14C]emodin in the rat
    • Bachmann M, Schlatter C. Metabolism of [14C]emodin in the rat. Xenobiotica. 1981;11:217-225.
    • (1981) Xenobiotica , vol.11 , pp. 217-225
    • Bachmann, M.1    Schlatter, C.2
  • 43
    • 0033678216 scopus 로고    scopus 로고
    • Aloe-emodin quinone pretreatment reduces acute liver injury induced by carbon tetrachloride
    • Arosio B, Gagliano N, Fusaro LM, et al. Aloe-emodin quinone pretreatment reduces acute liver injury induced by carbon tetrachloride. Pharmacol Toxicol. 2000;87:229-233.
    • (2000) Pharmacol Toxicol , vol.87 , pp. 229-233
    • Arosio, B.1    Gagliano, N.2    Fusaro, L.M.3
  • 44
    • 9444259793 scopus 로고    scopus 로고
    • NTP toxicology and carcinogenesis studies of emodin (CAS No. 518-82-1) feed studies in F344/N rats and B6C3F1 mice
    • National Toxicology Program. NTP toxicology and carcinogenesis studies of emodin (CAS No. 518-82-1) feed studies in F344/N rats and B6C3F1 mice. Natl Taxicol Program Tech Rep Ser. 2001;493: 1-278.
    • (2001) Natl Taxicol Program Tech Rep Ser , vol.493 , pp. 1-278
  • 46
    • 0033018831 scopus 로고    scopus 로고
    • Protein kinase CK2 and its role in cellular proliferation, development and pathology
    • Guerra B, Issinger OG. Protein kinase CK2 and its role in cellular proliferation, development and pathology. Electrophoresis. 1999; 20:391-408.
    • (1999) Electrophoresis , vol.20 , pp. 391-408
    • Guerra, B.1    Issinger, O.G.2
  • 47
    • 0036077214 scopus 로고    scopus 로고
    • Translated Alu sequence determines nuclear localization of a novel catalytic subunit of casein kinase 2
    • Hilgard P, Huang T, Wolkoff AW, Stockert RJ. Translated Alu sequence determines nuclear localization of a novel catalytic subunit of casein kinase 2. Am J Physiol Cell Physiol. 2002;283:C472-C483.
    • (2002) Am J Physiol Cell Physiol , vol.283
    • Hilgard, P.1    Huang, T.2    Wolkoff, A.W.3    Stockert, R.J.4
  • 48
    • 0037929502 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of protein kinase CK2 by Src-related tyrosine kinases correlates with increased catalytic activity
    • Donella-Deana A, Cesaro L, Sarno S, et al. Tyrosine phosphorylation of protein kinase CK2 by Src-related tyrosine kinases correlates with increased catalytic activity. Biochem J. 2003;372:841-849.
    • (2003) Biochem J , vol.372 , pp. 841-849
    • Donella-Deana, A.1    Cesaro, L.2    Sarno, S.3
  • 49
    • 0037269847 scopus 로고    scopus 로고
    • Protein kinase CK2: Structure, regulation and role in cellular decisions of life and death
    • Litchneld DW. Protein kinase CK2: structure, regulation and role in cellular decisions of life and death. Biochem J. 2003;369:1-15.
    • (2003) Biochem J , vol.369 , pp. 1-15
    • Litchneld, D.W.1
  • 50
    • 0036568813 scopus 로고    scopus 로고
    • Joining the cell survival squad: An emerging role for protein kinase CK2
    • Ahmed K, Gerber DA, Cochet C. Joining the cell survival squad: an emerging role for protein kinase CK2. Trends Cell Biol. 2002;12: 226-230.
    • (2002) Trends Cell Biol , vol.12 , pp. 226-230
    • Ahmed, K.1    Gerber, D.A.2    Cochet, C.3
  • 51
    • 0037107552 scopus 로고    scopus 로고
    • Protein kinase CK2: A challenge to canons
    • Pinna LA. Protein kinase CK2: a challenge to canons. J Cell Sci. 2002;115:3873-3878.
    • (2002) J Cell Sci , vol.115 , pp. 3873-3878
    • Pinna, L.A.1
  • 52
    • 0038340907 scopus 로고    scopus 로고
    • The raison d'être of constitutively active protein kinases: The lesson of CK2
    • Pinna LA. The raison d'être of constitutively active protein kinases: the lesson of CK2. Acc Chem Res. 2003;36:378-384.
    • (2003) Acc Chem Res , vol.36 , pp. 378-384
    • Pinna, L.A.1
  • 53
    • 1542409972 scopus 로고    scopus 로고
    • Protein kinase CK2 as regulator of cell survival: Implications for cancer therapy
    • Unger GM, Davis AT, Slaton JW, Ahmed K. Protein kinase CK2 as regulator of cell survival: implications for cancer therapy. Curr Cancer Drug Targets. 2004;4:77-84.
    • (2004) Curr Cancer Drug Targets , vol.4 , pp. 77-84
    • Unger, G.M.1    Davis, A.T.2    Slaton, J.W.3    Ahmed, K.4
  • 54
    • 2442594082 scopus 로고    scopus 로고
    • Protein kinase CK2: A new view of an old molecular complex
    • Filhol O, Martiel JL, Cochet C. Protein kinase CK2: a new view of an old molecular complex. EMBO Rep. 2004;5:351-355.
    • (2004) EMBO Rep , vol.5 , pp. 351-355
    • Filhol, O.1    Martiel, J.L.2    Cochet, C.3
  • 55
    • 11144355098 scopus 로고    scopus 로고
    • The protein kinase CK2 facilitates repair of chromosomal DNA single-strand breaks
    • Loizou JI, El-Khamisy SF, Zlatanou A, et al. The protein kinase CK2 facilitates repair of chromosomal DNA single-strand breaks. Cell. 2004;117:17-28.
    • (2004) Cell , vol.117 , pp. 17-28
    • Loizou, J.I.1    El-Khamisy, S.F.2    Zlatanou, A.3
  • 56
    • 0037093352 scopus 로고    scopus 로고
    • Protein kinase CK2 inhibitor 4,5,6,7-tetrabromobenzotriazole (TBB) induces apoptosis and caspase-dependent degradation of haematopoietic lineage cell-specific protein 1 (HS1) in Jurkat cells
    • Ruzzene M, Penzo D, Pinna LA. Protein kinase CK2 inhibitor 4,5,6,7-tetrabromobenzotriazole (TBB) induces apoptosis and caspase-dependent degradation of haematopoietic lineage cell-specific protein 1 (HS1) in Jurkat cells. Biochem J. 2002;364:41-47.
    • (2002) Biochem J , vol.364 , pp. 41-47
    • Ruzzene, M.1    Penzo, D.2    Pinna, L.A.3
  • 57
    • 0035669740 scopus 로고    scopus 로고
    • Protein kinase CK2: Signaling and tumorigenesis in the mammary gland
    • Landesman-Bollag E, Song DH, Romieu-Mourez R, et al. Protein kinase CK2: signaling and tumorigenesis in the mammary gland. Mol Cell Biochem. 2001;227:153-165.
    • (2001) Mol Cell Biochem , vol.227 , pp. 153-165
    • Landesman-Bollag, E.1    Song, D.H.2    Romieu-Mourez, R.3
  • 59
    • 0037112514 scopus 로고    scopus 로고
    • Protein kinase CK2 promotes aberrant activation of nuclear factor-κB, transformed phenotype, and survival of breast cancer cells
    • Romieu-Mourez R, Landesman-Bollag E, Seldin DC, Sonenshein GE. Protein kinase CK2 promotes aberrant activation of nuclear factor-κB, transformed phenotype, and survival of breast cancer cells. Cancer Res. 2002;62:6770-6778.
    • (2002) Cancer Res , vol.62 , pp. 6770-6778
    • Romieu-Mourez, R.1    Landesman-Bollag, E.2    Seldin, D.C.3    Sonenshein, G.E.4
  • 60
    • 0037334895 scopus 로고    scopus 로고
    • One-thousand-and-one substrates of protein kinase CK2?
    • Meggio F, Pinna LA. One-thousand-and-one substrates of protein kinase CK2? FASEB J. 2003;17:349-368.
    • (2003) FASEB J , vol.17 , pp. 349-368
    • Meggio, F.1    Pinna, L.A.2
  • 61
    • 0031306770 scopus 로고    scopus 로고
    • Protein kinase CK2 ("casein kinase-2") and its implication in cell division and proliferation
    • Pinna LA, Meggio F. Protein kinase CK2 ("casein kinase-2") and its implication in cell division and proliferation. Prog Cell Cycle Res. 1997;3:77-97.
    • (1997) Prog Cell Cycle Res , vol.3 , pp. 77-97
    • Pinna, L.A.1    Meggio, F.2
  • 62
    • 0345580627 scopus 로고    scopus 로고
    • Expression and regulation of protein kinase CK2 during the cell cycle
    • Bosc DG, Luscher B, Litchfield DW. Expression and regulation of protein kinase CK2 during the cell cycle. Mol Cell Biochem. 1999:191:213-222.
    • (1999) Mol Cell Biochem , vol.191 , pp. 213-222
    • Bosc, D.G.1    Luscher, B.2    Litchfield, D.W.3
  • 63
    • 0035677061 scopus 로고    scopus 로고
    • Consequences of CK2 signaling to the nuclear matrix
    • Yu S, Wang H, Davis A, Ahmed K. Consequences of CK2 signaling to the nuclear matrix. Mol Cell Biochem. 2001;227:67-71.
    • (2001) Mol Cell Biochem , vol.227 , pp. 67-71
    • Yu, S.1    Wang, H.2    Davis, A.3    Ahmed, K.4
  • 65
    • 0037155875 scopus 로고    scopus 로고
    • Urokinase-dependent human vascular smooth muscle cell adhesion requires selective vitronectin phosphorylation by ectoprotein kinase CK2
    • Stepanova V, Jerke U, Sagach V, et al. Urokinase-dependent human vascular smooth muscle cell adhesion requires selective vitronectin phosphorylation by ectoprotein kinase CK2. J Biol Chem. 2002;277:10265-10272.
    • (2002) J Biol Chem , vol.277 , pp. 10265-10272
    • Stepanova, V.1    Jerke, U.2    Sagach, V.3
  • 66
    • 0035670403 scopus 로고    scopus 로고
    • Localization of individual subunits of protein kinase CK2 to the endoplasmic reticulum and to the Golgi apparatus
    • Faust M, Jung M, Gunther J, Zimmermann R, Montenarh M. Localization of individual subunits of protein kinase CK2 to the endoplasmic reticulum and to the Golgi apparatus. Mol Cell Biochem. 2001;227:73-80.
    • (2001) Mol Cell Biochem , vol.227 , pp. 73-80
    • Faust, M.1    Jung, M.2    Gunther, J.3    Zimmermann, R.4    Montenarh, M.5
  • 68
    • 0037305657 scopus 로고    scopus 로고
    • Live-cell fluorescence imaging reveals the dynamics of protein kinase CK2 individual subunits
    • Filhol O, Nueda A, Martel V, et al. Live-cell fluorescence imaging reveals the dynamics of protein kinase CK2 individual subunits. Mol Cell Biol. 2003;23:975-987.
    • (2003) Mol Cell Biol , vol.23 , pp. 975-987
    • Filhol, O.1    Nueda, A.2    Martel, V.3
  • 71
    • 0029784488 scopus 로고    scopus 로고
    • Fibroblast growth factor-2 binds to the regulatory β subunit of CK2 and directly stimulates CK2 activity toward nucleolin
    • Bonnet H, Filhol O, Truchet I, et al. Fibroblast growth factor-2 binds to the regulatory β subunit of CK2 and directly stimulates CK2 activity toward nucleolin. J Biol Chem. 1996;271:24781-24787.
    • (1996) J Biol Chem , vol.271 , pp. 24781-24787
    • Bonnet, H.1    Filhol, O.2    Truchet, I.3
  • 72
    • 0033950003 scopus 로고    scopus 로고
    • Uncoupling of cell proliferation and differentiation activities of basic fibroblast growth factor
    • Bailly K, Soulet F, Leroy D, Amalric F, Bouche G. Uncoupling of cell proliferation and differentiation activities of basic fibroblast growth factor. FASEB J. 2000;14:333-344.
    • (2000) FASEB J , vol.14 , pp. 333-344
    • Bailly, K.1    Soulet, F.2    Leroy, D.3    Amalric, F.4    Bouche, G.5
  • 73
    • 0028316424 scopus 로고
    • Daidzein inhibits insulin- or insulin-like growth factor-1-mediated signaling in cell cycle progression of Swiss 3T3 cells
    • Higashi K, Ogawara H. Daidzein inhibits insulin- or insulin-like growth factor-1-mediated signaling in cell cycle progression of Swiss 3T3 cells. Biochim Biophys Acta. 1994;1221:29-35.
    • (1994) Biochim Biophys Acta , vol.1221 , pp. 29-35
    • Higashi, K.1    Ogawara, H.2
  • 74
    • 0029873891 scopus 로고    scopus 로고
    • Characterization of insulin-like growth factor binding protein-1 kinases from human hepatoma cells
    • Ankrapp DP, Jones JI, Clemmons DR. Characterization of insulin-like growth factor binding protein-1 kinases from human hepatoma cells. J Cell Biochem. 1996;60:387-399.
    • (1996) J Cell Biochem , vol.60 , pp. 387-399
    • Ankrapp, D.P.1    Jones, J.I.2    Clemmons, D.R.3
  • 75
    • 0034464043 scopus 로고    scopus 로고
    • The effect of phosphorylation by casein kinase 2 on the activity of insulin-like growth factor-binding protein-3
    • Coverley JA, Martin JL, Baxter RC. The effect of phosphorylation by casein kinase 2 on the activity of insulin-like growth factor-binding protein-3. Endocrinology. 2000;141:564-570.
    • (2000) Endocrinology , vol.141 , pp. 564-570
    • Coverley, J.A.1    Martin, J.L.2    Baxter, R.C.3
  • 76
    • 1942486312 scopus 로고    scopus 로고
    • CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37
    • Miyata Y, Nishida E. CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37. Mol Cell Biol. 2004;24:4065-4074.
    • (2004) Mol Cell Biol , vol.24 , pp. 4065-4074
    • Miyata, Y.1    Nishida, E.2
  • 77
    • 0035937168 scopus 로고    scopus 로고
    • A potential role of nuclear matrix-associated protein kinase CK2 in protection against drug-induced apoptosis in cancer cells
    • Guo C, Yu S, Davis AT, Wang H, Green JE, Ahmed K. A potential role of nuclear matrix-associated protein kinase CK2 in protection against drug-induced apoptosis in cancer cells. J Biol Chem. 2001; 276:5992-5999.
    • (2001) J Biol Chem , vol.276 , pp. 5992-5999
    • Guo, C.1    Yu, S.2    Davis, A.T.3    Wang, H.4    Green, J.E.5    Ahmed, K.6
  • 78
    • 1642535590 scopus 로고    scopus 로고
    • Emodin enhances arsenic trioxide-induced apoptosis via generation of reactive oxygen species and inhibition of survival signaling
    • Yi J, Yang J, He R, et al. Emodin enhances arsenic trioxide-induced apoptosis via generation of reactive oxygen species and inhibition of survival signaling. Cancer Res. 2004;64:108-116.
    • (2004) Cancer Res , vol.64 , pp. 108-116
    • Yi, J.1    Yang, J.2    He, R.3
  • 79
    • 1342324038 scopus 로고    scopus 로고
    • Emodin-induced apoptosis through p53-dependent pathway in human hepatoma cells
    • Shieh DE, Chen YY, Yen MH, Chiang LC, Lin CC. Emodin-induced apoptosis through p53-dependent pathway in human hepatoma cells. Life Sci. 2004;74:2279-2290.
    • (2004) Life Sci , vol.74 , pp. 2279-2290
    • Shieh, D.E.1    Chen, Y.Y.2    Yen, M.H.3    Chiang, L.C.4    Lin, C.C.5
  • 80
    • 0037114436 scopus 로고    scopus 로고
    • Emodin induces apoptosis in human promyeloleukemic HL-60 cells accompanied by activation of caspase 3 cascade but independent of reactive oxygen species production
    • Chen YC, Shen SC, Lee WR, et al. Emodin induces apoptosis in human promyeloleukemic HL-60 cells accompanied by activation of caspase 3 cascade but independent of reactive oxygen species production. Biochem Pharmacol. 2002;64:1713-1724.
    • (2002) Biochem Pharmacol , vol.64 , pp. 1713-1724
    • Chen, Y.C.1    Shen, S.C.2    Lee, W.R.3
  • 83
    • 0029005204 scopus 로고
    • The effect of oxygen on vasoformative cell division. Evidence that "physiological hypoxia" is the stimulus for normal retinal vasculogenesis
    • Chan-Ling T, Gock B, Stone J. The effect of oxygen on vasoformative cell division. Evidence that "physiological hypoxia" is the stimulus for normal retinal vasculogenesis. Invest Ophthalmol Vis Sci. 1995;36:1201-1214.
    • (1995) Invest Ophthalmol Vis Sci , vol.36 , pp. 1201-1214
    • Chan-Ling, T.1    Gock, B.2    Stone, J.3
  • 84
    • 0030004434 scopus 로고    scopus 로고
    • Vasoproliferation in the neonatal dog model of oxygen-induced retinopathy
    • McLeod DS, Crone SN, Lutty GA. Vasoproliferation in the neonatal dog model of oxygen-induced retinopathy. Invest Ophthalmol Vis Sci. 1996;37:1322-1333.
    • (1996) Invest Ophthalmol Vis Sci , vol.37 , pp. 1322-1333
    • McLeod, D.S.1    Crone, S.N.2    Lutty, G.A.3
  • 85
    • 0037449461 scopus 로고    scopus 로고
    • Quercetin, a dietary-derived flavonoid, possesses antiangiogenic potential
    • Tan WF, Lin LP, Li MH, et al. Quercetin, a dietary-derived flavonoid, possesses antiangiogenic potential. Eur J Pharmacol. 2003;459:255-262.
    • (2003) Eur J Pharmacol , vol.459 , pp. 255-262
    • Tan, W.F.1    Lin, L.P.2    Li, M.H.3
  • 86
    • 0035964450 scopus 로고    scopus 로고
    • Resveratrol and quercetin inhibit angiogenesis in vitro
    • Igura K, Ohta T, Kuroda Y, Kaji K. Resveratrol and quercetin inhibit angiogenesis in vitro. Cancer Lett. 2001;171:11-16.
    • (2001) Cancer Lett , vol.171 , pp. 11-16
    • Igura, K.1    Ohta, T.2    Kuroda, Y.3    Kaji, K.4


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