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Volumn 15, Issue 5, 2014, Pages 539-550

Human CDC2-like kinase 1 (CLK1): A novel target for Alzheimer's disease

Author keywords

Alzheimer's disease; Cdc2 like kinase (CLK); CLK1 inhibitors; Protein kinases; SR proteins

Indexed keywords

AKN 028; ALKALOID; BIOLOGICAL FACTOR; CDC2 LIKE KINASE; CDC2 LIKE KINASE 1; CDC2 LIKE KINASE 2; CDC2 LIKE KINASE 3; CDC2 LIKE KINASE 4; CLIOQUINOL; CYCLIN DEPENDENT KINASE 2; CYCLIN DEPENDENT KINASE 4; CYCLIN DEPENDENT KINASE 7; DEBROMOHYMENIALDISINE; DICHLOROINDOLYL ENAMINONITRILE; FLAVONOID; HYMENIALDISINE; INDOLOCARBAZOLE; LEUCETTAMINE B; LEUCETTINE L41; MERIDIANIN; MRNA SPLICING FACTOR 45; PROTEIN SERINE THREONINE KINASE; PROTEIN SERINE THREONINE KINASE INHIBITOR; QUINOLINE DERIVATIVE; RIBONUCLEOPROTEIN; SERINE ARGININE RICH PROTEIN; TAU PROTEIN; UBIQUINONE; UNCLASSIFIED DRUG; UNINDEXED DRUG; VARIOLIN; VARIOLIN B;

EID: 84898607348     PISSN: 13894501     EISSN: 18735592     Source Type: Journal    
DOI: 10.2174/1389450115666140226112321     Document Type: Article
Times cited : (78)

References (84)
  • 1
    • 0033785992 scopus 로고    scopus 로고
    • Biochemical characterization and localization of the dual specificity kinase CLK1
    • Menegay HJ, Myers MP, Moeslein FM, Landreth GE. Biochemical characterization and localization of the dual specificity kinase CLK1. J Cell Sci 2000; 113: 3241-3253.
    • (2000) J Cell Sci , vol.113 , pp. 3241-3253
    • Menegay, H.J.1    Myers, M.P.2    Moeslein, F.M.3    Landreth, G.E.4
  • 2
    • 0026345394 scopus 로고
    • Protein kinase catalytic domain sequence database: Identification of conserved features of primary structure and classification of family members
    • Hanks SK, Quinn AM. Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Meth Enzymol 1991; 200: 38-62.
    • (1991) Meth Enzymol , vol.200 , pp. 38-62
    • Hanks, S.K.1    Quinn, A.M.2
  • 3
    • 0023885305 scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains
    • Hanks SK, Quinn AM, Hunter T. The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains. Science 1988; 241: 42-52.
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 4
    • 0025343230 scopus 로고
    • Signal transduction by receptors with tyrosine kinase activity
    • Ullrich A, Schlessinger J. Signal transduction by receptors with tyrosine kinase activity. Cell 1990; 61: 203-212.
    • (1990) Cell , vol.61 , pp. 203-212
    • Ullrich, A.1    Schlessinger, J.2
  • 5
    • 0027939858 scopus 로고
    • The dual-specificity CLK kinase induces neuronal differentiation of PC12 cells
    • Myers MP, Murphy MB, Landreth K. The dual-specificity CLK kinase induces neuronal differentiation of PC12 cells. Mol Cell Biol 1994; 14(10): 6954-6961.
    • (1994) Mol Cell Biol , vol.14 , Issue.10 , pp. 6954-6961
    • Myers, M.P.1    Murphy, M.B.2    Landreth, K.3
  • 6
    • 0026100595 scopus 로고
    • MAP2 kinase and 70K S6 kinase lie on distinct signalling pathways
    • Ballou L, Luther H, Thomas G. MAP2 kinase and 70K S6 kinase lie on distinct signalling pathways. Nature 1991; 349: 348-350.
    • (1991) Nature , vol.349 , pp. 348-350
    • Ballou, L.1    Luther, H.2    Thomas, G.3
  • 7
    • 66449111724 scopus 로고    scopus 로고
    • Akt2 regulation of Cdc2-like kinases (Clk/Sty), serine/arginine-rich (SR) protein phosphorylation, and insulin-induced alternative splicing of PKCpII messenger ribonucleic acid
    • Jiang K, Patel NA, Watson JE, et al. Akt2 regulation of Cdc2-like kinases (Clk/Sty), serine/arginine-rich (SR) protein phosphorylation, and insulin-induced alternative splicing of PKCpII messenger ribonucleic acid. Endocrinol 2009; 150(5): 2087-2097.
    • (2009) Endocrinol , vol.150 , Issue.5 , pp. 2087-2097
    • Jiang, K.1    Patel, N.A.2    Watson, J.E.3
  • 8
    • 0029910142 scopus 로고    scopus 로고
    • Activity and autophosphorylation of LAMMER protein kinases
    • Lee K, Du C, Horn M, Rabinow L. Activity and autophosphorylation of LAMMER protein kinases. J Biol Chem 1996; 271: 27299-27303.
    • (1996) J Biol Chem , vol.271 , pp. 27299-27303
    • Lee, K.1    Du, C.2    Horn, M.3    Rabinow, L.4
  • 9
    • 79955567813 scopus 로고    scopus 로고
    • Potent and selective small molecule inhibitors of specific isoforms of Cdc2-like kinases (Clk) and dual specificity tyrosine-phosphorylation-regulated kinases (Dyrk)
    • Rosenthal AS, Tanega C, Shen M, et al. Potent and selective small molecule inhibitors of specific isoforms of Cdc2-like kinases (Clk) and dual specificity tyrosine-phosphorylation-regulated kinases (Dyrk). Bioorg Med Chem Lett 2011; 21: 3152-3158.
    • (2011) Bioorg Med Chem Lett , vol.21 , pp. 3152-3158
    • Rosenthal, A.S.1    Tanega, C.2    Shen, M.3
  • 10
    • 71749110422 scopus 로고    scopus 로고
    • Evaluation of substituted 6-arylquinazolin-4-amines as potent and selective inhibitors of cdc2-like kinases (Clk)
    • Mott BT, Tanega C, Shen M, et al. Evaluation of substituted 6-arylquinazolin-4-amines as potent and selective inhibitors of cdc2-like kinases (Clk). Bioorg Med Chem Lett 2009; 19; 6700-6705.
    • (2009) Bioorg Med Chem Lett , vol.19 , pp. 6700-6705
    • Mott, B.T.1    Tanega, C.2    Shen, M.3
  • 11
    • 29144463738 scopus 로고    scopus 로고
    • Alternative splicing: A new drug target of the post-genome era
    • Hagiwara M. Alternative splicing: A new drug target of the post-genome era. Biochim Biophy Acta 2005; 1754: 324-331.
    • (2005) Biochim Biophy Acta , vol.1754 , pp. 324-331
    • Hagiwara, M.1
  • 12
    • 61449243728 scopus 로고    scopus 로고
    • Kinase domain insertions define distinct roles of CLK kinases in SR protein phosphorylation
    • Bullock AN, Das S, Debreczeni JE, et al. Kinase domain insertions define distinct roles of CLK kinases in SR protein phosphorylation. Structure 2009; 17: 352-362.
    • (2009) Structure , vol.17 , pp. 352-362
    • Bullock, A.N.1    Das, S.2    Debreczeni, J.E.3
  • 13
    • 0026026935 scopus 로고
    • STY, a tyrosine phosphorylating enzyme with sequence homology to serine/threonine kinases
    • Howell B, Afar D, Lew J, et al. STY, a tyrosine phosphorylating enzyme with sequence homology to serine/threonine kinases. Mol Cell Biol 1991; 11: 568-572.
    • (1991) Mol Cell Biol , vol.11 , pp. 568-572
    • Howell, B.1    Afar, D.2    Lew, J.3
  • 14
    • 25844491145 scopus 로고    scopus 로고
    • Interplay between SRPK and Clk/Sty kinases in phosphorylation of the splicing factor ASF/SF2 is regulated by a docking motif in ASF/SF2
    • Ngo JCK, Chakrabarti S, Ding JH, et al. Interplay between SRPK and Clk/Sty kinases in phosphorylation of the splicing factor ASF/SF2 is regulated by a docking motif in ASF/SF2. Mol Cell 2005; 20: 77-89.
    • (2005) Mol Cell , vol.20 , pp. 77-89
    • Ngo, J.C.K.1    Chakrabarti, S.2    Ding, J.H.3
  • 15
    • 0033578839 scopus 로고    scopus 로고
    • The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the tyrosine phospha-tase, PTP-1B
    • Moeslein FM, Myers MP, Landreth GE. The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the tyrosine phospha-tase, PTP-1B. J Biol Chem 1999; 274(38): 26697-26704.
    • (1999) J Biol Chem , vol.274 , Issue.38 , pp. 26697-26704
    • Moeslein, F.M.1    Myers, M.P.2    Landreth, G.E.3
  • 16
    • 0028303751 scopus 로고
    • The Doa locus encodes a member of a new protein kinase family and is essential for eye and embryonic development in Drosophila melanogaster
    • Yun B, Farkas R, Lee K, Rabinow L. The Doa locus encodes a member of a new protein kinase family and is essential for eye and embryonic development in Drosophila melanogaster. Genes Dev 1994; 8: 1160-1173.
    • (1994) Genes Dev , vol.8 , pp. 1160-1173
    • Yun, B.1    Farkas, R.2    Lee, K.3    Rabinow, L.4
  • 17
    • 0029744344 scopus 로고    scopus 로고
    • SRPK1 and Clk/Sty protein kinases show distinct substrate specificities for serine/arginine-rich splicing factors
    • Colwill K, Fengi LL, Yeakleyi JM, et al. SRPK1 and Clk/Sty protein kinases show distinct substrate specificities for serine/arginine-rich splicing factors. J Biol Chem 1996; 271(40): 24569-24575.
    • (1996) J Biol Chem , vol.271 , Issue.40 , pp. 24569-24575
    • Colwill, K.1    Fengi, L.L.2    Yeakleyi, J.M.3
  • 18
    • 0030028882 scopus 로고    scopus 로고
    • The Clk/Sty protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution
    • Colwill K, Pawson T, Andrews B, et al. The Clk/Sty protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution. EMBO J 1996; 15: 265-275.
    • (1996) EMBO J , vol.15 , pp. 265-275
    • Colwill, K.1    Pawson, T.2    Andrews, B.3
  • 19
    • 0030863326 scopus 로고    scopus 로고
    • In vivo regulation of alternative pre-mRNA splicing by the Clk1 protein kinase
    • Duncan PI, Stojdl DF, Marius RM, Bell JC. In vivo regulation of alternative pre-mRNA splicing by the Clk1 protein kinase. Mol Cell Biol 1997; 17: 5996-6001.
    • (1997) Mol Cell Biol , vol.17 , pp. 5996-6001
    • Duncan, P.I.1    Stojdl, D.F.2    Marius, R.M.3    Bell, J.C.4
  • 20
    • 0030669604 scopus 로고    scopus 로고
    • Neuronal Cdc24ike kinases: Neuron-specific Forms of Cdk5
    • Lee KY, Qi Z, Yu YP, Wangji JY. Neuronal Cdc24ike kinases: Neuron-specific Forms of Cdk5. Int J Biochem Cell Bid 1997; 29(7): 951-958.
    • (1997) Int J Biochem Cell Bid , vol.29 , Issue.7 , pp. 951-958
    • Lee, K.Y.1    Qi, Z.2    Yu, Y.P.3    Wangji, J.Y.4
  • 21
    • 0026680802 scopus 로고
    • Purification and characterization of a novel proline-directed protein kinase from bovine brain
    • Lew J, Beaudette K, Litwin CME, Wang JH. Purification and characterization of a novel proline-directed protein kinase from bovine brain. J Biol Chem 1992; 267: 13383-13390.
    • (1992) J Biol Chem , vol.267 , pp. 13383-13390
    • Lew, J.1    Beaudette, K.2    Litwin, C.M.E.3    Wang, J.H.4
  • 22
    • 0028122011 scopus 로고
    • A brain-specific activator of cyclin-dependent kinase 5
    • Lew J, Huang QQ, Qi Z, et al. 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    Qi, Z.3
  • 23
    • 0029041001 scopus 로고
    • Structure, function, and regulation of neuronal Cdc2-like protein kinase
    • Lew J, Qi Z, Huang QQ, et al. Structure, function, and regulation of neuronal Cdc2-like protein kinase. Neurobiol Aging 1995; 16(3): 263-270.
    • (1995) Neurobiol Aging , vol.16 , Issue.3 , pp. 263-270
    • Lew, J.1    Qi, Z.2    Huang, Q.Q.3
  • 25
    • 0025756794 scopus 로고
    • Molecular cloning of a novel human cdc2/CDC28-like protein kinase
    • Johnson K, Smith K. Molecular cloning of a novel human cdc2/CDC28-like protein kinase. J Biol Chem 1991; 266: 3402-3407.
    • (1991) J Biol Chem , vol.266 , pp. 3402-3407
    • Johnson, K.1    Smith, K.2
  • 26
    • 84880920758 scopus 로고    scopus 로고
    • Partitioning RS domain phosphorylation in an SR protein through the CLK and SRPK protein kinases
    • Aubol BE, Plocinik RM, Hagopian JC, et al. Partitioning RS domain phosphorylation in an SR protein through the CLK and SRPK protein kinases. J Mol Biol 2013; 425: 2894-2909.
    • (2013) J Mol Biol , vol.425 , pp. 2894-2909
    • Aubol, B.E.1    Plocinik, R.M.2    Hagopian, J.C.3
  • 27
    • 29244449634 scopus 로고    scopus 로고
    • Mass spectromet-ric and kinetic analysis of ASF/SF2 phosphorylation by SRPK1 and Clk/Sty
    • Velazquez-Dones A, Hagopian JC, Ma CT, et al. Mass spectromet-ric and kinetic analysis of ASF/SF2 phosphorylation by SRPK1 and Clk/Sty. J Biol Chem 2005; 280: 41761-41768.
    • (2005) J Biol Chem , vol.280 , pp. 41761-41768
    • Velazquez-Dones, A.1    Hagopian, J.C.2    Ma, C.T.3
  • 28
    • 40649092847 scopus 로고    scopus 로고
    • A sliding docking interaction is essential for sequential and processive phosphorylation of an SR protein by SRPK1
    • Ngo JC, Giang K, Chakrabarti S, et al. A sliding docking interaction is essential for sequential and processive phosphorylation of an SR protein by SRPK1. Mol Cell 2008; 9: 563-576.
    • (2008) Mol Cell , vol.9 , pp. 563-576
    • Ngo, J.C.1    Giang, K.2    Chakrabarti, S.3
  • 29
    • 79958844308 scopus 로고    scopus 로고
    • Differential effect of CLK SR kinases on HIV-1 gene expression: Potential novel targets for therapy
    • Wong R, Balachandran A, Mao AYQ, Dobson W, Gray-Owen S, Cochrane A. Differential effect of CLK SR kinases on HIV-1 gene expression: potential novel targets for therapy. Retrovirol 2011; 8: 47-59.
    • (2011) Retrovirol , vol.8 , pp. 47-59
    • Wong, R.1    Balachandran, A.2    Mao, A.Y.Q.3    Dobson, W.4    Gray-Owen, S.5    Cochrane, A.6
  • 30
    • 39749151729 scopus 로고    scopus 로고
    • Combination of Clk family kinase and SRp75 modulates alternative splicing of Adenovirus E1A
    • Yomoda J, Muraki M, Kataoka N, et al. Combination of Clk family kinase and SRp75 modulates alternative splicing of Adenovirus E1A. Genes to Cells 2008; 13: 233-244.
    • (2008) Genes to Cells , vol.13 , pp. 233-244
    • Yomoda, J.1    Muraki, M.2    Kataoka, N.3
  • 31
    • 84877287737 scopus 로고    scopus 로고
    • Phosphorylation of the alternative mRNA SPF45 by Clk1 regulates its splice site utilization, cell migration and invasion
    • Liu Y, Conaway L, Bethard JR, et al. Phosphorylation of the alternative mRNA SPF45 by Clk1 regulates its splice site utilization, cell migration and invasion. Nucleic Acids Res 2013; 41(9): 4949-4962.
    • (2013) Nucleic Acids Res , vol.41 , Issue.9 , pp. 4949-4962
    • Liu, Y.1    Conaway, L.2    Bethard, J.R.3
  • 32
    • 0142182109 scopus 로고    scopus 로고
    • Human SPF45, a splicing factor, has limited expression in normal tissues, is overexpressed in many tumors, and can confer a multidrug-resistant phenotype to cells
    • Sampath J, Long PR, Shepard RL, et al. Human SPF45, a splicing factor, has limited expression in normal tissues, is overexpressed in many tumors, and can confer a multidrug-resistant phenotype to cells. Am J Pathol 2003; 163: 1781-1790.
    • (2003) Am J Pathol , vol.163 , pp. 1781-1790
    • Sampath, J.1    Long, P.R.2    Shepard, R.L.3
  • 33
    • 23044441609 scopus 로고    scopus 로고
    • Human splicing factor SPF45 (RBM17) confers broad multidrug resistance to antican-cer drugs when overexpressed-a phenotype partially reversed by selective estrogen receptor modulators
    • Perry WL 3rd, Shepard RL, Sampath J, et al. Human splicing factor SPF45 (RBM17) confers broad multidrug resistance to antican-cer drugs when overexpressed-a phenotype partially reversed by selective estrogen receptor modulators. Cancer Res 2005; 65: 6593-6600.
    • (2005) Cancer Res , vol.65 , pp. 6593-6600
    • Perry, W.L.1    Shepard, R.L.2    Sampath, J.3
  • 34
    • 78649696631 scopus 로고    scopus 로고
    • Cortac-tin phosphorylated by ERK1/2 localizes to sites of dynamic actin regulation and is required for carcinoma lamellipodia persistence
    • Kelley LC, Hayes KE, Ammer AG, Martin KH, Weed SA. Cortac-tin phosphorylated by ERK1/2 localizes to sites of dynamic actin regulation and is required for carcinoma lamellipodia persistence. PLoS One 2010; 5: 13847.
    • (2010) PLoS One , vol.5 , pp. 13847
    • Kelley, L.C.1    Hayes, K.E.2    Ammer, A.G.3    Martin, K.H.4    Weed, S.A.5
  • 35
    • 17044461433 scopus 로고    scopus 로고
    • The endogenous and cell cycle-dependent phosphorylation of tau protein in living cells: Implications for Alzheimer's disease
    • Illenberger S, Zheng-Fischerhofer Q, Preuss U, et al. The endogenous and cell cycle-dependent phosphorylation of tau protein in living cells: implications for Alzheimer's disease. Mol Biol Cell 1998; 9: 1495-1512.
    • (1998) Mol Biol Cell , vol.9 , pp. 1495-1512
    • Illenberger, S.1    Zheng-Fischerhofer, Q.2    Preuss, U.3
  • 36
    • 0029008731 scopus 로고
    • Alzheimer abnormally phosphorylated tau is more hyperphosphorylated than the fetal tau and causes the disruption of microtubules
    • Iqbal K, Grundke-Iqbal I. Alzheimer abnormally phosphorylated tau is more hyperphosphorylated than the fetal tau and causes the disruption of microtubules. Neurobiol Aging 1995; 16: 375-379.
    • (1995) Neurobiol Aging , vol.16 , pp. 375-379
    • Iqbal, K.1    Grundke-Iqbal, I.2
  • 37
    • 0034093228 scopus 로고    scopus 로고
    • Progressive supranuclear palsy pathology caused by a novel silent mutation in exon 10 of the tau gene: Expansion of the disease phenotype caused by tau gene mutations
    • Stanford PM, Halliday GM, Brooks WS, et al. Progressive supranuclear palsy pathology caused by a novel silent mutation in exon 10 of the tau gene: Expansion of the disease phenotype caused by tau gene mutations. Brain 2000; 123: 880-893.
    • (2000) Brain , vol.123 , pp. 880-893
    • Stanford, P.M.1    Halliday, G.M.2    Brooks, W.S.3
  • 38
    • 48249148310 scopus 로고    scopus 로고
    • Tau exon 10 alternative splicing and tauopathies
    • Liu F, Gong CX. Tau exon 10 alternative splicing and tauopathies. Mol Neurodegeneration 2008; 3: 8(1-10).
    • (2008) Mol Neurodegeneration , vol.3 , Issue.8 , pp. 1-10
    • Liu, F.1    Gong, C.X.2
  • 39
    • 34548036227 scopus 로고    scopus 로고
    • Tau-mediated neurodegeneration in Alzheimer's disease and related disorders
    • Ballatore C, Lee VM, Trojanowski JQ. Tau-mediated neurodegeneration in Alzheimer's disease and related disorders. Nat Rev Neu-rosci 2007; 8: 663-672.
    • (2007) Nat Rev Neu-rosci , vol.8 , pp. 663-672
    • Ballatore, C.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 40
    • 0027151934 scopus 로고
    • Modulation of exon skipping and inclusion by heterogeneous nuclear ribonucleoprotein A1 and pre-mRNA splicing factor SF2/ASF [published erratum appears in Mol Cell Biol 1993; 13(7): 4458]
    • Mayeda A, Helfman DM, Krainer AR. Modulation of exon skipping and inclusion by heterogeneous nuclear ribonucleoprotein A1 and pre-mRNA splicing factor SF2/ASF [published erratum appears in Mol Cell Biol 1993; 13(7): 4458]. Mol Cell Biol 1993; 13: 2993-3001.
    • (1993) Mol Cell Biol , vol.13 , pp. 2993-3001
    • Mayeda, A.1    Helfman, D.M.2    Krainer, A.R.3
  • 42
    • 84864795907 scopus 로고    scopus 로고
    • Cholinergic-associated loss of hnRNP-A/B in Alzheimer's disease impairs cortical splicing and cognitive function in mice
    • Berson A, Barbash S, Shaltiel G, et al. Cholinergic-associated loss of hnRNP-A/B in Alzheimer's disease impairs cortical splicing and cognitive function in mice. EMBO Mol Med 2012; 4: 730-742.
    • (2012) EMBO Mol Med , vol.4 , pp. 730-742
    • Berson, A.1    Barbash, S.2    Shaltiel, G.3
  • 43
    • 0026543785 scopus 로고
    • Regulation of alternative pre-mRNA splicing by hnRNP A1 and splicing factor SF2
    • Mayeda A, Krainer AR. Regulation of alternative pre-mRNA splicing by hnRNP A1 and splicing factor SF2. Cell 1992; 68: 365-375.
    • (1992) Cell , vol.68 , pp. 365-375
    • Mayeda, A.1    Krainer, A.R.2
  • 44
    • 70350569286 scopus 로고    scopus 로고
    • Mechanisms of alternative splicing regulation: Insights from molecular and genomics approaches
    • Chen M, Manley JL. Mechanisms of alternative splicing regulation: insights from molecular and genomics approaches. Nat Rev Mol Cell Biol 2009; 10: 741-754
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 741-754
    • Chen, M.1    Manley, J.L.2
  • 45
    • 0029767662 scopus 로고    scopus 로고
    • SR proteins and splicing control
    • Manley JL, Tacke R. SR proteins and splicing control. Genes Dev 1996; 10: 1569-1579.
    • (1996) Genes Dev , vol.10 , pp. 1569-1579
    • Manley, J.L.1    Tacke, R.2
  • 46
    • 84876078981 scopus 로고    scopus 로고
    • Mitochondrial deficiency: A double-edgeds word for aging and neurodegeneration
    • Article 244
    • Troulinaki K, Bano D. Mitochondrial deficiency: a double-edgeds word for aging and neurodegeneration. Frontiers in Genetics 2012; 3: Article 244 (1-10).
    • (2012) Frontiers In Genetics , vol.3 , pp. 1-10
    • Troulinaki, K.1    Bano, D.2
  • 47
    • 0029776793 scopus 로고    scopus 로고
    • Determination of life-span in Caenorhabdi-tis elegans by four clock genes
    • Lakowski B, Hekimi S. Determination of life-span in Caenorhabdi-tis elegans by four clock genes. Science 1996; 272: 1010-1013.
    • (1996) Science , vol.272 , pp. 1010-1013
    • Lakowski, B.1    Hekimi, S.2
  • 48
    • 0033118981 scopus 로고    scopus 로고
    • CLK-1 controls respiration, behavior and aging in the nematode Caenorhabditis elegans
    • Felkai S, Ewbank JJ, Lemieux J, Labbe JC, Brown GG, Hekimi S. CLK-1 controls respiration, behavior and aging in the nematode Caenorhabditis elegans. EMBO J 1999; 18: 1783-1792.
    • (1999) EMBO J , vol.18 , pp. 1783-1792
    • Felkai, S.1    Ewbank, J.J.2    Lemieux, J.3    Labbe, J.C.4    Brown, G.G.5    Hekimi, S.6
  • 49
    • 0034964390 scopus 로고    scopus 로고
    • Treatment with a copper-zinc chelator markedly and rapidly inhibits beta- amyloid accumulation in Alzheimer's disease transgenic mice
    • Cherny RA, Atwood CS, Xilinas ME, et al. Treatment with a copper-zinc chelator markedly and rapidly inhibits beta- amyloid accumulation in Alzheimer's disease transgenic mice. Neuron 2001; 30: 665-676.
    • (2001) Neuron , vol.30 , pp. 665-676
    • Cherny, R.A.1    Atwood, C.S.2    Xilinas, M.E.3
  • 50
    • 0242684415 scopus 로고    scopus 로고
    • Geneticor pharmacological iron chelation prevents MPTP-induced neurotoxicity in vivo: A novel therapy for Parkinson's disease
    • Kaur D, Yantiri F, Rajagopalan S, et al. Geneticor pharmacological iron chelation prevents MPTP-induced neurotoxicity in vivo: a novel therapy for Parkinson's disease. Neuron 2003; 37: 899-909.
    • (2003) Neuron , vol.37 , pp. 899-909
    • Kaur, D.1    Yantiri, F.2    Rajagopalan, S.3
  • 51
    • 23844482456 scopus 로고    scopus 로고
    • Clioquinol down-regulates mutant hunting in expression in vitro and mitigates pathology in a Huntington's disease mouse model
    • Nguyen T, Hamby A, Massa SM. Clioquinol down-regulates mutant hunting in expression in vitro and mitigates pathology in a Huntington's disease mouse model. Proc Natl Acad Sci USA 2005; 102: 11840-11845.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 11840-11845
    • Nguyen, T.1    Hamby, A.2    Massa, S.M.3
  • 55
    • 58649090275 scopus 로고    scopus 로고
    • The anti-neurodegeneration drug clioquinol inhibits the aging-associated protein CLK-1
    • Wang Y, Branicky R, Stepanyan Z, et al. The anti-neurodegeneration drug clioquinol inhibits the aging-associated protein CLK-1. J Biol Chem 2009; 284: 314-323.
    • (2009) J Biol Chem , vol.284 , pp. 314-323
    • Wang, Y.1    Branicky, R.2    Stepanyan, Z.3
  • 56
    • 37349020313 scopus 로고    scopus 로고
    • Clioquinol promotes cancer cell toxicity through tumor necrosis factor a release from macrophages
    • Du T, Filiz G, Caragounis A, Crouch PJ, White AR. Clioquinol promotes cancer cell toxicity through tumor necrosis factor a release from macrophages. J Pharmacol Exp Ther 2008; 324: 360-367.
    • (2008) J Pharmacol Exp Ther , vol.324 , pp. 360-367
    • Du, T.1    Filiz, G.2    Caragounis, A.3    Crouch, P.J.4    White, A.R.5
  • 57
    • 79251579303 scopus 로고    scopus 로고
    • Specific CLK inhibitors from a novel chemotype for regulation of alternative splicing
    • Fedorov O, Huber K, Eisenreich A, et al. Specific CLK inhibitors from a novel chemotype for regulation of alternative splicing. Chem Biol 2011; 18: 67-76.
    • (2011) Chem Biol , vol.18 , pp. 67-76
    • Fedorov, O.1    Huber, K.2    Eisenreich, A.3
  • 58
    • 0028179832 scopus 로고
    • Beta-Carbolines from the blue-green alga Dichothrix baueriana
    • Larsen LK, Moore RE, Patterson GM. Beta-Carbolines from the blue-green alga Dichothrix baueriana. J Nat Prod 1994; 57: 419-421.
    • (1994) J Nat Prod , vol.57 , pp. 419-421
    • Larsen, L.K.1    Moore, R.E.2    Patterson, G.M.3
  • 59
    • 79959406830 scopus 로고    scopus 로고
    • Leucettines, a class of potent inhibitors of cdc2-like kinases and dual specificity, tyrosine phosphorylation regulated kinases derived from the marine sponge Leucettamine B: Modulation of alternative pre-RNA splicing
    • Debdab M, Carreaux F, Renault S, et al. Leucettines, a class of potent inhibitors of cdc2-like kinases and dual specificity, tyrosine phosphorylation regulated kinases derived from the marine sponge Leucettamine B: Modulation of alternative pre-RNA splicing. J Med Chem 2011; 54: 4172-4186.
    • (2011) J Med Chem , vol.54 , pp. 4172-4186
    • Debdab, M.1    Carreaux, F.2    Renault, S.3
  • 60
    • 1542509425 scopus 로고    scopus 로고
    • Meridianins, a new family of protein kinase inhibitors isolated from the ascidian Aplid-ium meridianum
    • Gompel M, Leost M, De Kier Joffe EB, et al. Meridianins, a new family of protein kinase inhibitors isolated from the ascidian Aplid-ium meridianum. Bioorg Med Chem Lett 2004; 14: 1703-1707.
    • (2004) Bioorg Med Chem Lett , vol.14 , pp. 1703-1707
    • Gompel, M.1    Leost, M.2    De Kier Joffe, E.B.3
  • 61
    • 79960196093 scopus 로고    scopus 로고
    • Synthesis, protein kinase inhibitory potencies, and in vitro antiproliferative activities of merid-ianin derivatives
    • Giraud F, Alves G, Debiton E, et al. Synthesis, protein kinase inhibitory potencies, and in vitro antiproliferative activities of merid-ianin derivatives. J Med Chem 2011; 54: 4474-4489.
    • (2011) J Med Chem , vol.54 , pp. 4474-4489
    • Giraud, F.1    Alves, G.2    Debiton, E.3
  • 62
    • 0028230338 scopus 로고
    • Alkaloids from the antarctic sponge Kirkpatrickia varialosa. Part 2: Variolin A and N (3')-methyl tetrahydrovariolin
    • Trimurtulu G, Faulkner DJ, Perry NB, et al. Alkaloids from the antarctic sponge Kirkpatrickia varialosa. Part 2: Variolin A and N (3')-methyl tetrahydrovariolin. Tetrahedron 1994; 50: 3993-4000.
    • (1994) Tetrahedron , vol.50 , pp. 3993-4000
    • Trimurtulu, G.1    Faulkner, D.J.2    Perry, N.B.3
  • 63
    • 0028198228 scopus 로고
    • Alkaloids from the antarctic sponge Kirkpatrickia varialosa.: Part 1: Variolin b, a new antitumour and antiviral compound
    • Perry NB, Ettouati L, Litaudon M, Blunt JW, Munro MHG. Alkaloids from the antarctic sponge Kirkpatrickia varialosa.: Part 1: Variolin b, a new antitumour and antiviral compound. Tetrahedron 1994; 50: 3987-3992.
    • (1994) Tetrahedron , vol.50 , pp. 3987-3992
    • Perry, N.B.1    Ettouati, L.2    Litaudon, M.3    Blunt, J.W.4    Munro, M.H.G.5
  • 65
    • 84898632223 scopus 로고    scopus 로고
    • Unpublished results, PhD candidate, University of Adelaide
    • Carter E. Unpublished results, PhD candidate, University of Adelaide, 2005-2011.
    • (2005)
    • Carter, E.1
  • 67
    • 39749165071 scopus 로고    scopus 로고
    • Meriolins, (3-(pyrimidin-4-yl)-7-azaindoles): Synthesis, kinase inhibitory activity, cellular effects, and structure of a CDK2/cyclin A/meriolin complex
    • Echalier A, Bettayeb K, Ferandin Y, et al. Meriolins, (3-(pyrimidin-4-yl)-7-azaindoles): synthesis, kinase inhibitory activity, cellular effects, and structure of a CDK2/cyclin A/meriolin complex. J Med Chem 2008; 51: 737-751.
    • (2008) J Med Chem , vol.51 , pp. 737-751
    • Echalier, A.1    Bettayeb, K.2    Ferandin, Y.3
  • 68
    • 34548583169 scopus 로고    scopus 로고
    • Meriolins, a new class of cell death-inducing kinase inhibitors with enhanced selectivity for cyclin-dependent kinases
    • Bettayeb K, Tirado OM, Marionneau-Lambot S, et al. Meriolins, a new class of cell death-inducing kinase inhibitors with enhanced selectivity for cyclin-dependent kinases. Cancer Res 2007; 67: 8325-8334.
    • (2007) Cancer Res , vol.67 , pp. 8325-8334
    • Bettayeb, K.1    Tirado, O.M.2    Marionneau-Lambot, S.3
  • 69
    • 84898621613 scopus 로고    scopus 로고
    • Effects of a series of meriolins, new class of cyclin-dependent kinase inhibitors, on glioma proliferation
    • Jarry M, Schouft MT, Liger F, et al. Effects of a series of meriolins, new class of cyclin-dependent kinase inhibitors, on glioma proliferation, Glia 2009; 57: S168.
    • (2009) Glia , vol.57
    • Jarry, M.1    Schouft, M.T.2    Liger, F.3
  • 70
    • 84863356201 scopus 로고    scopus 로고
    • Synthesis, biological evaluation, and molecular modeling of natural and unnatural fla-vonoidal alkaloids, inhibitors of kinases
    • Nguyen TB, Lozach O, Surpateanu G, et al. Synthesis, biological evaluation, and molecular modeling of natural and unnatural fla-vonoidal alkaloids, inhibitors of kinases. J Med Chem 2012; 55: 2811-2819.
    • (2012) J Med Chem , vol.55 , pp. 2811-2819
    • Nguyen, T.B.1    Lozach, O.2    Surpateanu, G.3
  • 71
    • 84869782889 scopus 로고    scopus 로고
    • Recent advances in the design, synthesis, and biological evaluation of selective DYRK1A inhibitors: A new avenue for a disease modifying treatment of Alzheimer's". ACS
    • Smith B, Medda F, Gokhale V, Dunckley T, Hulme C. Recent advances in the design, synthesis, and biological evaluation of selective DYRK1A inhibitors: A new avenue for a disease modifying treatment of Alzheimer's". ACS Chem. Neurosci. 2012; 3(11): 857-872.
    • (2012) Chem. Neurosci , vol.3 , Issue.11 , pp. 857-872
    • Smith, B.1    Medda, F.2    Gokhale, V.3    Dunckley, T.4    Hulme, C.5
  • 72
    • 84865969722 scopus 로고    scopus 로고
    • The novel tyrosine kinase inhibitor AKN-028 has significant antileukemic activity in cell lines and primary cultures of acute myeloid leukemia
    • Eriksson A, Hermanson M, Wickström M, et al. The novel tyrosine kinase inhibitor AKN-028 has significant antileukemic activity in cell lines and primary cultures of acute myeloid leukemia. Blood Cancer J 2012; 2: e81.
    • (2012) Blood Cancer J , vol.2
    • Eriksson, A.1    Hermanson, M.2    Wickström, M.3
  • 73
    • 0034010742 scopus 로고    scopus 로고
    • Inhibition of cyclin-dependent kinases, GSK-3p and CK1 by hymenialdisine, a marine sponge constituent
    • Meijer L, Thunnissen AMWH, White AW, et al. Inhibition of cyclin-dependent kinases, GSK-3p and CK1 by hymenialdisine, a marine sponge constituent. Chem Biol 2000; 7: 51-63.
    • (2000) Chem Biol , vol.7 , pp. 51-63
    • Meijer, L.1    Thunnissen, A.M.W.H.2    White, A.W.3
  • 74
    • 84857032650 scopus 로고    scopus 로고
    • Synthesis and evaluation of debromohymenialdisine-derived Chk2 inhibitors
    • Saleem RSZ, Lansdell TA, Tepe JJ. Synthesis and evaluation of debromohymenialdisine-derived Chk2 inhibitors. Bioorg Med Chem 2012; 20: 1475-1481.
    • (2012) Bioorg Med Chem , vol.20 , pp. 1475-1481
    • Saleem, R.S.Z.1    Lansdell, T.A.2    Tepe, J.J.3
  • 77
    • 84878111705 scopus 로고    scopus 로고
    • Small-molecule pyrimidine inhibitors of the cdc2-like (Clk) and dual specificity tyrosine phos-phorylation-regulated (Dyrk) kinases: Development of chemical probe ML315
    • Coombs TC, Tanega C, Shen M, et al. Small-molecule pyrimidine inhibitors of the cdc2-like (Clk) and dual specificity tyrosine phos-phorylation-regulated (Dyrk) kinases: Development of chemical probe ML315. Bioorg Med Chem Lett 2013; 23(12): 3654-3661.
    • (2013) Bioorg Med Chem Lett , vol.23 , Issue.12 , pp. 3654-3661
    • Coombs, T.C.1    Tanega, C.2    Shen, M.3
  • 78
    • 84869129800 scopus 로고    scopus 로고
    • Synthesis of N,N0-bis(5-arylidene-4-oxo-3,5-dihydro-4H-imidazol-2-yl)diamines bearing various linkers and biological evaluation as potential inhibitors of kinases
    • Coulibaly WK, Paquin L, Bénie A, et al. Synthesis of N,N0-bis(5-arylidene-4-oxo-3,5-dihydro-4H-imidazol-2-yl)diamines bearing various linkers and biological evaluation as potential inhibitors of kinases. Eur J Med Chem 2012; 58: 581-590.
    • (2012) Eur J Med Chem , vol.58 , pp. 581-590
    • Coulibaly, W.K.1    Paquin, L.2    Bénie, A.3
  • 79
    • 84868236760 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of N-arylbenzo[b]thieno[3,2-d]pyrimidin-4amines and their pyrido and pyrazino analogues as Ser/Thr kinase inhibitors
    • Loidreau Y, Marchand P, Dubouilh-Benard C, et al. Synthesis and biological evaluation of N-arylbenzo[b]thieno[3,2-d]pyrimidin-4amines and their pyrido and pyrazino analogues as Ser/Thr kinase inhibitors. Eur J Med Chem 2012; 58: 171-183.
    • (2012) Eur J Med Chem , vol.58 , pp. 171-183
    • Loidreau, Y.1    Marchand, P.2    Dubouilh-Benard, C.3
  • 80
    • 84870724248 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of N-aryl-7-methoxybenzo[b]furo[3,2-d]pyrimidin-4-amines and their N-arylbenzo[b]thieno[3,2-d]pyrimidin-4-amine analogues as dual inhibitors of CLK1 and DYRK1A kinases
    • Loidreau Y, Marchand P, Dubouilh-Benard C, et al. Synthesis and biological evaluation of N-aryl-7-methoxybenzo[b]furo[3,2-d]pyrimidin-4-amines and their N-arylbenzo[b]thieno[3,2-d]pyrimidin-4-amine analogues as dual inhibitors of CLK1 and DYRK1A kinases. Eur J Med Chem 2013; 59: 283-295.
    • (2013) Eur J Med Chem , vol.59 , pp. 283-295
    • Loidreau, Y.1    Marchand, P.2    Dubouilh-Benard, C.3
  • 81
    • 84888861819 scopus 로고    scopus 로고
    • Synthesis of novel 7-substituted pyrido[2',3':4,5]furo[3,2-d]pyrimidin-4-amines and their N-aryl analogues and evaluation of their inhibitory activity against Ser/Thr kinases
    • Deau E, Loidreau Y, Marchand P, et al. Synthesis of novel 7-substituted pyrido[2',3':4,5]furo[3,2-d]pyrimidin-4-amines and their N-aryl analogues and evaluation of their inhibitory activity against Ser/Thr kinases. Bioorg Med Chem Lett 2013; 23(24): 6784-6788.
    • (2013) Bioorg Med Chem Lett , vol.23 , Issue.24 , pp. 6784-6788
    • Deau, E.1    Loidreau, Y.2    Marchand, P.3
  • 82
    • 84855824393 scopus 로고    scopus 로고
    • 7,8-Dichloro-1-oxo-p-carbolines as a versatile scaffold for the development of potent and selective kinase inhibitors with unusual binding modes
    • Huber K, Brault L, Fedorov O, et al. 7,8-Dichloro-1-oxo-p-carbolines as a versatile scaffold for the development of potent and selective kinase inhibitors with unusual binding modes. J Med Chem 2012; 55(1): 403-413.
    • (2012) J Med Chem , vol.55 , Issue.1 , pp. 403-413
    • Huber, K.1    Brault, L.2    Fedorov, O.3
  • 84
    • 84898616863 scopus 로고    scopus 로고
    • http://www.alz.co.uk/research/WorldAlzheimerReport2013.pdf


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