메뉴 건너뛰기




Volumn 43, Issue 1, 2000, Pages 1-18

Cyclin-dependent kinase inhibitors: Useful targets in cell cycle regulation

Author keywords

[No Author keywords available]

Indexed keywords

2 (2 AMINOCYCLOHEXYLAMINO) 6 (3,4 DICHLOROANILINO) 9 ETHYLPURINE; 2 (3 CHLOROANILINO) 4 [2 (3 HYDROXYPROPYLAMINO) 4 PYRIDYL]PYRIMIDINE; 2 BIS(2 HYDROXYETHYL)AMINO 9 ISOPROPYL 6 (4 METHOXYBENZYLAMINO)PURINE; 3 [(4,5 DIMETHYL 1H PYRROL 2 YL)METHYLENE] 1,3 DIHYDRO 2H INDOL 2 ONE; 7 HYDROXYSTAUROSPORINE; ACETOPHTHALIDIN; AG 12268; AG 12275; ANTINEOPLASTIC AGENT; BOHEMINE; BUTYROLACTONE; CYCLIN DEPENDENT KINASE INHIBITOR; FASUDIL; FLAVOPIRIDOL; ISOPENTYLADENINE; K 252A; N METHYL 4 [2 (2 OXOPYRIDO[2,3 E]INDOL 3 YLIDENE)HYDRAZINO]PHENYLMETHANESULFONAMIDE; N METHYL 4 [2 (7 OXOTHIAZOLO[4,5 E]INDOL 8 YLIDENE)HYDRAZINO]BENZENESULFONAMIDE; OLOMOUCINE; OXINDOLE; PAULLONE; PURVALANOL; QUERCETIN; ROSCOVITINE; STAUROSPORINE; UNCLASSIFIED DRUG;

EID: 0034642532     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm990256j     Document Type: Review
Times cited : (335)

References (189)
  • 2
    • 0031040149 scopus 로고    scopus 로고
    • The development and clinical utility of the taxane class of antimicrotubule chemotherapy agents
    • Rowinsky, E. K. The Development and Clinical Utility of the Taxane Class of Antimicrotubule Chemotherapy Agents. Annu. Rev. Med. 1997, 48, 353-374.
    • (1997) Annu. Rev. Med. , vol.48 , pp. 353-374
    • Rowinsky, E.K.1
  • 5
    • 0029114101 scopus 로고
    • Staurosporine, a potentially important gift from a microorganism
    • Omura, S.; Sasaki, Y.; Iwai, Y.; Takeshima, H. Staurosporine, a Potentially Important Gift from a Microorganism. J. Antibiot. 1995, 48, 535-548.
    • (1995) J. Antibiot. , vol.48 , pp. 535-548
    • Omura, S.1    Sasaki, Y.2    Iwai, Y.3    Takeshima, H.4
  • 8
    • 27644447540 scopus 로고    scopus 로고
    • Recent advances in tyrosine kinase inhibitors
    • Fry, D. W. Recent Advances in Tyrosine Kinase Inhibitors. Annu. Rep. Med. Chem. 1996, 31, 151-160.
    • (1996) Annu. Rep. Med. Chem. , vol.31 , pp. 151-160
    • Fry, D.W.1
  • 10
    • 0031809781 scopus 로고    scopus 로고
    • The therapeutic potential of targeting the cell cycle
    • Webster, K. R. The Therapeutic Potential of Targeting the Cell Cycle. Exp. Opin. Invest. Drugs 1998, 7, 865-887.
    • (1998) Exp. Opin. Invest. Drugs , vol.7 , pp. 865-887
    • Webster, K.R.1
  • 11
    • 0033551218 scopus 로고    scopus 로고
    • Tossing monkey wrenches into the clock: New ways of treating cancer
    • Lees, J. A.; Weinberg, R. A. Tossing Monkey Wrenches into the Clock: New Ways of Treating Cancer. Proc. Natl. Acad. Sci. U.S.A. 1999, 96, 4221-4223.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 4221-4223
    • Lees, J.A.1    Weinberg, R.A.2
  • 12
    • 0027938209 scopus 로고
    • Cyclins and cancer II: Cyclin D and CDK inhibitors come of age
    • Hunter, T.; Pines, J. Cyclins and Cancer II: Cyclin D and CDK Inhibitors Come of Age. Cell 1994, 79, 573-583.
    • (1994) Cell , vol.79 , pp. 573-583
    • Hunter, T.1    Pines, J.2
  • 13
    • 0028828204 scopus 로고
    • Cyclins and cyclin-dependent kinases: Theme and variations
    • Pines, J. Cyclins and Cyclin-Dependent Kinases: Theme and Variations. Adv. Cancer Res. 1995, 55, 181-212.
    • (1995) Adv. Cancer Res. , vol.55 , pp. 181-212
    • Pines, J.1
  • 14
    • 0030657690 scopus 로고    scopus 로고
    • The restriction point and control of cell proliferation
    • Planas-Silva, M. D.; Weinberg, R. A. The Restriction Point and Control of Cell Proliferation. Curr. Opin. Cell Biol. 1997, 9, 768-772.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 768-772
    • Planas-Silva, M.D.1    Weinberg, R.A.2
  • 15
    • 0028675322 scopus 로고
    • Cyclin-dependent kinases: Regulators of the cell cycle and more
    • Murray, A. Cyclin-Dependent Kinases: Regulators of the Cell Cycle and More. Chem. Biol. 1994, 1, 191-195.
    • (1994) Chem. Biol. , vol.1 , pp. 191-195
    • Murray, A.1
  • 16
    • 0033022375 scopus 로고    scopus 로고
    • The CDK-activating kinase (CAK): From yeast to mammals
    • Kaldis, P. The CDK-Activating Kinase (CAK): From Yeast to Mammals. Cell. Mol. Life Sci. 1999, 55, 284-296.
    • (1999) Cell. Mol. Life Sci. , vol.55 , pp. 284-296
    • Kaldis, P.1
  • 17
    • 0030575534 scopus 로고    scopus 로고
    • CAK in TFIIH: Crucial connection or confounding coincidence?
    • Fisher, R. P.; Morgan, D. O. CAK in TFIIH: Crucial Connection or Confounding Coincidence? Biochim. Biophys. Acta 1996, 1288, 7-10.
    • (1996) Biochim. Biophys. Acta , vol.1288 , pp. 7-10
    • Fisher, R.P.1    Morgan, D.O.2
  • 18
    • 0027978170 scopus 로고
    • p35 is a neural-specific regulatory subunit of cyclin-dependent kinase 5
    • Tsai, L. H.; Delalle, I.; Caviness Jr., V. S.; Chae, T.; Harlow, E. p35 is a Neural-Specific Regulatory Subunit of Cyclin-Dependent Kinase 5. Nature 1994, 371, 419-423.
    • (1994) Nature , vol.371 , pp. 419-423
    • Tsai, L.H.1    Delalle, I.2    Caviness V.S., Jr.3    Chae, T.4    Harlow, E.5
  • 19
    • 0028122011 scopus 로고
    • A brain-specific activator of cyclin-dependent kinase 5
    • Lew, J.; Huang, Q. Q.; Winkfein, R. J.; Aebersold, R.; Hunt, T.; Wang, J. H.; MRC Group in Signal Transduction, University of Calgary, Alberta, Canada. A Brain-Specific Activator of Cyclin-Dependent Kinase 5. Nature 1994, 371, 423-426.
    • (1994) Nature , vol.371 , pp. 423-426
    • Lew, J.1    Huang, Q.Q.2    Winkfein, R.J.3    Aebersold, R.4    Hunt, T.5    Wang, J.H.6
  • 20
    • 0027467832 scopus 로고
    • Cyclin E and cyclin A as candidates for the restriction point protein
    • Dou, Q. P.; Levin, A. H.; Zhao, S. Z.; Pardee, A. B. Cyclin E and Cyclin A as Candidates for the Restriction Point Protein. Cancer Res. 1993, 53, 1493-1497.
    • (1993) Cancer Res. , vol.53 , pp. 1493-1497
    • Dou, Q.P.1    Levin, A.H.2    Zhao, S.Z.3    Pardee, A.B.4
  • 22
    • 0027204555 scopus 로고
    • Physical interaction of the retinoblastoma protein with human D cyclins
    • Dowdy, S. F.; Hinds, P. W.; Louie, K.; Reed, S. I.; Arnold, A.; Weinberg, R. A. Physical Interaction of the Retinoblastoma Protein with Human D Cyclins. Cell 1993, 73, 499-511.
    • (1993) Cell , vol.73 , pp. 499-511
    • Dowdy, S.F.1    Hinds, P.W.2    Louie, K.3    Reed, S.I.4    Arnold, A.5    Weinberg, R.A.6
  • 23
    • 0031844197 scopus 로고    scopus 로고
    • Defining the minimal portion of the retinoblastoma protein that serves as an efficient substrate for CDK4 kinase/cyclin D1 complex
    • Pan, W.; Sun, T.; Hoess, R.; Grafstrom, R. Defining the Minimal Portion of the Retinoblastoma Protein that Serves as an Efficient Substrate for CDK4 Kinase/Cyclin D1 Complex. Carcinogenesis 1998, 19, 765-769.
    • (1998) Carcinogenesis , vol.19 , pp. 765-769
    • Pan, W.1    Sun, T.2    Hoess, R.3    Grafstrom, R.4
  • 24
    • 0032549001 scopus 로고    scopus 로고
    • Rb interacts with histone deacetylase to repress transcription
    • Luo, R. X.; Postigo, A. A.; Dean, D. C. Rb Interacts with Histone Deacetylase to Repress Transcription. Cell 1998, 92, 463-473.
    • (1998) Cell , vol.92 , pp. 463-473
    • Luo, R.X.1    Postigo, A.A.2    Dean, D.C.3
  • 25
    • 0025905183 scopus 로고
    • The E2F transcription factor is a cellular target for the RB protein
    • Chellappan, S.; Hiebert, S.; Mudryi, M.; Horowitz, J. M.; Nevins, J. R. The E2F Transcription Factor is a Cellular Target for the RB Protein. Cell 1991, 65, 1053-1061.
    • (1991) Cell , vol.65 , pp. 1053-1061
    • Chellappan, S.1    Hiebert, S.2    Mudryi, M.3    Horowitz, J.M.4    Nevins, J.R.5
  • 26
    • 0032931991 scopus 로고    scopus 로고
    • Cumulative effect of phosphorylation of pRB on regulation of E2F activity
    • Brown, V. D.; Phillips, R. A.; Gallie, B. L. Cumulative Effect of Phosphorylation of pRB on Regulation of E2F Activity. Mol. Cell. Biol. 1999, 19, 3246-3256.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3246-3256
    • Brown, V.D.1    Phillips, R.A.2    Gallie, B.L.3
  • 27
    • 0029849620 scopus 로고    scopus 로고
    • Cancer cell cycles
    • Sherr, C. J. Cancer Cell Cycles. Science 1996, 274, 1672-1677.
    • (1996) Science , vol.274 , pp. 1672-1677
    • Sherr, C.J.1
  • 28
    • 0029125622 scopus 로고
    • Early events in DNA replication require cyclin E and are blocked by p21CIP1
    • Jackson, P. K.; Chevalier, S.; Phillippe, M.; Kirschner, M. W. Early Events in DNA Replication Require Cyclin E and are Blocked by p21CIP1. J. Cell. Biol. 1995, 130, 755-769.
    • (1995) J. Cell. Biol. , vol.130 , pp. 755-769
    • Jackson, P.K.1    Chevalier, S.2    Phillippe, M.3    Kirschner, M.W.4
  • 29
    • 0032562610 scopus 로고    scopus 로고
    • Formation of a preinitiation complex by S-phase cyclin CDK-dependent loading of Cdc45p onto chromatin
    • Zou, L.; Stillman, B. Formation of a Preinitiation Complex by S-phase Cyclin CDK-Dependent Loading of Cdc45p onto Chromatin. Science 1998, 280, 593-596.
    • (1998) Science , vol.280 , pp. 593-596
    • Zou, L.1    Stillman, B.2
  • 30
    • 0030561571 scopus 로고    scopus 로고
    • The retinoblastoma protein pathway and the restriction point
    • Bartek, J.; Bartkova, J.; Lukas, J. The Retinoblastoma Protein Pathway and the Restriction Point. Curr. Opin. Cell. Biol. 1996, 8, 5-14.
    • (1996) Curr. Opin. Cell. Biol. , vol.8 , pp. 5-14
    • Bartek, J.1    Bartkova, J.2    Lukas, J.3
  • 33
    • 0032937751 scopus 로고    scopus 로고
    • Loss of CAK4 expression causes insulin-deficient diabetes and CAK4 activation results in β-islet cell hyperplasia
    • Rane, S. G.; Dubus, P.; Mettus, R. V.; Galbreath, E. J.; Boden, G.; Reddy, E. P.; Barbacid, M. Loss of CAK4 Expression Causes Insulin-Deficient Diabetes and CAK4 Activation Results in β-Islet Cell Hyperplasia. Nat. Genet. 1999, 22, 44-52.
    • (1999) Nat. Genet. , vol.22 , pp. 44-52
    • Rane, S.G.1    Dubus, P.2    Mettus, R.V.3    Galbreath, E.J.4    Boden, G.5    Reddy, E.P.6    Barbacid, M.7
  • 34
    • 0029910364 scopus 로고    scopus 로고
    • Convergence of motigenic signaling cascades from diverse classes of receptors at the cyclin D-cyclin-dependent kinase: pRb-controlled G1 checkpoint
    • Lukas, J.; Bartkova, J.; Bartek, J. Convergence of Motigenic Signaling Cascades from Diverse Classes of Receptors at the Cyclin D-Cyclin-Dependent Kinase: pRb-Controlled G1 Checkpoint. Mol. Cell Biol. 1996, 16, 6917-6925.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 6917-6925
    • Lukas, J.1    Bartkova, J.2    Bartek, J.3
  • 35
    • 0033055061 scopus 로고    scopus 로고
    • Cyclin-dependent kinase control of centrosome duplication
    • Lacey, K.; Jackson, P. K.; Stearns, T. Cyclin-Dependent Kinase Control of Centrosome Duplication. Natl. Acad. Sci. U.S.A. 1999, 96, 2817-2822.
    • (1999) Natl. Acad. Sci. U.S.A. , vol.96 , pp. 2817-2822
    • Lacey, K.1    Jackson, P.K.2    Stearns, T.3
  • 36
    • 0030887999 scopus 로고    scopus 로고
    • Cyclin/Cdk-dependent initiation of DNA replication in a human cell-free system
    • Krude, T.; Jackman, M.; Pines, J.; Laskey, R. A. Cyclin/Cdk-Dependent Initiation of DNA Replication in a Human Cell-Free System. Cell 1997, 88, 109-119.
    • (1997) Cell , vol.88 , pp. 109-119
    • Krude, T.1    Jackman, M.2    Pines, J.3    Laskey, R.A.4
  • 37
    • 0028271690 scopus 로고
    • Protein kinase regulation: Insights from crystal structure analysis
    • Morgan, D. O.; De Bondt, H. L. Protein Kinase Regulation: Insights from Crystal Structure Analysis. Curr. Opin. Cell. Biol. 1994, 6, 239-246.
    • (1994) Curr. Opin. Cell. Biol. , vol.6 , pp. 239-246
    • Morgan, D.O.1    De Bondt, H.L.2
  • 38
    • 0030308967 scopus 로고    scopus 로고
    • Regulation of Cdc2 activity by phosphorylation at T14/Y15
    • Berry, L. D.; Gould, K. L. Regulation of Cdc2 Activity by Phosphorylation at T14/Y15. Prog. Cell. Cycle Res. 1996, 2, 99-105.
    • (1996) Prog. Cell. Cycle Res. , vol.2 , pp. 99-105
    • Berry, L.D.1    Gould, K.L.2
  • 39
    • 0032544440 scopus 로고    scopus 로고
    • Cdc2 kinase directly phosphorylates the Cis-Golgi matrix protein GM130 and is required for Golgi fragmentation in mitosis
    • Lowe, M.; Rabouille, C.; Nakamura, N.; Watsch, R.; Jackson, M.; Tamsa, E.; Rahman, D.; Pappin, D. J. C.; Warren, G. Cdc2 Kinase Directly Phosphorylates the Cis-Golgi Matrix Protein GM130 and is Required for Golgi Fragmentation in Mitosis. Cell 1998, 94, 783-793.
    • (1998) Cell , vol.94 , pp. 783-793
    • Lowe, M.1    Rabouille, C.2    Nakamura, N.3    Watsch, R.4    Jackson, M.5    Tamsa, E.6    Rahman, D.7    Pappin, D.J.C.8    Warren, G.9
  • 40
    • 0028931265 scopus 로고
    • Principles of CDK regulation
    • Morgan, D. O. Principles of CDK Regulation. Nature 1995, 375, 131-134.
    • (1995) Nature , vol.375 , pp. 131-134
    • Morgan, D.O.1
  • 42
    • 0032478177 scopus 로고    scopus 로고
    • Identification of a substrate-targeting domain in cyclin E for phosphorylation of the retinoblastoma protein
    • Kelly, B. L.; Wolfe, K. G.; Roberts, J. M. Identification of a Substrate-Targeting Domain in Cyclin E for Phosphorylation of the Retinoblastoma Protein. Proc. Natl. Acad. Sci. U.S.A. 1998, 95, 2535-2540.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 2535-2540
    • Kelly, B.L.1    Wolfe, K.G.2    Roberts, J.M.3
  • 45
    • 0028786264 scopus 로고
    • Molecular cloning of CDK7-associated human MAT1, a cyclin-dependent kinase-activating kinase (CAK) assembly factor
    • Yee, A.; Nichols, M. A.; Wu, L.; Hall, F. L.; Kobayashi, R.; Xiong, Y. Molecular Cloning of CDK7-associated Human MAT1, a Cyclin-Dependent Kinase-Activating Kinase (CAK) Assembly Factor. Cancer Res. 1995, 55, 6058-6062.
    • (1995) Cancer Res. , vol.55 , pp. 6058-6062
    • Yee, A.1    Nichols, M.A.2    Wu, L.3    Hall, F.L.4    Kobayashi, R.5    Xiong, Y.6
  • 47
    • 0030973878 scopus 로고    scopus 로고
    • New functional activities for the p21 family of CDK inhibitors
    • Fattaey, A.; Harlow, E. New Functional Activities for the p21 Family of CDK Inhibitors. Genes Dev. 1997, 11, 847-862.
    • (1997) Genes Dev. , vol.11 , pp. 847-862
    • Fattaey, A.1    Harlow, E.2
  • 50
    • 0031297716 scopus 로고    scopus 로고
    • Mytl: A weel-type kinase that phosphorylates Cdc2 on residue Thr14
    • Fattaey, A.; Booher, R. N. Mytl: A Weel-Type Kinase that Phosphorylates Cdc2 on Residue Thr14. Prog. Cell Cycle Res. 1997, 3, 233-240.
    • (1997) Prog. Cell Cycle Res. , vol.3 , pp. 233-240
    • Fattaey, A.1    Booher, R.N.2
  • 51
    • 0343742594 scopus 로고    scopus 로고
    • Cdc25 protein phosphatases in cell proliferation
    • Draetta, G.; Eckstein, J. Cdc25 Protein Phosphatases in Cell Proliferation. Biochim. Biophys. Acta 1997, 1332, M53-M63.
    • (1997) Biochim. Biophys. Acta , vol.1332
    • Draetta, G.1    Eckstein, J.2
  • 52
    • 0028575906 scopus 로고
    • The role of cdc25 in checkpoints and feedback controls in the eukaryotic cell cycle
    • Hoffman, I.; Karsenti, E. The Role of cdc25 in Checkpoints and Feedback Controls in the Eukaryotic Cell Cycle. J. Cell. Sci. Suppl. 1994, 18, 75-79.
    • (1994) J. Cell. Sci. Suppl. , vol.18 , pp. 75-79
    • Hoffman, I.1    Karsenti, E.2
  • 54
    • 0027769876 scopus 로고
    • A new regulatory motif in cell-cycle control causing specific inhibition of cyclin D/CDK4
    • Serrano, M.; Hannon, G. J.; Beach, D. A New Regulatory Motif in Cell-Cycle Control Causing Specific Inhibition of Cyclin D/CDK4. Nature 1993, 366, 704-707.
    • (1993) Nature , vol.366 , pp. 704-707
    • Serrano, M.1    Hannon, G.J.2    Beach, D.3
  • 55
    • 0032981481 scopus 로고    scopus 로고
    • ink4a inhibits both CDK4- and CDK2-associated kinase activity by reassortment of cyclin-CDK inhibitor complexes
    • ink4a Inhibits Both CDK4- and CDK2-Associated Kinase Activity by Reassortment of Cyclin-CDK Inhibitor Complexes. Mol. Cell. Biol. 1999, 19, 1981-1989.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1981-1989
    • McConnell, B.B.1    Gregory, F.J.2    Stott F, J.3    Hara, E.4    Peters, G.5
  • 56
    • 0024425887 scopus 로고
    • Checkpoints: Controls that ensure the order of cell cycle events
    • Hartwell, L. H.; Weinart, T. A. Checkpoints: Controls that Ensure the Order of Cell Cycle Events. Science 1989, 246, 629-634.
    • (1989) Science , vol.246 , pp. 629-634
    • Hartwell, L.H.1    Weinart, T.A.2
  • 57
    • 0030612164 scopus 로고    scopus 로고
    • Control of the G1/S transition
    • Reed, S. I. Control of the G1/S Transition. Cancer Surv. 1997, 29, 7-23.
    • (1997) Cancer Surv. , vol.29 , pp. 7-23
    • Reed, S.I.1
  • 58
    • 0030308959 scopus 로고    scopus 로고
    • Tyrosine kinases weel and Mik1 as effectors of DNA replication checkpoint control
    • Tourret, J.; McKeon, F. Tyrosine Kinases Weel and Mik1 as Effectors of DNA Replication Checkpoint Control. Prog. Cell Cycle Res. 1996, 2, 91-97.
    • (1996) Prog. Cell Cycle Res. , vol.2 , pp. 91-97
    • Tourret, J.1    McKeon, F.2
  • 59
    • 0032496322 scopus 로고    scopus 로고
    • Replication checkpoint enforced by kinases Cds1 and Chk1
    • Boddy, M. N.; Furnari, B.; Mondesert, O.; Russell, P. Replication Checkpoint Enforced by Kinases Cds1 and Chk1. Science 1998, 280, 909-912.
    • (1998) Science , vol.280 , pp. 909-912
    • Boddy, M.N.1    Furnari, B.2    Mondesert, O.3    Russell, P.4
  • 60
    • 0032483576 scopus 로고    scopus 로고
    • The DNA replication and damage checkpoint pathways induce transcription by inhibition of the Crtl repressor
    • Huang, M.; Zhou, Z.; Elledge, S. J. The DNA Replication and Damage Checkpoint Pathways Induce Transcription by Inhibition of the Crtl Repressor. Cell 1998, 94, 595-605.
    • (1998) Cell , vol.94 , pp. 595-605
    • Huang, M.1    Zhou, Z.2    Elledge, S.J.3
  • 61
    • 0032190082 scopus 로고    scopus 로고
    • Replication of checkpoint requires phosphorylation of the phosphates Cdc25 by Cds1 or Chk1
    • Zeng, Y.; Forbes, K. C.; Wu, Z.; Moreno, S.; Piwnica-Worms, H.; Enoch, T. Replication of Checkpoint Requires Phosphorylation of the Phosphates Cdc25 by Cds1 or Chk1. Nature 1998, 395, 507-510.
    • (1998) Nature , vol.395 , pp. 507-510
    • Zeng, Y.1    Forbes, K.C.2    Wu, Z.3    Moreno, S.4    Piwnica-Worms, H.5    Enoch, T.6
  • 62
    • 0032996507 scopus 로고    scopus 로고
    • The spindle checkpoint
    • Amon, A. The Spindle Checkpoint. Curr. Opin. Genet. Dev. 1999, 9, 69-75.
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , pp. 69-75
    • Amon, A.1
  • 63
    • 0031600105 scopus 로고    scopus 로고
    • The spindle checkpoint
    • Hardwick, K. G. The Spindle Checkpoint. Trends Genet. 1998, 14, 1-4.
    • (1998) Trends Genet. , vol.14 , pp. 1-4
    • Hardwick, K.G.1
  • 64
    • 0032432556 scopus 로고    scopus 로고
    • Cyclin-dependent kinase inhibitors in restriction point control, genomic stability and tumorigenesis
    • Millard, S. S.; Koff, A. Cyclin-Dependent Kinase Inhibitors in Restriction Point Control, Genomic Stability and Tumorigenesis. J. Cell. Biochem. Suppl. 1998, 30, 37-42.
    • (1998) J. Cell. Biochem. Suppl. , vol.30 , pp. 37-42
    • Millard, S.S.1    Koff, A.2
  • 65
    • 0030434824 scopus 로고    scopus 로고
    • Cell cycle and cancer: Critical events at the G1 restriction point
    • DelSal, G.; Loda, M.; Pagano, M. Cell Cycle and Cancer: Critical Events at the G1 Restriction Point. Crit. Rev. Oncogene 1996, 7, 127-142.
    • (1996) Crit. Rev. Oncogene , vol.7 , pp. 127-142
    • DelSal, G.1    Loda, M.2    Pagano, M.3
  • 66
    • 0029849620 scopus 로고    scopus 로고
    • Cancer cell cycles
    • Sherr, C. J. Cancer Cell Cycles. Science 1996, 274, 1672-1677.
    • (1996) Science , vol.274 , pp. 1672-1677
    • Sherr, C.J.1
  • 67
    • 0028568315 scopus 로고
    • Cell cycle control and cancer
    • Hartwell, L. H.; Kastan, M. B. Cell Cycle Control and Cancer. Science 1994, 266, 1821-1828.
    • (1994) Science , vol.266 , pp. 1821-1828
    • Hartwell, L.H.1    Kastan, M.B.2
  • 68
    • 0029921317 scopus 로고    scopus 로고
    • Genetic alterations of cyclins, cyclin-dependent kinases, and Cdk inhibitors in human cancer
    • Hall, M.; Peters, G. Genetic Alterations of Cyclins, Cyclin-Dependent Kinases, and Cdk Inhibitors in Human Cancer. Adv. Cancer Res. 1996, 56, 67-108.
    • (1996) Adv. Cancer Res. , vol.56 , pp. 67-108
    • Hall, M.1    Peters, G.2
  • 69
    • 0027178335 scopus 로고
    • Cell death and the cell cycle: A relationship between transformation and neurodegeneration?
    • Heintz, N. Cell Death and the Cell Cycle: A Relationship Between Transformation and Neurodegeneration? Trends Biochem. Sci. 1993, 18, 157-159.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 157-159
    • Heintz, N.1
  • 70
    • 0031593598 scopus 로고    scopus 로고
    • Aberrancies in signal transduction and cell cycle related events in Alzheimer's disease
    • Arendt, T.; Holzer, M.; Gartner, U.; Bruckner, M. K. Aberrancies in Signal Transduction and Cell Cycle Related Events in Alzheimer's Disease. J. Neural Transm. Suppl. 1998, 54, 147-158.
    • (1998) J. Neural Transm. Suppl. , vol.54 , pp. 147-158
    • Arendt, T.1    Holzer, M.2    Gartner, U.3    Bruckner, M.K.4
  • 71
    • 0032548918 scopus 로고    scopus 로고
    • A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA
    • Wei, P.; Garber, M. E.; Fang, S.; Fischer, W. H.; Jones, K. A. A Novel CDK9-Associated C-Type Cyclin Interacts Directly with HIV-1 Tat and Mediates Its High-Affinity, Loop-Specific Binding to TAR RNA. Cell 1998, 92, 451-462.
    • (1998) Cell , vol.92 , pp. 451-462
    • Wei, P.1    Garber, M.E.2    Fang, S.3    Fischer, W.H.4    Jones, K.A.5
  • 72
    • 0030561611 scopus 로고    scopus 로고
    • The dynamics of cyclin dependent kinase structure
    • Morgan, D. O. The Dynamics of Cyclin Dependent Kinase Structure. Curr. Opin. Cell Biol. 1996, 8, 767-772.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 767-772
    • Morgan, D.O.1
  • 73
    • 0000863502 scopus 로고    scopus 로고
    • Structure-based inhibitor design for CDK2, a cell cycle controlling protein kinase
    • Kim, S.-H. Structure-based Inhibitor Design for CDK2, a Cell Cycle Controlling Protein Kinase. Pure Appl. Chem. 1998, 70, 555-565.
    • (1998) Pure Appl. Chem. , vol.70 , pp. 555-565
    • Kim, S.-H.1
  • 76
    • 0030753686 scopus 로고    scopus 로고
    • Chemical inhibitors of cyclin-dependent kinases
    • Meijer, L.; Kim, S. H. Chemical Inhibitors of Cyclin-Dependent Kinases. Methods Enzymol. 1997, 283, 113-128.
    • (1997) Methods Enzymol. , vol.283 , pp. 113-128
    • Meijer, L.1    Kim, S.H.2
  • 77
    • 0029786705 scopus 로고    scopus 로고
    • Purification and crystallization of cyclin-dependent kinase inhibitor p21
    • Mayrose, D. R.; Nichols, M. A.; Xiong, Y.; Ke, H. Purification and Crystallization of Cyclin-dependent Kinase Inhibitor p21. Protein Sci. 1996, 5, 1928-1930.
    • (1996) Protein Sci. , vol.5 , pp. 1928-1930
    • Mayrose, D.R.1    Nichols, M.A.2    Xiong, Y.3    Ke, H.4
  • 80
    • 0032893263 scopus 로고    scopus 로고
    • SU5416 is a potent and selective inhibitor of the vascular endothelial growth factor receptor (Flk-1/KDR) that inhibits tyrosine kinase catalysis, tumor vascularization, and growth of multiple tumor types
    • Fong, T. A. T.; Shawver, L. K.; Sun, L.; Tang, C.; App, H.; Powell, T. J.; Kim, Y. H.; Schreck, R.; Wang, X.; Risau, W.; Ullrich, A.; Hirth, K. P.; McMahon, G. SU5416 is a Potent and Selective Inhibitor of the Vascular Endothelial Growth Factor Receptor (Flk-1/KDR) that Inhibits Tyrosine Kinase Catalysis, Tumor Vascularization, and Growth of Multiple Tumor Types. Cancer Res. 1999, 59, 99-106.
    • (1999) Cancer Res. , vol.59 , pp. 99-106
    • Fong, T.A.T.1    Shawver, L.K.2    Sun, L.3    Tang, C.4    App, H.5    Powell, T.J.6    Kim, Y.H.7    Schreck, R.8    Wang, X.9    Risau, W.10    Ullrich, A.11    Hirth, K.P.12    McMahon, G.13
  • 81
    • 0342740218 scopus 로고    scopus 로고
    • R&D Focus 1997, Dec 15.
    • (1997) R&D Focus , vol.DEC 15
  • 82
    • 0031745021 scopus 로고    scopus 로고
    • Inhibitors of the epidermal growth factor receptor protein tyrosine kinase. A quantitative structure-activity relationship analysis
    • Singh, P.; Kumar, R. Inhibitors of the Epidermal Growth Factor Receptor Protein Tyrosine Kinase. A Quantitative Structure-Activity Relationship Analysis. J. Enzyme Inhib. 1998, 13, 125-134.
    • (1998) J. Enzyme Inhib. , vol.13 , pp. 125-134
    • Singh, P.1    Kumar, R.2
  • 84
    • 0030773557 scopus 로고    scopus 로고
    • Tyrosine kinase inhibitors. 13. Structure-activity relationships for soluble 7-substituted 4-[(3-bromophenyl)amino]pyrido[4,3-d]pyrimidines designed as inhibitors of the tyrosine kinase activity of the epidermal growth factor receptor
    • Thompson, A. M.; Murray, D. K.; Elliott, W. L.; Fry, D. W.; Nelson, J. A.; Showalter, H. D. Hollis; Roberts, B. J.; Vincent, P. W.; Denny, W. A. Tyrosine Kinase Inhibitors. 13. Structure-Activity Relationships for Soluble 7-Substituted 4-[(3-Bromophenyl)amino]pyrido[4,3-d]pyrimidines Designed as Inhibitors of the Tyrosine Kinase Activity of the Epidermal Growth Factor Receptor. J. Med. Chem. 1997, 40, 3915-3925.
    • (1997) J. Med. Chem. , vol.40 , pp. 3915-3925
    • Thompson, A.M.1    Murray, D.K.2    Elliott, W.L.3    Fry, D.W.4    Nelson, J.A.5    Showalter, H.D.H.6    Roberts, B.J.7    Vincent, P.W.8    Denny, W.A.9
  • 85
    • 0013364640 scopus 로고    scopus 로고
    • A short and unequivocal synthesis of 5-aminotetrazolo[1,5-a]quinazoline as a tricyclic analogue of 4-(3-bromoanilino)-6,7-dimethoxyquinazoline (PD 153035)
    • Bencteux, E.; Houssin, R.; Henichart, J. A short and Unequivocal Synthesis of 5-Aminotetrazolo[1,5-a]quinazoline as a Tricyclic Analogue of 4-(3-Bromoanilino)-6,7-dimethoxyquinazoline (PD 153035). J. Heterocycl. Chem. 1997, 34, 1375-1378.
    • (1997) J. Heterocycl. Chem. , vol.34 , pp. 1375-1378
    • Bencteux, E.1    Houssin, R.2    Henichart, J.3
  • 87
  • 88
    • 13344262678 scopus 로고    scopus 로고
    • Tyrosine kinase inhibitors. 9. Synthesis and evaluation of fused tricyclic quinazoline analogues as ATP site inhibitors of the tyrosine kinase activity of the epidermal growth factor receptor
    • Newcastle, G. W.; Palmer, B. D.; Bridges, A. J.; Showalter, H. D. H.; Sun, L.; Nelson, J.; McMichael, A.; Kraker, A. J.; Fry, D. W.; Denny, W. A. Tyrosine Kinase Inhibitors. 9. Synthesis and Evaluation of Fused Tricyclic Quinazoline Analogues as ATP Site Inhibitors of the Tyrosine Kinase Activity of the Epidermal Growth Factor Receptor. J. Med. Chem. 1996, 39, 918-928.
    • (1996) J. Med. Chem. , vol.39 , pp. 918-928
    • Newcastle, G.W.1    Palmer, B.D.2    Bridges, A.J.3    Showalter, H.D.H.4    Sun, L.5    Nelson, J.6    McMichael, A.7    Kraker, A.J.8    Fry, D.W.9    Denny, W.A.10
  • 89
    • 0342305120 scopus 로고    scopus 로고
    • R&D Focus 1997, Aug 11.
    • (1997) R&D Focus , vol.AUG 11
  • 90
    • 0020417379 scopus 로고
    • The crystal and molecular structure of staurosporine, a new alkaloid from a streptomyces strain
    • Furusaki, A.; Hashiba, N.; Matsumoto, T.; Hirano, A.; Iwai, Y.; Omura, S. The Crystal and Molecular Structure of Staurosporine, a New Alkaloid from a Streptomyces Strain. Bull. Chem. Soc. Jpn. 1982, 55, 3681-3685.
    • (1982) Bull. Chem. Soc. Jpn. , vol.55 , pp. 3681-3685
    • Furusaki, A.1    Hashiba, N.2    Matsumoto, T.3    Hirano, A.4    Iwai, Y.5    Omura, S.6
  • 91
    • 0030271304 scopus 로고    scopus 로고
    • Chemical inhibitors of cyclin-dependent kinases
    • Meijer, L. Chemical Inhibitors of Cyclin-Dependent Kinases. Trends Cell. Biol. 1996, 6, 393-397.
    • (1996) Trends Cell. Biol. , vol.6 , pp. 393-397
    • Meijer, L.1
  • 93
    • 0029417882 scopus 로고
    • Chemical inhibitors of cyclin-dependent kinases
    • Meijer, L., Guidet, S., Tung, H. Y. L., Eds.; Plenum Press: New York
    • Meijer, L. Chemical Inhibitors of Cyclin-Dependent Kinases. In Progress in Cell Cycle Research; Meijer, L., Guidet, S., Tung, H. Y. L., Eds.; Plenum Press: New York, 1995; Vol. 1, pp 351-361.
    • (1995) Progress in Cell Cycle Research , vol.1 , pp. 351-361
    • Meijer, L.1
  • 94
    • 0031253655 scopus 로고    scopus 로고
    • Protein kinase inhibition by staurosporine revealed in details of the molecular interaction with CDK2
    • Lawrie, A. M.; Noble, M. E. M.; Tunnah, P.; Brown, N. R.; Johnson, L. N.; Endicott, J. A. Protein Kinase Inhibition by Staurosporine Revealed in Details of the Molecular Interaction with CDK2. Nat. Struct. Biol. 1997, 4, 796-801.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 796-801
    • Lawrie, A.M.1    Noble, M.E.M.2    Tunnah, P.3    Brown, N.R.4    Johnson, L.N.5    Endicott, J.A.6
  • 96
    • 84982078104 scopus 로고
    • Protein kinase C inhibitor as a potent inhibitor of accelerated repopulation during radiotherapy: I. Growth inhibitory, cytotoxic, and indirect radiosensitizing effects of a staurosporine derivative (UCN-01) in vitro
    • Urano, M.; Reynolds, R.; Begley, J. Protein kinase C Inhibitor as a Potent Inhibitor of Accelerated Repopulation During Radiotherapy: I. Growth Inhibitory, Cytotoxic, and Indirect Radiosensitizing Effects of a Staurosporine Derivative (UCN-01) In Vitro. Radiat. Oncol. Invest. 1995, 3, 64-71.
    • (1995) Radiat. Oncol. Invest. , vol.3 , pp. 64-71
    • Urano, M.1    Reynolds, R.2    Begley, J.3
  • 98
    • 0027232037 scopus 로고
    • Enhancement of antitumor activity of mitomycin C in vitro and in vivo by UCN-01, a selective inhibitor of protein kinase C
    • Akinaga, S.; Nomura, K.; Gomi, K.; Okabe, M. Enhancement of Antitumor Activity of Mitomycin C In Vitro and In Vivo by UCN-01, a Selective Inhibitor of Protein Kinase C. Cancer Chemother. Pharmacol. 1993, 32, 183-189.
    • (1993) Cancer Chemother. Pharmacol. , vol.32 , pp. 183-189
    • Akinaga, S.1    Nomura, K.2    Gomi, K.3    Okabe, M.4
  • 99
    • 0027157590 scopus 로고
    • Cell cycle arrest and growth inhibition by the protein kinase antagonist UCN-01 in human breast carcinoma
    • Seynaeve, C. M.; Stetler, S. M.; Sebers, S.; Kaur, G.; Sausville, E. A.; Worland, P. J. Cell Cycle Arrest and Growth Inhibition by the Protein Kinase Antagonist UCN-01 in Human Breast Carcinoma. Cancer Res. 1993, 53, 2081-2086.
    • (1993) Cancer Res. , vol.53 , pp. 2081-2086
    • Seynaeve, C.M.1    Stetler, S.M.2    Sebers, S.3    Kaur, G.4    Sausville, E.A.5    Worland, P.J.6
  • 100
    • 0001231055 scopus 로고    scopus 로고
    • 7-Hydroxystaurosporine (UCN-01), a selective inhibitor of protein kinase C, blocks malignant glioma growth by inducing apoptosis independent of p53 and in a time-dependent manner
    • Bredel, M.; Pollack, I. F.; Freund, J. M.; Rusnak, J.; Lazo, J. S. 7-Hydroxystaurosporine (UCN-01), a Selective Inhibitor of Protein Kinase C, Blocks Malignant Glioma Growth by Inducing Apoptosis Independent of p53 and in a Time-Dependent manner. Proc. Am. Assoc. Cancer Res. 1997, 38, 500.
    • (1997) Proc. Am. Assoc. Cancer Res. , vol.38 , pp. 500
    • Bredel, M.1    Pollack, I.F.2    Freund, J.M.3    Rusnak, J.4    Lazo, J.S.5
  • 101
    • 0001627298 scopus 로고    scopus 로고
    • The protein kinase C (PKC) inhibitors UCN-01 and flavopiridol (FLAVO) significantly enhance the cytotoxic effect of chemotherapy by promoting apoptosis in gastric and breast cancer cells
    • Schwartz, G. K.; Farsi, K.; Danso, D.; Dhupar, S. K.; Kelsen, D.; Spriggs, D. The Protein Kinase C (PKC) Inhibitors UCN-01 and Flavopiridol (FLAVO) Significantly Enhance the Cytotoxic Effect of Chemotherapy by Promoting Apoptosis in Gastric and Breast Cancer Cells. Proc. ASCO 1996, 15, 501.
    • (1996) Proc. ASCO , vol.15 , pp. 501
    • Schwartz, G.K.1    Farsi, K.2    Danso, D.3    Dhupar, S.K.4    Kelsen, D.5    Spriggs, D.6
  • 102
    • 0000314933 scopus 로고    scopus 로고
    • Staurosporine and ent-staurosporine: The first total syntheses, prospects for a regioselective approach, and activity profiles
    • Link, J. T.; Raghavan, S.; Gallant, M.; Danishefsky, S. J.; Chou, T. C.; Ballas, L. M. Staurosporine and ent-Staurosporine: The First Total Syntheses, Prospects for a Regioselective Approach, and Activity Profiles. J. Am. Chem. Soc. 1996, 118, 2825-2842.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 2825-2842
    • Link, J.T.1    Raghavan, S.2    Gallant, M.3    Danishefsky, S.J.4    Chou, T.C.5    Ballas, L.M.6
  • 103
    • 0000714445 scopus 로고    scopus 로고
    • Structure-activity relationships in a series of substituted indolocarbazoles: Topoisomerase I and protein kinase C inhibition and antitumoral and antimicrobial properties
    • Pereira, E. R.; Belin, L.; Sancelme, M.; Prudhomme, M.; Oilier, M.; Rapp, M.; Severe, D.; Riou, J.-F.; Fabbro, D.; Meyer, T. Structure-Activity Relationships in a Series of Substituted Indolocarbazoles: Topoisomerase I and Protein Kinase C Inhibition and Antitumoral and Antimicrobial Properties. J. Med. Chem. 1996, 39, 4471-4477.
    • (1996) J. Med. Chem. , vol.39 , pp. 4471-4477
    • Pereira, E.R.1    Belin, L.2    Sancelme, M.3    Prudhomme, M.4    Oilier, M.5    Rapp, M.6    Severe, D.7    Riou, J.-F.8    Fabbro, D.9    Meyer, T.10
  • 104
    • 0030665684 scopus 로고    scopus 로고
    • Design and implementation of an efficient synthetic approach to pyranosylated indolocarbazoles: Total synthesis of (+)-RK286c, (+)-MLR-52, (+)-staurosporine, and (-)-TAN-1030a
    • Wood, J. L.; Stoltz, B. M.; Goodman, S. N.; Onwueme, K. Design and Implementation of an Efficient Synthetic Approach to Pyranosylated Indolocarbazoles: Total Synthesis of (+)-RK286c, (+)-MLR-52, (+)-Staurosporine, and (-)-TAN-1030a. J. Am. Chem. Soc. 1997, 119, 9652-9661.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 9652-9661
    • Wood, J.L.1    Stoltz, B.M.2    Goodman, S.N.3    Onwueme, K.4
  • 105
    • 0030574007 scopus 로고    scopus 로고
    • The synthesis of desamido analogues of staurosporine, RK-286c, and TAN-1030a
    • Wood, J. L.; Stoltz, B. M.; Onwueme, K.; Goodman, S. N. The Synthesis of Desamido Analogues of Staurosporine, RK-286c, and TAN-1030a. Tetrahedron Lett. 1996, 37, 7335-7338.
    • (1996) Tetrahedron Lett. , vol.37 , pp. 7335-7338
    • Wood, J.L.1    Stoltz, B.M.2    Onwueme, K.3    Goodman, S.N.4
  • 106
    • 0029841520 scopus 로고    scopus 로고
    • Total synthesis of (+)-RK-286c, (+)-MLR-52, (+)-staurosporine, and (+)-K252a
    • Wood, L.; Stoltz, B. M.; Goodman, S. N. Total Synthesis of (+)-RK-286c, (+)-MLR-52, (+)-Staurosporine, and (+)-K252a. J. Am. Chem. Soc. 1996, 118, 10656-10657.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 10656-10657
    • Wood, L.1    Stoltz, B.M.2    Goodman, S.N.3
  • 108
    • 85038052790 scopus 로고    scopus 로고
    • NCI PDG Clinical Trial Search, November 1997
    • NCI PDG Clinical Trial Search, November 1997.
  • 109
    • 0342305087 scopus 로고    scopus 로고
    • R&D Drug News 1998, Jan 19.
    • (1998) R&D Drug News , vol.JAN 19
  • 111
    • 85038060180 scopus 로고    scopus 로고
    • Preparation of Analogues of Chromones as Inhibitors of Cyclin-Dependent Kinases. PCT Int. Appl. WO 9716447 A1 970509
    • Mansuri, M. M.; Murthi, K. K.; Pal, K. Preparation of Analogues of Chromones as Inhibitors of Cyclin-Dependent Kinases. PCT Int. Appl. WO 9716447 A1 970509.
    • Mansuri, M.M.1    Murthi, K.K.2    Pal, K.3
  • 113
    • 0029665778 scopus 로고    scopus 로고
    • Flavopiridol induces G1 arrest with inhibition of cyclin-dependent kinase CDK2 and CDK4 in human breast carcinoma cells
    • Carlson, B. A.; Dubay, M. M.; Sausville, E. A.; Brizuela, L.; Worland, P. J. Flavopiridol Induces G1 Arrest with Inhibition of Cyclin-Dependent Kinase CDK2 and CDK4 in Human Breast Carcinoma Cells. Cancer Res. 1996, 56, 2973-2978.
    • (1996) Cancer Res. , vol.56 , pp. 2973-2978
    • Carlson, B.A.1    Dubay, M.M.2    Sausville, E.A.3    Brizuela, L.4    Worland, P.J.5
  • 115
    • 0342740169 scopus 로고    scopus 로고
    • The protein kinase C (PKC) inhibitor flavopiridol (FLAVO) significantly enhances the cytotoxic effect of chemotherapy by promoting apoptosis in gastric cancer cells
    • Schwartz, G. K.; Farsi, D.; Greaney, C.; Werner, J.; Kelsen, D. K. The protein Kinase C (PKC) Inhibitor Flavopiridol (FLAVO) Significantly Enhances the Cytotoxic Effect of Chemotherapy by Promoting Apoptosis in Gastric Cancer Cells. Prog. Gastric Res. 1997, 1, 627-629.
    • (1997) Prog. Gastric Res. , vol.1 , pp. 627-629
    • Schwartz, G.K.1    Farsi, D.2    Greaney, C.3    Werner, J.4    Kelsen, D.K.5
  • 118
    • 85038058646 scopus 로고    scopus 로고
    • The protein kinase C (PKC) inhibitor flavopiridol (FLAVO) significantly enhances the cytotoxic effect of chemotherapy by promoting apoptosis in gastric cancer cells
    • Munich, Germany, Apr 27-30
    • Schwartz, G. K.; Farsi, D.; Greaney, C.; Werner, J.; Kelsen, D. K. The Protein Kinase C (PKC) Inhibitor Flavopiridol (FLAVO) Significantly Enhances the Cytotoxic Effect of Chemotherapy by Promoting Apoptosis in Gastric Cancer Cells. 2nd International Gastric Cancer Congress, Munich, Germany, Apr 27-30, 1997; pp 627-629.
    • (1997) 2nd International Gastric Cancer Congress , pp. 627-629
    • Schwartz, G.K.1    Farsi, D.2    Greaney, C.3    Werner, J.4    Kelsen, D.K.5
  • 119
    • 0030812207 scopus 로고    scopus 로고
    • Cytotoxic synergy between flavopiridol (NSC 649890, L86-8275) and various antineoplastic agents: The importance of sequence of administration
    • Bible, K. C.; Kaufmann, S. H. Cytotoxic Synergy Between Flavopiridol (NSC 649890, L86-8275) and Various Antineoplastic Agents: the Importance of Sequence of Administration. Cancer Res. 1997, 57, 3375-3380.
    • (1997) Cancer Res. , vol.57 , pp. 3375-3380
    • Bible, K.C.1    Kaufmann, S.H.2
  • 122
    • 85038071437 scopus 로고    scopus 로고
    • Preparation of 2-Thia-or 2-Oxa-flavopiridol Analogues for use as Protein Kinase Inhibitors. PCT Int. Appl. WO 9742949
    • Kim, K. Preparation of 2-Thia-or 2-Oxa-flavopiridol Analogues for use as Protein Kinase Inhibitors. PCT Int. Appl. WO 9742949.
    • Kim, K.1
  • 124
    • 0027948283 scopus 로고
    • Olomoucine, an inhibitor of the CDC2/CDK2 kinases activity, blocks plant cells at the G1 to S and G2 to M cell cycle transitions
    • Glab, N.; Labidi, N. H.; Qin, L. X.; Trehin, C.; Bergounioux, C.; Meijer, L. Olomoucine, an Inhibitor of the CDC2/CDK2 Kinases Activity, Blocks Plant Cells at the G1 to S and G2 to M Cell Cycle Transitions. FEES Lett. 1994, 353, 207-211.
    • (1994) FEES Lett. , vol.353 , pp. 207-211
    • Glab, N.1    Labidi, N.H.2    Qin, L.X.3    Trehin, C.4    Bergounioux, C.5    Meijer, L.6
  • 126
    • 0029116545 scopus 로고
    • Inactivation of CDC2 increases the level of apoptosis induced by DNA damage
    • Ongkeko, W.; Fergusson, J. P.; Harris, A. L.; Norbury, J. Inactivation of CDC2 Increases the Level of Apoptosis Induced by DNA Damage. J. Cell Sci. 1995, 108, 2897-2904.
    • (1995) J. Cell Sci. , vol.108 , pp. 2897-2904
    • Ongkeko, W.1    Fergusson, J.P.2    Harris, A.L.3    Norbury, J.4
  • 128
    • 0031028163 scopus 로고    scopus 로고
    • Inhibition of cyclin-dependent kinases by purine analogues-crystal structure of human CDK2 complexed with roscovitine
    • Deazevedo, W. F.; Leclerc, S.; Meijer, L.; Havlicek, L.; Strand, M.; Kim, S. H. Inhibition of Cyclin-Dependent Kinases by Purine Analogues-Crystal Structure of Human CDK2 Complexed with Roscovitine. Eur. J. Biochem. 1997, 243, 518-526.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 518-526
    • Deazevedo, W.F.1    Leclerc, S.2    Meijer, L.3    Havlicek, L.4    Strand, M.5    Kim, S.H.6
  • 129
    • 0029090514 scopus 로고
    • Multiple modes of ligand recognition: Crystal structures of cyclin-dependent protein kinase 2 in complex with ATP and two inhibitors, olomoucine and isopentenyladenine
    • Schulze-Gahmen, U.; Brandsen, J.; Jones, H. D.; Morgan, D. O.; Meijer, L.; Vesely, J.; Kim, S. H. Multiple Modes of Ligand Recognition: Crystal Structures of Cyclin-Dependent Protein Kinase 2 in Complex with ATP and Two Inhibitors, Olomoucine and Isopentenyladenine. Proteins: Struct. Funct. Genet. 1995, 22, 378-391.
    • (1995) Proteins: Struct. Funct. Genet. , vol.22 , pp. 378-391
    • Schulze-Gahmen, U.1    Brandsen, J.2    Jones, H.D.3    Morgan, D.O.4    Meijer, L.5    Vesely, J.6    Kim, S.H.7
  • 134
    • 85038053502 scopus 로고    scopus 로고
    • Preparation of Purine Inhibitors of Cyclin Dependent Kinase 2 and IkB-a Kinase for use as Antitumor, Antiproliferative, and Leukemia Inhibiting Agents. PCT Int. Appl. WO 9805335 A1 980212
    • Lum, R. T.; Blum, C. L.; Mackman, R.; Wick, M. M.; Schow, S. R. Preparation of Purine Inhibitors of Cyclin Dependent Kinase 2 and IkB-a Kinase for use as Antitumor, Antiproliferative, and Leukemia Inhibiting Agents. PCT Int. Appl. WO 9805335 A1 980212.
    • Lum, R.T.1    Blum, C.L.2    Mackman, R.3    Wick, M.M.4    Schow, S.R.5
  • 136
    • 0032492705 scopus 로고    scopus 로고
    • Synthesis of C2 alkynylated purines, a new family of potent inhibitors of cyclin-dependent kinases
    • Legraverend, M.; Ludwig, O.; Bisagni, E.; Leclerc, S.; Merijer, L. Synthesis of C2 Alkynylated Purines, a New Family of Potent Inhibitors of Cyclin-Dependent Kinases. Bioorg. Med. Chem. Lett. 1998, 8, 793-798.
    • (1998) Bioorg. Med. Chem. Lett. , vol.8 , pp. 793-798
    • Legraverend, M.1    Ludwig, O.2    Bisagni, E.3    Leclerc, S.4    Merijer, L.5
  • 139
    • 85038063198 scopus 로고    scopus 로고
    • Substituted Oxindole Derivatives as Protein Tyrosine Kinase and as Protein Serine/Threonine Kinase Inhibitors. PCT Int. Appl. W09915500 A1 990401
    • Davis, S. T.; Dickerson, S. H.; Frye, S. V.; Harris, P. A. Substituted Oxindole Derivatives as Protein Tyrosine Kinase and as Protein Serine/Threonine Kinase Inhibitors. PCT Int. Appl. W09915500 A1 990401.
    • Davis, S.T.1    Dickerson, S.H.2    Frye, S.V.3    Harris, P.A.4
  • 141
    • 85038061905 scopus 로고    scopus 로고
    • Preparation of Arylmethyleneazaoxindoles as Protein Kinase Inhibitors. PCT Int. Appl. W09921859 A1 990506
    • Cheung, M.; Glennon, K. C.; Lackey, K. E.; Peel, M. R. Preparation of Arylmethyleneazaoxindoles as Protein Kinase Inhibitors. PCT Int. Appl. W09921859 A1 990506.
    • Cheung, M.1    Glennon, K.C.2    Lackey, K.E.3    Peel, M.R.4
  • 142
    • 85038068939 scopus 로고    scopus 로고
    • Use of Pyrazolo [3,4-b] Pyridine as Cyclin Dependent Kinase Inhibitors. PCT Int. Appl. WO9930710 A1 990624
    • Misra, R. N.; Kimball, S. D.; Rawlins, D. B.; Webster, K. R.; Bursuker, I. Use of Pyrazolo [3,4-b] Pyridine as Cyclin Dependent Kinase Inhibitors. PCT Int. Appl. WO9930710 A1 990624.
    • Misra, R.N.1    Kimball, S.D.2    Rawlins, D.B.3    Webster, K.R.4    Bursuker, I.5
  • 145
    • 85038051765 scopus 로고    scopus 로고
    • Preparation of Pyrido[2,3-d]pyrimidines and 4-Aminopyrimidines as Inhibitors of Cellular Proliferation. PCT Int. Appl. WO 9833798 A2 980806
    • Boschelli, D. H.; Dobrusin, E. M.; Doherty, A. M.; Fattacy, A.; Fry, D. W.; Barvian, M. R.; Kallmeyer, S. T.; Wu, Z. Preparation of Pyrido[2,3-d]pyrimidines and 4-Aminopyrimidines as Inhibitors of Cellular Proliferation. PCT Int. Appl. WO 9833798 A2 980806.
    • Boschelli, D.H.1    Dobrusin, E.M.2    Doherty, A.M.3    Fattacy, A.4    Fry, D.W.5    Barvian, M.R.6    Kallmeyer, S.T.7    Wu, Z.8
  • 149
    • 0028290821 scopus 로고
    • Inhibition of cell cycle oscillation of DNA replication by a selective inhibitor of the CDC2 kinase family, butyrolactone I, in xenopus egg extracts
    • Someya, A.; Tanaka, N.; Okuyama, A. Inhibition of Cell Cycle Oscillation of DNA Replication by a Selective Inhibitor of the CDC2 Kinase Family, Butyrolactone I, in Xenopus Egg Extracts. Biochem. Biophys. Res. Commun. 1994, 198, 536-545.
    • (1994) Biochem. Biophys. Res. Commun. , vol.198 , pp. 536-545
    • Someya, A.1    Tanaka, N.2    Okuyama, A.3
  • 152
    • 0030057602 scopus 로고    scopus 로고
    • Initial triggering of M phase in starfish oocytes: A possible novel component of maturation-promoting factor besides CDC2 kinase
    • Okumura, E.; Sekiai, T.; Hisanaga, S.; Tachibana, K.; Kishimoto, T. Initial Triggering of M Phase in Starfish Oocytes: A Possible Novel Component of Maturation-Promoting Factor Besides CDC2 Kinase. J. Cell. Biol. 1996, 732, 125-135.
    • (1996) J. Cell. Biol. , vol.732 , pp. 125-135
    • Okumura, E.1    Sekiai, T.2    Hisanaga, S.3    Tachibana, K.4    Kishimoto, T.5
  • 153
    • 0033614949 scopus 로고    scopus 로고
    • Paullones, a series of cyclin-dependent kinase inhibitors: Synthesis, evaluation of CDK1/cyclin B inhibition, and in vitro antitumor activity
    • Schultz, C.; Link, A.; Leost, M.; Zaharevitz, D. W.; Gussio, R.; Sausville, E. A.; Meijer, L.; Kunick, C. Paullones, a Series of Cyclin-Dependent Kinase Inhibitors: Synthesis, Evaluation of CDK1/Cyclin B Inhibition, and in Vitro Antitumor Activity. J. Med. Chem. 1999, 42, 2909-2919.
    • (1999) J. Med. Chem. , vol.42 , pp. 2909-2919
    • Schultz, C.1    Link, A.2    Leost, M.3    Zaharevitz, D.W.4    Gussio, R.5    Sausville, E.A.6    Meijer, L.7    Kunick, C.8
  • 154
    • 0031555861 scopus 로고    scopus 로고
    • Butyrate stimulates cyclin D and p21 and inhibits cyclin-dependent kinase 2 expression in HT-29 colonic epithelial cells
    • Siavoshian, S.; Blottiere, H. M.; Cherbut, C.; Galmiche, J.-P. Butyrate Stimulates Cyclin D and p21 and Inhibits Cyclin-Dependent Kinase 2 Expression in HT-29 Colonic Epithelial Cells. Biochem. Biophys. Res. Commun. 1997, 232, 169-172.
    • (1997) Biochem. Biophys. Res. Commun. , vol.232 , pp. 169-172
    • Siavoshian, S.1    Blottiere, H.M.2    Cherbut, C.3    Galmiche, J.-P.4
  • 157
    • 33748836655 scopus 로고    scopus 로고
    • Synthetic microbial chemistry. Part 30. Synthesis of acetophthalidin, a fungal metabolite which inhibits the progression of the mammalian cell cycle
    • Nomoto, S.; Mori, K. Synthetic microbial chemistry. Part 30. Synthesis of Acetophthalidin, a Fungal Metabolite Which Inhibits the Progression of the Mammalian Cell Cycle. Liebigs Ann. Recueil. 1997, 4, 721-723.
    • (1997) Liebigs Ann. Recueil. , vol.4 , pp. 721-723
    • Nomoto, S.1    Mori, K.2
  • 158
    • 0028170687 scopus 로고
    • Effect of suramin on p34CDC2 kinase in vitro and in extracts from human H69 cells: Evidence for a double mechanism of action
    • Bojanowski, K.; Nishio, K.; Fukuda, M.; Larsen, A. K.; Saijo, N. Effect of Suramin on p34CDC2 Kinase In Vitro and in Extracts From Human H69 Cells: Evidence for a Double Mechanism of Action. Biochem. Biophys. Res. Commun. 1994, 203, 1574-1580.
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 1574-1580
    • Bojanowski, K.1    Nishio, K.2    Fukuda, M.3    Larsen, A.K.4    Saijo, N.5
  • 159
    • 0026083843 scopus 로고
    • Chemical form of selenium, critical metabolites and cancer prevention
    • Ip, C.; Hayes, C.; Budnick, R. M.; Ganther, H. E. Chemical Form of Selenium, Critical Metabolites and Cancer Prevention. Cancer Res. 1991, 51, 595-600.
    • (1991) Cancer Res. , vol.51 , pp. 595-600
    • Ip, C.1    Hayes, C.2    Budnick, R.M.3    Ganther, H.E.4
  • 160
    • 0002884818 scopus 로고
    • Relationship between the chemical form of selenium and anticarcinogenic activity
    • Wattenberg, L., Lipkin, M., Boone, C. W., Kellof, G. J., Eds.; CRC Press: Boca Raton, FL
    • Ip, C.; Ganther, H. E. Relationship Between the Chemical Form of Selenium and Anticarcinogenic Activity. In Cancer Chemoprevention; Wattenberg, L., Lipkin, M., Boone, C. W., Kellof, G. J., Eds.; CRC Press: Boca Raton, FL, 1992; pp 479-488.
    • (1992) Cancer Chemoprevention , pp. 479-488
    • Ip, C.1    Ganther, H.E.2
  • 161
    • 0031418209 scopus 로고    scopus 로고
    • Inhibition of CDK2 kinase activity by methylselenocysteine in synchronized mouse mammary epithelial tumor cells
    • Sinha, R.; Medina, D. Inhibition of CDK2 Kinase Activity by Methylselenocysteine in Synchronized Mouse Mammary Epithelial Tumor Cells. Carcinogenesis 1997, 18, 1541-1547.
    • (1997) Carcinogenesis , vol.18 , pp. 1541-1547
    • Sinha, R.1    Medina, D.2
  • 162
    • 85038058724 scopus 로고    scopus 로고
    • INK4 Protein p16-Derived Peptides or Peptide Mimetics that Bind by Cyclin-Dependent Kinases, Inhibit Rb Protein Phosphorylation, and are Useful for Treating Hyperproliferative Disorders. PCT Int. Appl. WO 9711174 A1 970327
    • Fahraeus, R.; Lane, D. P. INK4 Protein p16-Derived Peptides or Peptide Mimetics that Bind by Cyclin-Dependent Kinases, Inhibit Rb Protein Phosphorylation, and are Useful for Treating Hyperproliferative Disorders. PCT Int. Appl. WO 9711174 A1 970327.
    • Fahraeus, R.1    Lane, D.P.2
  • 163
  • 165
    • 0028331092 scopus 로고
    • Amplification and overexpression of cyclin D1 in breast cancer detected by immunohistochemical staining
    • Gillett, C.; Fantl, V.; Smith, R.; Fisher, C.; Bartek, J.; Dickson, C.; Barnes, D.; Peters, G. Amplification and Overexpression of Cyclin D1 in Breast Cancer Detected by Immunohistochemical Staining. Cancer Res. 1994, 54, 1812-1817.
    • (1994) Cancer Res. , vol.54 , pp. 1812-1817
    • Gillett, C.1    Fantl, V.2    Smith, R.3    Fisher, C.4    Bartek, J.5    Dickson, C.6    Barnes, D.7    Peters, G.8
  • 166
    • 0028967830 scopus 로고
    • Cyclin D1 oncoprotein aberrantly accumulates in malignancies of diverse histogenesis
    • Bartkova, J.; Lukas, J.; Strauss, M.; Bartek, J. Cyclin D1 Oncoprotein Aberrantly Accumulates in Malignancies of Diverse Histogenesis. Oncogene 1995, 10, 775-778.
    • (1995) Oncogene , vol.10 , pp. 775-778
    • Bartkova, J.1    Lukas, J.2    Strauss, M.3    Bartek, J.4
  • 168
    • 0033590604 scopus 로고    scopus 로고
    • Co-amplification and overexpression of CDK4, SAS and MDM2 occurs frequently in human parosteal osteosarcomas
    • Wunder, J. S.; Eppert, K.; Burrow, S. R.; Gogkoz, N.; Bell, R. S.; Andrulis, I. L. Co-amplification and Overexpression of CDK4, SAS and MDM2 Occurs Frequently in Human Parosteal Osteosarcomas. Oncogene 1999, 18, 783-788.
    • (1999) Oncogene , vol.18 , pp. 783-788
    • Wunder, J.S.1    Eppert, K.2    Burrow, S.R.3    Gogkoz, N.4    Bell, R.S.5    Andrulis, I.L.6
  • 169
    • 0028673746 scopus 로고
    • Role of a cell cycle regulator in hereditary and sporadic cancer
    • Kamb, A. Role of a Cell Cycle Regulator in Hereditary and Sporadic Cancer. Cold Spring Harb. Symp. Quantum Biol. 1994, 59, 39-47.
    • (1994) Cold Spring Harb. Symp. Quantum Biol. , vol.59 , pp. 39-47
    • Kamb, A.1
  • 170
    • 0344301900 scopus 로고    scopus 로고
    • Role of the p16 tumor suppressor gene in cancer
    • Liggett, W. H., Jr.; Sidransky D. Role of the p16 Tumor Suppressor Gene in Cancer. J. Clin. Oncol. 1998, 16, 1197-1206.
    • (1998) J. Clin. Oncol. , vol.16 , pp. 1197-1206
    • Liggett W.H., Jr.1    Sidransky, D.2
  • 171
    • 0033564697 scopus 로고    scopus 로고
    • CDk inhibitors: Positive and negative regulators of G1-phase progression
    • Sherr C. J.; Roberts, J. M. CDK Inhibitors: Positive and Negative Regulators of G1-Phase Progression. Genes Dev. 1999, 13, 1501-1512.
    • (1999) Genes Dev. , vol.13 , pp. 1501-1512
    • Sherr C, J.1    Roberts, J.M.2
  • 172
    • 0032937751 scopus 로고    scopus 로고
    • Loss of Cdk4 expression causes insulin-deficient diabetes and Cdk4 activation results in beta-islet hyperplasia
    • Rane, S. G.; Dubus, P.; Mettus, R. V.; Galbreath, E. J.; Boden, G.; Reddy, E. P.; Barbacid, M. Loss of Cdk4 Expression Causes Insulin-deficient Diabetes and Cdk4 Activation Results in Beta-islet Hyperplasia. Nat. Genet. 1999, 22, 44-52.
    • (1999) Nat. Genet. , vol.22 , pp. 44-52
    • Rane, S.G.1    Dubus, P.2    Mettus, R.V.3    Galbreath, E.J.4    Boden, G.5    Reddy, E.P.6    Barbacid, M.7
  • 174
    • 0027742184 scopus 로고
    • Distinct roles for cyclin-dependent kinases in cell cycle control
    • Van den Heuvel, S.; Harlow, E. Distinct Roles for Cyclin-dependent Kinases in Cell Cycle Control. Science 1993, 262, 2050-2054.
    • (1993) Science , vol.262 , pp. 2050-2054
    • Van Den Heuvel, S.1    Harlow, E.2
  • 175
    • 0033559264 scopus 로고    scopus 로고
    • The p21(Cip1) and p27(Kip1) CDK 'inhibitors' are essential activators of cyclin D-dependent kinases in murine fibroblasts
    • Cheng, M.; Olivier, P.; Diehl, J. A.; Fero, M.; Roussel, M. F.; Roberts, J. M.; Sherr, C. J. The p21(Cip1) and p27(Kip1) CDK 'Inhibitors' are Essential Activators of Cyclin D-dependent Kinases in Murine Fibroblasts. EMBO J. 1999, 18, 1571-1583.
    • (1999) EMBO J. , vol.18 , pp. 1571-1583
    • Cheng, M.1    Olivier, P.2    Diehl, J.A.3    Fero, M.4    Roussel, M.F.5    Roberts, J.M.6    Sherr, C.J.7
  • 176
    • 0032981481 scopus 로고    scopus 로고
    • Induced expression of p16ink41 inhibits both CDK4 and CDK2 associated kinase activity by reassortment of cyclin-CDK inhibitor complexes
    • McConnell, B. B.; Gregory, F. J.; Stott, F. J.; Hara, E.; Peters, G. Induced Expression of p16ink41 Inhibits Both CDK4 and CDK2 Associated Kinase Activity by Reassortment of Cyclin-CDK Inhibitor Complexes. Mot. Cell. Biol. 1999, 19, 1981-1989.
    • (1999) Mot. Cell. Biol. , vol.19 , pp. 1981-1989
    • McConnell, B.B.1    Gregory, F.J.2    Stott, F.J.3    Hara, E.4    Peters, G.5
  • 177
    • 0029587551 scopus 로고
    • Alternate reading frames of the INK4a tumor suppressor gene encode two unrelated proteins capable of inducing cell cycle arrest
    • Quelle, D. E.; Zindy, F.; Ashmun, R. E.; Sherr, C. J. Alternate Reading Frames of the INK4a Tumor Suppressor Gene Encode Two Unrelated Proteins Capable of Inducing Cell Cycle Arrest. Cell 1995, 83, 993-1000.
    • (1995) Cell , vol.83 , pp. 993-1000
    • Quelle, D.E.1    Zindy, F.2    Ashmun, R.E.3    Sherr, C.J.4
  • 178
  • 179
    • 0031297713 scopus 로고    scopus 로고
    • Contribution of the dual coding capacity of the p16INK4a/MTS1/CDKN2 locus to human malignancies
    • Larsen, C. J. Contribution of the Dual Coding Capacity of the p16INK4a/MTS1/CDKN2 Locus to Human Malignancies. Prog. Cell Cycle Res. 1997, 3, 109-124.
    • (1997) Prog. Cell Cycle Res. , vol.3 , pp. 109-124
    • Larsen, C.J.1
  • 180
    • 0032549711 scopus 로고    scopus 로고
    • ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppressor pathways
    • Zhang Y.; Xiong, Y.; Yarbrough, W. G. ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a Locus Deletion Impairs Both the Rb and p53 Tumor Suppressor Pathways. Cell 1998, 92, 725-734.
    • (1998) Cell , vol.92 , pp. 725-734
    • Zhang, Y.1    Xiong, Y.2    Yarbrough, W.G.3
  • 183
    • 0033521621 scopus 로고    scopus 로고
    • Association of p19(ARF) with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53
    • Honda R.; Yasuda, H. Association of p19(ARF) with Mdm2 Inhibits Ubiquitin Ligase Activity of Mdm2 for Tumor Suppressor p53. EMBO J. 1999, 18, 22-27.
    • (1999) EMBO J. , vol.18 , pp. 22-27
    • Honda, R.1    Yasuda, H.2
  • 184
    • 0033536063 scopus 로고    scopus 로고
    • P19(ARF) stabilizes p53 by blocking nucleo-cytoplasmic shuttling of Mdm2
    • Tao, W.; Levine, A. J. P19(ARF) stabilizes p53 by blocking nucleo-cytoplasmic shuttling of Mdm2. Proc. Nati. Acad. Sci. U.S.A. 1999, 96, 6937-6941.
    • (1999) Proc. Nati. Acad. Sci. U.S.A. , vol.96 , pp. 6937-6941
    • Tao, W.1    Levine, A.J.2
  • 186
    • 0030027049 scopus 로고    scopus 로고
    • Dependence of cyclin E-CDK2 kinase activity on cell anchorage
    • Fang, F.; Orend, G.; Watanabe, N.; Hunter, T.; Ruoslahti, E. Dependence of Cyclin E-CDK2 Kinase Activity on Cell Anchorage. Science 1996, 277, 499-502.
    • (1996) Science , vol.277 , pp. 499-502
    • Fang, F.1    Orend, G.2    Watanabe, N.3    Hunter, T.4    Ruoslahti, E.5
  • 187
    • 0032554775 scopus 로고    scopus 로고
    • Cytoplasmic displacement of cyclin E-cdk2 inhibitors p21Cip1 and p27Kip1 in anchorage independent cells
    • Orend, G.; Hunter, T.; Ruoslahti, E. Cytoplasmic Displacement of Cyclin E-cdk2 Inhibitors p21Cip1 and p27Kip1 in Anchorage Independent Cells. Oncogene 1998, 16, 2575-2583.
    • (1998) Oncogene , vol.16 , pp. 2575-2583
    • Orend, G.1    Hunter, T.2    Ruoslahti, E.3
  • 189
    • 0028693067 scopus 로고
    • 1001 Protein kinases redux - Towards 2000
    • Hunter, T. 1001 Protein Kinases Redux - Towards 2000. Cell 1994, 5, 367-376.
    • (1994) Cell , vol.5 , pp. 367-376
    • Hunter, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.