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Volumn 1830, Issue 8, 2013, Pages 4091-4101

A novel inhibitor, 16-hydroxy-cleroda-3,13-dien-16,15-olide, blocks the autophosphorylation site of focal adhesion kinase (Y397) by molecular docking

Author keywords

16 hydroxy cleroda 3,13 dien 16,15 olide; Anti tumorigenesis; Epithelial mesenchymal transition; Filopodia; Focal adhesion kinase

Indexed keywords

16 HYDROXYCLERODA 3,13 DIEN 16,15 OLIDE; 3,4 DIHYDROXYPHENYL ACETIC ACID; 4 HYDROXYPHENYLACETIC ACID; ACTINODAPHNINE; CATECHIN HYDRATE; CELL PROTEIN; CINNAMIC ACID BENZYL ESTER; CISPLATIN; CURCUMIN; FOCAL ADHESION KINASE; FOCAL ADHESION KINASE INHIBITOR; GELATINASE A; GELATINASE B; KAEMPFEROL; NATURAL PRODUCT; PROTEIN CDC42; QUERCETIN; RAC1 PROTEIN; RESVERATROL; UNCLASSIFIED DRUG;

EID: 84877829471     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2013.04.027     Document Type: Article
Times cited : (46)

References (43)
  • 2
    • 0028918391 scopus 로고
    • Identification of Tyr-397 as the primary site of tyrosine phosphorylation and pp60src association in the focal adhesion kinase, pp125FAK
    • B.L. Eide, C.W. Turck, and J.A. Escobedo Identification of Tyr-397 as the primary site of tyrosine phosphorylation and pp60src association in the focal adhesion kinase, pp125FAK Mol. Cell. Biol. 15 1995 2819 2827
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2819-2827
    • Eide, B.L.1    Turck, C.W.2    Escobedo, J.A.3
  • 4
    • 0028173980 scopus 로고
    • Stable association of pp60src and pp59fyn with the focal adhesion-associated protein tyrosine kinase, pp125FAK
    • B.S. Cobb, M.D. Schaller, T.H. Leu, and J.T. Parsons Stable association of pp60src and pp59fyn with the focal adhesion-associated protein tyrosine kinase, pp125FAK Mol. Cell. Biol. 14 1994 147 155
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 147-155
    • Cobb, B.S.1    Schaller, M.D.2    Leu, T.H.3    Parsons, J.T.4
  • 5
    • 0028350859 scopus 로고
    • Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src
    • M.D. Schaller, J.D. Hildebrand, J.D. Shannon, J.W. Fox, R.R. Vines, and J.T. Parsons Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src Mol. Cell. Biol. 14 1994 1680 1688
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1680-1688
    • Schaller, M.D.1    Hildebrand, J.D.2    Shannon, J.D.3    Fox, J.W.4    Vines, R.R.5    Parsons, J.T.6
  • 7
    • 34548085454 scopus 로고    scopus 로고
    • Focal Adhesion Kinase and p53 Signaling in Cancer Cells
    • DOI 10.1016/S0074-7696(07)63003-4, PII S0074769607630034, A Survey of Cell Biology
    • V.M. Golubovskaya, and W.G. Cance Focal adhesion kinase and p53 signaling in cancer cells Int. Rev. Cytol. 263 2007 103 153 (Pubitemid 47296394)
    • (2007) International Review of Cytology , vol.263 , pp. 103-153
    • Golubovskaya, V.M.1    Cance, W.G.2
  • 9
    • 0037509990 scopus 로고    scopus 로고
    • Focal adhesion kinase: The first ten years
    • DOI 10.1242/jcs.00373
    • J.T. Parsons Focal adhesion kinase: the first ten years J. Cell Sci. 116 2003 1409 1416 (Pubitemid 36527488)
    • (2003) Journal of Cell Science , vol.116 , Issue.8 , pp. 1409-1416
    • Parsons, J.T.1
  • 11
    • 84872149479 scopus 로고    scopus 로고
    • Sonic hedgehog signaling pathway induces cell migration and invasion through focal adhesion kinase/AKT signaling-mediated activation of matrix metalloproteinase (MMP)-2 and MMP-9 in liver cancer
    • J.S. Chen, X.H. Huang, Q. Wang, J.Q. Huang, L.J. Zhang, X.L. Chen, J. Lei, and Z.X. Cheng Sonic hedgehog signaling pathway induces cell migration and invasion through focal adhesion kinase/AKT signaling-mediated activation of matrix metalloproteinase (MMP)-2 and MMP-9 in liver cancer Carcinogenesis 34 2013 10 19
    • (2013) Carcinogenesis , vol.34 , pp. 10-19
    • Chen, J.S.1    Huang, X.H.2    Wang, Q.3    Huang, J.Q.4    Zhang, L.J.5    Chen, X.L.6    Lei, J.7    Cheng, Z.X.8
  • 13
    • 22644443940 scopus 로고    scopus 로고
    • The origin of vimentin expression in invasive breast cancer: Epithelial- mesenchymal transition, myoepithelial histogenesis or histogenesis from progenitor cells with bilinear differentiation potential?
    • DOI 10.1002/path.1797
    • E. Korsching, J. Packeisen, C. Liedtke, D. Hungermann, P. Wulfing, P.J. van Diest, B. Brandt, W. Boecker, and H. Buerger The origin of vimentin expression in invasive breast cancer: epithelial-mesenchymal transition, myoepithelial histogenesis or histogenesis from progenitor cells with bilinear differentiation potential? J. Pathol. 206 2005 451 457 (Pubitemid 41025348)
    • (2005) Journal of Pathology , vol.206 , Issue.4 , pp. 451-457
    • Korsching, E.1    Packeisen, J.2    Liedtke, C.3    Hungermann, D.4    Wulfing, P.5    Van Diest, P.J.6    Brandt, B.7    Boecker, W.8    Buerger, H.9
  • 14
    • 16244422687 scopus 로고    scopus 로고
    • Linking epithelial-mesenchymal transition to the well-known polarity protein par6
    • DOI 10.1016/j.devcel.2005.03.002, PII S1534580705000833
    • J.P. Thiery, and R. Huang Linking epithelial-mesenchymal transition to the well-known polarity protein Par6 Dev. Cell 8 2005 456 458 (Pubitemid 40450734)
    • (2005) Developmental Cell , vol.8 , Issue.4 , pp. 456-458
    • Thiery, J.P.1    Huang, R.2
  • 15
    • 33645302628 scopus 로고    scopus 로고
    • The epithelial-mesenchymal transition: New insights in signaling, development, and disease
    • J.M. Lee, S. Dedhar, R. Kalluri, and E.W. Thompson The epithelial-mesenchymal transition: new insights in signaling, development, and disease J. Cell Biol. 172 2006 973 981
    • (2006) J. Cell Biol. , vol.172 , pp. 973-981
    • Lee, J.M.1    Dedhar, S.2    Kalluri, R.3    Thompson, E.W.4
  • 16
    • 77954363056 scopus 로고    scopus 로고
    • Molecular docking studies of curcumin derivatives with multiple protein targets for procarcinogen activating enzyme inhibition
    • P.K.C.R. Girija, Chetan S. Poojari, Noor Shahina Begum, and Akheel Ahmed Syed Molecular docking studies of curcumin derivatives with multiple protein targets for procarcinogen activating enzyme inhibition J. Proteome Bioinform. 3 2010 200 203
    • (2010) J. Proteome Bioinform. , vol.3 , pp. 200-203
    • Girija, P.K.C.R.1    Poojari, C.S.2    Begum, N.S.3    Syed, A.A.4
  • 17
    • 57349153946 scopus 로고    scopus 로고
    • A small molecule inhibitor, 1,2,4,5-benzenetetraamine tetrahydrochloride, targeting the y397 site of focal adhesion kinase decreases tumor growth
    • V.M. Golubovskaya, C. Nyberg, M. Zheng, F. Kweh, A. Magis, D. Ostrov, and W.G. Cance A small molecule inhibitor, 1,2,4,5-benzenetetraamine tetrahydrochloride, targeting the y397 site of focal adhesion kinase decreases tumor growth J. Med. Chem. 51 2008 7405 7416
    • (2008) J. Med. Chem. , vol.51 , pp. 7405-7416
    • Golubovskaya, V.M.1    Nyberg, C.2    Zheng, M.3    Kweh, F.4    Magis, A.5    Ostrov, D.6    Cance, W.G.7
  • 20
    • 84860478933 scopus 로고    scopus 로고
    • A small molecule focal adhesion kinase (FAK) inhibitor, targeting Y397 site: 1-(2-hydroxyethyl)-3, 5, 7-triaza-1-azoniatricyclo [3.3.1.1(3,7)]decane; Bromide effectively inhibits FAK autophosphorylation activity and decreases cancer cell viability, clonogenicity and tumor growth in vivo
    • V.M. Golubovskaya, S. Figel, B.T. Ho, C.P. Johnson, M. Yemma, G. Huang, M. Zheng, C. Nyberg, A. Magis, D.A. Ostrov, I.H. Gelman, and W.G. Cance A small molecule focal adhesion kinase (FAK) inhibitor, targeting Y397 site: 1-(2-hydroxyethyl)-3, 5, 7-triaza-1-azoniatricyclo [3.3.1.1(3,7)]decane; bromide effectively inhibits FAK autophosphorylation activity and decreases cancer cell viability, clonogenicity and tumor growth in vivo Carcinogenesis 33 2012 1004 1013
    • (2012) Carcinogenesis , vol.33 , pp. 1004-1013
    • Golubovskaya, V.M.1    Figel, S.2    Ho, B.T.3    Johnson, C.P.4    Yemma, M.5    Huang, G.6    Zheng, M.7    Nyberg, C.8    Magis, A.9    Ostrov, D.A.10    Gelman, I.H.11    Cance, W.G.12
  • 22
    • 0842281645 scopus 로고    scopus 로고
    • Cell Death: Critical Control Points
    • DOI 10.1016/S0092-8674(04)00046-7
    • N.N. Danial, and S.J. Korsmeyer Cell death: critical control points Cell 116 2004 205 219 (Pubitemid 38167313)
    • (2004) Cell , vol.116 , Issue.2 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 23
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • C.B. Thompson Apoptosis in the pathogenesis and treatment of disease Science 267 1995 1456 1462
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 24
    • 0042833078 scopus 로고    scopus 로고
    • Apoptosis-based drug screening and detection of selective toxicity to cancer cells
    • DOI 10.1097/00001813-200308000-00008
    • O.S. Frankfurt, and A. Krishan Apoptosis-based drug screening and detection of selective toxicity to cancer cells Anticancer Drugs 14 2003 555 561 (Pubitemid 37083161)
    • (2003) Anti-Cancer Drugs , vol.14 , Issue.7 , pp. 555-561
    • Frankfurt, O.S.1    Krishan, A.2
  • 25
    • 0027282044 scopus 로고
    • Bcl-x, A bcl-2-related gene that functions as a dominant regulator of apoptotic cell death
    • DOI 10.1016/0092-8674(93)90508-N
    • L.H. Boise, M. Gonzalez-Garcia, C.E. Postema, L. Ding, T. Lindsten, L.A. Turka, X. Mao, G. Nunez, and C.B. Thompson bcl-x, a bcl-2-related gene that functions as a dominant regulator of apoptotic cell death Cell 74 1993 597 608 (Pubitemid 23259741)
    • (1993) Cell , vol.74 , Issue.4 , pp. 597-608
    • Boise, L.H.1    Gonzalez-Garcia, M.2    Postema, C.E.3    Ding, L.4    Lindsten, T.5    Turka, L.A.6    Mao, X.7    Nunez, G.8    Thompson, C.B.9
  • 26
    • 0027166048 scopus 로고
    • Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programed cell death
    • DOI 10.1016/0092-8674(93)90509-O
    • Z.N. Oltvai, C.L. Milliman, and S.J. Korsmeyer Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death Cell 74 1993 609 619 (Pubitemid 23259742)
    • (1993) Cell , vol.74 , Issue.4 , pp. 609-619
    • Oltvai, Z.N.1    Milliman, C.L.2    Korsmeyer, S.J.3
  • 27
    • 0028149786 scopus 로고
    • Checkpoints of dueling dimers foil death wishes
    • DOI 10.1016/0092-8674(94)90188-0
    • Z.N. Oltvai, and S.J. Korsmeyer Checkpoints of dueling dimers foil death wishes Cell 79 1994 189 192 (Pubitemid 24324909)
    • (1994) Cell , vol.79 , Issue.2 , pp. 189-192
    • Oltvai, Z.N.1    Korsmeyer, S.J.2
  • 28
    • 8944230657 scopus 로고    scopus 로고
    • Overexpression of the death-promoting gene bax-α which is downregulated in breast cancer restores sensitivity to different apoptotic stimuli and reduces tumor growth in SCID mice
    • R.C. Bargou, C. Wagener, K. Bommert, M.Y. Mapara, P.T. Daniel, W. Arnold, M. Dietel, H. Guski, A. Feller, H.D. Royer, and B. Dorken Overexpression of the death-promoting gene bax-alpha which is downregulated in breast cancer restores sensitivity to different apoptotic stimuli and reduces tumor growth in SCID mice J. Clin. Invest. 97 1996 2651 2659 (Pubitemid 26187353)
    • (1996) Journal of Clinical Investigation , vol.97 , Issue.11 , pp. 2651-2659
    • Bargou, R.C.1    Wagener, C.2    Bommert, K.3    Mapara, M.Y.4    Daniel, P.T.5    Arnold, W.6    Dietel, M.7    Guski, H.8    Feller, A.9    Royer, H.D.10    Dorken, B.11
  • 29
    • 0030062205 scopus 로고    scopus 로고
    • Induction of the death-promoting gene bax-α sensitizes cultures breast-cancer cells to drug-induced apoptosis
    • DOI 10.1002/(SICI)1097-0215(1996 0703)67:1<138::AID-IJC22>3. 0.CO;2-9
    • C. Wagener, R.C. Bargou, P.T. Daniel, K. Bommert, M.Y. Mapara, H.D. Royer, and B. Dorken Induction of the death-promoting gene bax-alpha sensitizes cultured breast-cancer cells to drug-induced apoptosis Int. J. Cancer 67 1996 138 141 (Pubitemid 26236080)
    • (1996) International Journal of Cancer , vol.67 , Issue.1 , pp. 138-141
    • Wagener, C.1    Bargou, R.C.2    Daniel, P.T.3    Bommert, K.4    Mapara, M.Y.5    Royer, H.D.6    Dorren, B.7
  • 30
    • 0031907378 scopus 로고    scopus 로고
    • P53 modulation of Fas/Apo-1 mediated apoptosis in a human renal cell carcinoma cell line
    • H. Miyake, I. Hara, K. Gohji, S. Arakawa, and S. Kamidono p53 modulation of Fas/Apo-1 mediated apoptosis in a human renal cell carcinoma cell line Int. J. Oncol. 12 1998 469 473 (Pubitemid 28064878)
    • (1998) International Journal of Oncology , vol.12 , Issue.2 , pp. 469-473
    • Miyake, H.1    Hara, I.2    Gohji, K.3    Arakawa, S.4    Kamidono, S.5
  • 31
    • 2442621492 scopus 로고    scopus 로고
    • Role of AIF in caspase-dependent and caspase-independent cell death
    • DOI 10.1038/sj.onc.1207517
    • S.P. Cregan, V.L. Dawson, and R.S. Slack Role of AIF in caspase-dependent and caspase-independent cell death Oncogene 23 2004 2785 2796 (Pubitemid 38638842)
    • (2004) Oncogene , vol.23 , Issue.16 REV. ISS. 2 , pp. 2785-2796
    • Cregan, S.P.1    Dawson, V.L.2    Slack, R.S.3
  • 32
    • 10044219518 scopus 로고    scopus 로고
    • A role for caveolae in cell migration
    • DOI 10.1096/fj.04-2516rev
    • A. Navarro, B. Anand-Apte, and M.O. Parat A role for caveolae in cell migration FASEB J. 18 2004 1801 1811 (Pubitemid 39602266)
    • (2004) FASEB Journal , vol.18 , Issue.15 , pp. 1801-1811
    • Navarro, A.1    Anand-Apte, B.2    Parat, M.-O.3
  • 33
    • 0037192635 scopus 로고    scopus 로고
    • Complex roles of tissue inhibitors of metalloproteinases in cancer
    • DOI 10.1038/sj.onc.1205291
    • Y. Jiang, I.D. Goldberg, and Y.E. Shi Complex roles of tissue inhibitors of metalloproteinases in cancer Oncogene 21 2002 2245 2252 (Pubitemid 34311378)
    • (2002) Oncogene , vol.21 , Issue.14 , pp. 2245-2252
    • Jiang, Y.1    Goldberg, I.D.2    Shi, Y.E.3
  • 34
    • 0032850365 scopus 로고    scopus 로고
    • Matrix metalloproteinases in tumour invasion and metastasis
    • DOI 10.1002/(SICI)1096-9896(1999 11)189:3<300::AID-PATH456>3. 0.CO;2-C
    • S. Curran, and G.I. Murray Matrix metalloproteinases in tumour invasion and metastasis J. Pathol. 189 1999 300 308 (Pubitemid 29489213)
    • (1999) Journal of Pathology , vol.189 , Issue.3 , pp. 300-308
    • Curran, S.1    Murray, G.I.2
  • 35
    • 0037052641 scopus 로고    scopus 로고
    • Matrix metalloproteinases in cancer: Prognostic markers and therapeutic targets
    • DOI 10.1002/ijc.10329
    • P. Vihinen, and V.M. Kahari Matrix metalloproteinases in cancer: prognostic markers and therapeutic targets Int. J. Cancer 99 2002 157 166 (Pubitemid 34309470)
    • (2002) International Journal of Cancer , vol.99 , Issue.2 , pp. 157-166
    • Vihinen, P.1    Kahari, V.-M.2
  • 36
    • 15244342010 scopus 로고    scopus 로고
    • Matrix metalloproteinases as therapeutic targets in cancer
    • DOI 10.2174/1568009053765799
    • P. Vihinen, R. Ala-aho, and V.M. Kahari Matrix metalloproteinases as therapeutic targets in cancer Curr. Cancer Drug Targets 5 2005 203 220 (Pubitemid 40694861)
    • (2005) Current Cancer Drug Targets , vol.5 , Issue.3 , pp. 203-220
    • Vihinen, P.1    Ala-Aho, R.2    Kahari, V.-M.3
  • 38
    • 0034676334 scopus 로고    scopus 로고
    • A role for FAK in the Concanavalin A-dependent secretion of matrix metalloproteinase-2 and -9
    • DOI 10.1038/sj.onc.1203932
    • T.T. Sein, A.A. Thant, Y. Hiraiwa, A.R. Amin, Y. Sohara, Y. Liu, S. Matsuda, T. Yamamoto, and M. Hamaguchi A role for FAK in the concanavalin A-dependent secretion of matrix metalloproteinase-2 and -9 Oncogene 19 2000 5539 5542 (Pubitemid 32000922)
    • (2000) Oncogene , vol.19 , Issue.48 , pp. 5539-5542
    • Sein, T.T.1    Thant, A.A.2    Hiraiwa, Y.3    Amin, A.R.M.R.4    Sohara, Y.5    Liu, Y.6    Matsuda, S.7    Yamamoto, T.8    Hamaguchi, M.9
  • 39
    • 0035476836 scopus 로고    scopus 로고
    • Inhibition of focal adhesion kinase expression or activity disrupts epidermal growth factor-stimulated signaling promoting the migration of invasive human carcinoma cells
    • C.R. Hauck, D.J. Sieg, D.A. Hsia, J.C. Loftus, W.A. Gaarde, B.P. Monia, and D.D. Schlaepfer Inhibition of focal adhesion kinase expression or activity disrupts epidermal growth factor-stimulated signaling promoting the migration of invasive human carcinoma cells Cancer Res. 61 2001 7079 7090 (Pubitemid 32946499)
    • (2001) Cancer Research , vol.61 , Issue.19 , pp. 7079-7090
    • Hauck, C.R.1    Sieg, D.J.2    Hsia, D.A.3    Loftus, J.C.4    Gaarde, W.A.5    Monia, B.P.6    Schlaepfer, D.D.7
  • 40
    • 34447517479 scopus 로고    scopus 로고
    • FAK signaling in neoplastic disorders: A linkage between inflammation and cancer
    • DOI 10.1196/annals.1377.019, Integrated Molecular Medicine for Neuronal and Neoplastic Disorders
    • N.N. Mon, S. Ito, T. Senga, and M. Hamaguchi FAK signaling in neoplastic disorders: a linkage between inflammation and cancer Ann. N. Y. Acad. Sci. 1086 2006 199 212 (Pubitemid 47084387)
    • (2006) Annals of the New York Academy of Sciences , vol.1086 , pp. 199-212
    • Mon, N.N.1    Ito, S.2    Senga, T.3    Hamaguchi, M.4
  • 42
    • 60649087564 scopus 로고    scopus 로고
    • Accelerated metastasis after short-term treatment with a potent inhibitor of tumor angiogenesis
    • J.M. Ebos, C.R. Lee, W. Cruz-Munoz, G.A. Bjarnason, J.G. Christensen, and R.S. Kerbel Accelerated metastasis after short-term treatment with a potent inhibitor of tumor angiogenesis Cancer Cell 15 2009 232 239
    • (2009) Cancer Cell , vol.15 , pp. 232-239
    • Ebos, J.M.1    Lee, C.R.2    Cruz-Munoz, W.3    Bjarnason, G.A.4    Christensen, J.G.5    Kerbel, R.S.6


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