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Volumn 15, Issue 3, 2010, Pages 901-912

Focal Adhesion Kinase and p53 signal transduction pathways in cancer

Author keywords

Apoptosis; Cancer; Focal adhesion kinase; Inhibitors; MDM 2; P53; Protein interaction; Review; Small molecules; Survival; Tumorigenesis

Indexed keywords

ANTINEOPLASTIC AGENT; FOCAL ADHESION KINASE; PROTEIN P53;

EID: 77956626576     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/3653     Document Type: Article
Times cited : (64)

References (115)
  • 2
    • 0027448821 scopus 로고
    • Expression of focal adhesion kinase gene and invasive cancer
    • DOI 10.1016/0140-6736(93)92881-S
    • T. M. Weiner, E. T. Liu, R. J. Craven and W. G. Cance: Expression of focal adhesion kinase gene and invasive cancer. Lancet, 342(8878), 1024-1025 (1993). (Pubitemid 23314806)
    • (1993) Lancet , vol.342 , Issue.8878 , pp. 1024-1025
    • Weiner, T.M.1    Liu, E.T.2    Craven, R.J.3    Cance, W.G.4
  • 4
    • 0029690892 scopus 로고    scopus 로고
    • Focal adhesion kinase as a marker of invasive potential in differentiated human thyroid cancer
    • L. V. Owens, L. Xu, G. A. Dent, X. Yang, G. C. Sturge, R. J. Craven and W. G. Cance: Focal adhesion kinase as a marker of invasive potential in differentiated human thyroid cancer. Annals of Surgical Oncology, 3(1), 100-105 (1996). (Pubitemid 126729497)
    • (1996) Annals of Surgical Oncology , vol.3 , Issue.1 , pp. 100-105
    • Owens, L.V.1    Xu, L.2    Dent, G.A.3    Yang, X.4    Sturge, G.C.5    Craven, R.J.6    Cance, W.G.7
  • 5
    • 0034044795 scopus 로고    scopus 로고
    • Immunohistochemical analyses of focal adhesion kinase expression in benign and malignant human breast and colon tissues: Correlation with preinvasive and invasive phenotypes
    • W. G. Cance, J. E. Harris, M. V. Iacocca, E. Roche, X. Yang, J. Chang, S. Simkins and L. Xu: Immunohistochemical analyses of focal adhesion kinase expression in benign and malignant human breast and colon tissues: correlation with preinvasive and invasive phenotypes. Clin Cancer Res, 6(6), 2417-2423. (2000). (Pubitemid 30399210)
    • (2000) Clinical Cancer Research , vol.6 , Issue.6 , pp. 2417-2423
    • Cance, W.G.1    Harris, J.E.2    Iacocca, M.V.3    Roche, E.4    Yang, X.H.5    Chang, J.6    Simkins, S.7    Xu, L.H.8
  • 6
    • 0033570076 scopus 로고    scopus 로고
    • Overexpression of focal adhesion kinase, a protein tyrosine kinase, in ovarian carcinoma
    • DOI 10.1002/(SICI)1097-0142(19991015)86:6<1551::AID-CNCR23>3.0. CO;2-P
    • P. L. Judson, X. He, W. G. Cance and L. Van Le: Overexpression of focal adhesion kinase, a protein tyrosine kinase, in ovarian carcinoma. Cancer, 86(8), 1551-1556 (1999). (Pubitemid 29489790)
    • (1999) Cancer , vol.86 , Issue.8 , pp. 1551-1556
    • Judson, P.L.1    He, X.2    Cance, W.G.3    Van Le, L.4
  • 7
    • 0037237066 scopus 로고    scopus 로고
    • Overexpression of focal adhesion kinase in primary colorectal carcinomas and colorectal liver metastases: Immunohistochemistry and real-time PCR analyses
    • A. L. Lark, C. A. Livasy, B. Calvo, L. Caskey, D. T. Moore, X. Yang and W. G. Cance: Overexpression of focal adhesion kinase in primary colorectal carcinomas and colorectal liver metastases: immunohistochemistry and real-time PCR analyses. Clin Cancer Res, 9(1), 215-222 (2003). (Pubitemid 36109736)
    • (2003) Clinical Cancer Research , vol.9 , Issue.1 , pp. 215-222
    • Lark, A.L.1    Livasy, C.A.2    Calvo, B.3    Caskey, L.4    Moore, D.T.5    Yang, X.6    Cance, W.G.7
  • 8
    • 9644275426 scopus 로고    scopus 로고
    • Upregulation of focal adhesion kinase (FAK) expression in ductal carcinoma in situ (DCIS) is an early event in breast tumorigenesis
    • DOI 10.1007/s10549-004-1022-8
    • H. M. Lightfoot, Jr., A. Lark, C. A. Livasy, D. T. Moore, D. Cowan, L. Dressler, R. J. Craven and W. G. Cance: Upregulation of focal adhesion kinase (FAK) expression in ductal carcinoma in situ (DCIS) is an early event in breast tumorigenesis. Breast Cancer Res Treat, 88(2), 109-116 (2004). (Pubitemid 39575569)
    • (2004) Breast Cancer Research and Treatment , vol.88 , Issue.2 , pp. 109-116
    • Lightfoot, H.M.1    Lark, A.2    Livasy, C.A.3    Moore, D.T.4    Cowan, D.5    Dressler, L.6    Craven, R.J.7    Cance, W.G.8
  • 9
    • 2942531163 scopus 로고    scopus 로고
    • Focal adhesion kinase suppresses apoptosis by binding to the death domain of receptor-interacting protein
    • DOI 10.1128/MCB.24.10.4361-4371.2004
    • E. Kurenova, L.-H. Xu, X. Yang, A. S. Baldwin Jr., R. J. Craven, S. K. Hanks, Z.-g. Liu and W. G. Cance: Focal Adhesion Kinase Suppresses Apoptosis by Binding to the Death Domain of Receptor-Interacting Protein. Mol. Cell. Biol., 24(10), 4361-4371 (2004). (Pubitemid 41071006)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.10 , pp. 4361-4371
    • Kurenova, E.1    Xu, L.-H.2    Yang, X.3    Baldwin Jr., A.S.4    Craven, R.J.5    Hanks, S.K.6    Liu, Z.-G.7    Cance, W.G.8
  • 10
    • 21644466387 scopus 로고    scopus 로고
    • Direct interaction of the N-terminal domain of focal adhesion kinase with the N-terminal transactivation domain of p53
    • DOI 10.1074/jbc.M414172200
    • V. M. Golubovskaya, R. Finch and W. G. Cance: Direct interaction of the N-terminal domain of focal adhesion kinase with the N-terminal transactivation domain of p53. J Biol Chem, 280(26), 25008-25021 (2005). (Pubitemid 40934593)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.26 , pp. 25008-25021
    • Golubovskaya, V.M.1    Finch, R.2    Cance, W.G.3
  • 11
    • 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, 103-153 (2007). (Pubitemid 47296394)
    • (2007) International Review of Cytology , vol.263 , pp. 103-153
    • Golubovskaya, V.M.1    Cance, W.G.2
  • 12
    • 48849112195 scopus 로고    scopus 로고
    • Focal adhesion kinase versus p53: Apoptosis or survival?
    • W. G. Cance and V. M. Golubovskaya: Focal Adhesion Kinase Versus p53: Apoptosis or Survival? Sci Signal, 1(20), pe22 (2008).
    • (2008) Sci Signal , vol.1 , Issue.20
    • Cance, W.G.1    Golubovskaya, V.M.2
  • 13
    • 2442583529 scopus 로고    scopus 로고
    • Cloning and characterization of the promoter region of human focal adhesion kinase gene: Nuclear factor kappa B and p53 binding sites
    • DOI 10.1016/j.bbaexp.2004.03.002, PII S0167478104000570
    • V. Golubovskaya, A. Kaur and W. Cance: Cloning and characterization of the promoter region of human focal adhesion kinase gene: nuclear factor kappa B and p53 binding sites*1. Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1678(2-3), 111-125 (2004). (Pubitemid 38626172)
    • (2004) Biochimica et Biophysica Acta - Gene Structure and Expression , vol.1678 , Issue.2-3 , pp. 111-125
    • Golubovskaya, V.1    Kaur, A.2    Cance, W.3
  • 15
    • 0029240425 scopus 로고
    • Mapping of the focal adhesion kinase (Fadk) gene to mouse chromosome 15 and human chromosome 8
    • F. T. Fiedorek, Jr. and E. S. Kay: Mapping of the focal adhesion kinase (Fadk) gene to mouse chromosome 15 and human chromosome 8. Mammalian Genome, 6(2), 123-126 (1995).
    • (1995) Mammalian Genome , vol.6 , Issue.2 , pp. 123-126
    • Fiedorek Jr., F.T.1    Kay, E.S.2
  • 16
    • 0033533746 scopus 로고    scopus 로고
    • Increased dosage and amplification of the focal adhesion kinase gene in human cancer cells
    • DOI 10.1038/sj.onc.1202957
    • M. Agochiya, V. G. Brunton, D. W. Owens, E. K. Parkinson, C. Paraskeva, W. N. Keith and M. C. Frame: Increased dosage and amplification of the focal adhesion kinase gene in human cancer cells Oncogene, 18(41), 5646-5653 (1999). (Pubitemid 29497599)
    • (1999) Oncogene , vol.18 , Issue.41 , pp. 5646-5653
    • Agochiya, M.1    Brunton, V.G.2    Owens, D.W.3    Parkinson, E.K.4    Paraskeva, C.5    Keith, W.N.6    Frame, M.C.7
  • 17
  • 18
    • 33748954120 scopus 로고    scopus 로고
    • Organization and post-transcriptional processing of focal adhesion kinase gene
    • J. M. Corsi, E. Rouer, J. A. Girault and H. Enslen: Organization and post-transcriptional processing of focal adhesion kinase gene. BMC Genomics, 7, 198 (2006).
    • (2006) BMC Genomics , vol.7 , pp. 198
    • Corsi, J.M.1    Rouer, E.2    Girault, J.A.3    Enslen, H.4
  • 19
    • 0031081425 scopus 로고    scopus 로고
    • Signaling through focal adhesion kinase
    • S. K. Hanks and T. R. Polte: Signaling through focal adhesion kinase. Bioessays, 19(2), 137-145 (1997). (Pubitemid 27114962)
    • (1997) BioEssays , vol.19 , Issue.2 , pp. 137-145
    • Hanks, S.K.1    Polte, T.R.2
  • 21
  • 22
    • 0029150292 scopus 로고
    • Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains
    • M. D. Schaller, C. A. Otey, J. D. Hildebrand and J. T. Parsons: Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains. Journal of Cell Biology, 130(5), 1181-1187 (1995).
    • (1995) Journal of Cell Biology , vol.130 , Issue.5 , pp. 1181-1187
    • Schaller, M.D.1    Otey, C.A.2    Hildebrand, J.D.3    Parsons, J.T.4
  • 24
    • 0242495710 scopus 로고    scopus 로고
    • Regulation of Focal Adhesion Kinase by Its Amino-Terminal Domain through an Autoinhibitory Interaction
    • DOI 10.1128/MCB.23.22.8030-8041.2003
    • L. A. Cooper, T. L. Shen and J. L. Guan: Regulation of focal adhesion kinase by its amino-terminal domain through an autoinhibitory interaction. Mol Cell Biol, 23(22), 8030-8041 (2003). (Pubitemid 37377496)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.22 , pp. 8030-8041
    • Cooper, L.A.1    Shen, T.-L.2    Guan, J.-L.3
  • 25
    • 34250026140 scopus 로고    scopus 로고
    • Structural Basis for the Autoinhibition of Focal Adhesion Kinase
    • DOI 10.1016/j.cell.2007.05.041, PII S0092867407006800
    • D. Lietha, X. Cai, D. F. Ceccarelli, Y. Li, M. D. Schaller and M. J. Eck: Structural basis for the autoinhibition of focal adhesion kinase. Cell, 129(6), 1177- 87 (2007). (Pubitemid 46891044)
    • (2007) Cell , vol.129 , Issue.6 , pp. 1177-1187
    • Lietha, D.1    Cai, X.2    Ceccarelli, D.F.J.3    Li, Y.4    Schaller, M.D.5    Eck, M.J.6
  • 27
    • 0032859988 scopus 로고    scopus 로고
    • Complex formation with focal adhesion kinase: A mechanism to regulate activity and subcellular localization of Src kinases
    • M. D. Schaller, J. D. Hildebrand and J. T. Parsons: Complex formation with focal adhesion kinase: A mechanism to regulate activity and subcellular localization of Src kinases. Mol Biol Cell, 10(10), 3489-3505 (1999). (Pubitemid 29489577)
    • (1999) Molecular Biology of the Cell , vol.10 , Issue.10 , pp. 3489-3505
    • Schaller, M.D.1    Hildebrand, J.D.2    Parsons, J.T.3
  • 28
    • 0142141199 scopus 로고    scopus 로고
    • Focal adhesion kinase signaling activities and their implications in the control of cell survival and motility
    • d870-1297
    • S. K. Hanks, L. Ryzhova, N. Y. Shin and J. Brabek: Focal adhesion kinase signaling activities and their implications in the control of cell survival and motility. Front Biosci, 8,d982-96 (2003). (Pubitemid 38943176)
    • (2003) Frontiers in Bioscience , vol.8
    • Hanks, S.K.1    Ryzhova, L.2    Shin, N.-Y.3    Brabek, J.4
  • 29
    • 0028877919 scopus 로고
    • Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: A role for Src family kinases
    • M. B. Calalb, T. R. Polte and S. K. Hanks: Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases. Molecular & Cellular Biology, 15(2), 954- 963 (1995).
    • (1995) Molecular & Cellular Biology , vol.15 , Issue.2 , pp. 954-963
    • Calalb, M.B.1    Polte, T.R.2    Hanks, S.K.3
  • 31
    • 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(Pt 8), 1409-16 (2003). (Pubitemid 36527488)
    • (2003) Journal of Cell Science , vol.116 , Issue.8 , pp. 1409-1416
    • Parsons, J.T.1
  • 32
    • 0037038686 scopus 로고    scopus 로고
    • Src activation regulates anoikis in human colon tumor cell lines
    • DOI 10.1038/sj.onc.1205989
    • T. C. Windham, N. U. Parikh, D. R. Siwak, J. M. Summy, D. J. McConkey, A. J. Kraker and G. E. Gallick: Src activation regulates anoikis in human colon tumor cell lines. Oncogene, 21(51), 7797-7807 (2002). (Pubitemid 35398837)
    • (2002) Oncogene , vol.21 , Issue.51 , pp. 7797-7807
    • Windham, T.C.1    Parikh, N.U.2    Siwak, D.R.3    Summy, J.M.4    McConkey, D.J.5    Kraker, A.J.6    Gallick, G.E.7
  • 33
    • 0029257377 scopus 로고
    • Signal transduction through integrins: A central role for focal adhesion kinase?
    • A. Richardson and J. T. Parsons: Signal transduction through integrins: a central role for focal adhesion kinase? Bioessays, 17(3), 229-236 (1995).
    • (1995) Bioessays , vol.17 , Issue.3 , pp. 229-236
    • Richardson, A.1    Parsons, J.T.2
  • 34
    • 0036172186 scopus 로고    scopus 로고
    • The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin
    • DOI 10.1038/nsb755
    • I. Hayashi, K. Vuori and R. C. Liddington: The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin. Nat Struct Biol, 9(2), 101-106 (2002). (Pubitemid 34132410)
    • (2002) Nature Structural Biology , vol.9 , Issue.2 , pp. 101-106
    • Hayashi, I.1    Vuori, K.2    Liddington, R.C.3
  • 35
    • 2342649951 scopus 로고    scopus 로고
    • The focal adhesion targeting domain of focal adhesion kinase contains a hinge region that modulates tyrosine 926 phosphorylation
    • DOI 10.1016/j.str.2004.02.028, PII S0969212604000978
    • K. C. Prutzman, G. Gao, M. L. King, V. V. Iyer, G. A. Mueller, M. D. Schaller and S. L. Campbell: The focal adhesion targeting domain of focal adhesion kinase contains a hinge region that modulates tyrosine 926 phosphorylation. Structure (Camb), 12(5), 881-891 (2004). (Pubitemid 38595776)
    • (2004) Structure , vol.12 , Issue.5 , pp. 881-891
    • Prutzman, K.C.1    Gao, G.2    King, M.L.3    Iyer, V.V.4    Mueller, G.A.5    Schaller, M.D.6    Campbell, S.L.7
  • 36
    • 0036118284 scopus 로고    scopus 로고
    • The structural basis of localization and signaling by the focal adhesion targeting domain
    • DOI 10.1016/S0969-2126(02)00717-7, PII S0969212602007177
    • S. T. Arold, M. K. Hoellerer and M. E. Noble: The structural basis of localization and signaling by the focal adhesion targeting domain. Structure, 10(3), 319-327 (2002). (Pubitemid 34230620)
    • (2002) Structure , vol.10 , Issue.3 , pp. 319-327
    • Arold, S.T.1    Hoellerer, M.K.2    Noble, M.E.M.3
  • 37
    • 0029739950 scopus 로고    scopus 로고
    • Control of adhesion-dependent cell survival by focal adhesion kinase
    • S. M. Frisch, K. Vuori, E. Ruoslahti and P. Y. Chan- Hui: Control of adhesion-dependent cell survival by focal adhesion kinase. Journal of Cell Biology, 134(3), 793-9 (1996). (Pubitemid 26269148)
    • (1996) Journal of Cell Biology , vol.134 , Issue.3 , pp. 793-799
    • Frisch, S.M.1    Vuori, K.2    Ruoslahti, E.3    Chan-Hui, P.-Y.4
  • 40
    • 0033598202 scopus 로고    scopus 로고
    • Evidence for a function of death-receptor-related, death-domain- containing proteins in anoikis
    • DOI 10.1016/S0960-9822(99)80455-2
    • S. M. Frisch: Evidence for a function of deathreceptor- related, death-domain-containing proteins in anoikis. Curr Biol, 9(18), 1047-1049 (1999). (Pubitemid 29456175)
    • (1999) Current Biology , vol.9 , Issue.18 , pp. 1047-1049
    • Frisch, S.M.1
  • 42
    • 27644545721 scopus 로고    scopus 로고
    • Effect of focal adhesion kinase (FAK) downregulation with FAK antisense oligonucleotides and 5-fluorouracil on the viability of melanoma cell lines
    • DOI 10.1097/00008390-200510000-00003
    • C. S. Smith, V. M. Golubovskaya, E. Peck, L. H. Xu, B. P. Monia, X. Yang and W. G. Cance: Effect of focal adhesion kinase (FAK) downregulation with FAK antisense oligonucleotides and 5-fluorouracil on the viability of melanoma cell lines. Melanoma Res, 15(5), 357-362 (2005). (Pubitemid 41558945)
    • (2005) Melanoma Research , vol.15 , Issue.5 , pp. 357-362
    • Smith, C.S.1    Golubovskaya, V.M.2    Peck, E.3    Xu, L.-H.4    Monia, B.P.5    Yang, X.6    Cance, W.G.7
  • 43
    • 0032443850 scopus 로고    scopus 로고
    • The COOH-terminal domain of the focal adhesion kinase induces loss of adhesion and cell death in human tumor cells
    • L. H. Xu, X. Yang, R. J. Craven and W. G. Cance: The COOH-terminal domain of the focal adhesion kinase induces loss of adhesion and cell death in human tumor cells. Cell Growth Differ, 9(12), 999-1005 (1998). (Pubitemid 29036194)
    • (1998) Cell Growth and Differentiation , vol.9 , Issue.12 , pp. 999-1005
    • Xu, L.-H.1    Yang, X.2    Craven, R.J.3    Cance, W.G.4
  • 44
    • 0034730632 scopus 로고    scopus 로고
    • The focal adhesion kinase suppresses transformation-associated, anchorage-Independent apoptosis in human breast cancer cells
    • L.-h. Xu, X.-h. Yang, C. A. Bradham, D. A. Brenner, A. S. Baldwin, R. J. Craven and W. G. Cance: The focal adhesion kinase suppresses transformation-associated, anchorage-Independent apoptosis in human breast cancer cells. J. Biol. Chem., 275, 30597-30604 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 30597-30604
    • Xu, L.-H.1    Yang, X.-H.2    Bradham, C.A.3    Brenner, D.A.4    Baldwin, A.S.5    Craven, R.J.6    Cance, W.G.7
  • 45
    • 0037064030 scopus 로고    scopus 로고
    • Dual inhibition of focal adhesion kinase and epidermal growth factor receptor pathways cooperatively induces death receptor-mediated apoptosis in human breast cancer cells
    • DOI 10.1074/jbc.M205002200
    • V. Golubovskaya, L. Beviglia, L. H. Xu, H. S. Earp,3rd, R. Craven and W. Cance: Dual inhibition of focal adhesion kinase and epidermal growth factor receptor pathways cooperatively induces death receptor-mediated apoptosis in human breast cancer cells. J Biol Chem, 277(41), 38978-38987 (2002). (Pubitemid 35154764)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.41 , pp. 38978-38987
    • Golubovskaya, V.1    Beviglia, L.2    Xu, L.-H.3    Shelton Earp III, H.4    Craven, R.5    Cance, W.6
  • 46
    • 0041426730 scopus 로고    scopus 로고
    • Simultaneous inhibition of focal adhesion kinase and Src enhances detachment and apoptosis in colon cancer cell lines
    • V. M. Golubovskaya, S. Gross, A. S. Kaur, R. I. Wilson, L. H. Xu, X. H. Yang and W. G. Cance: Simultaneous inhibition of focal adhesion kinase and SRC enhances detachment and apoptosis in colon cancer cell lines. Mol Cancer Res, 1(10), 755-764 (2003). (Pubitemid 37025594)
    • (2003) Molecular Cancer Research , vol.1 , Issue.10 , pp. 755-764
    • Golubovskaya, V.M.1    Gross, S.2    Kaur, A.S.3    Wilson, R.I.4    Xu, L.-H.5    Yang, X.H.6    Cance, W.G.7
  • 47
    • 0038005805 scopus 로고    scopus 로고
    • Focal adhesion kinase N-terminus in breast carcinoma cells induces rounding, detachment and apoptosis
    • DOI 10.1042/BJ20021846
    • L. Beviglia, V. Golubovskaya, L. Xu, X. Yang, R. J. Craven and W. G. Cance: Focal adhesion kinase Nterminus in breast carcinoma cells induces rounding, detachment and apoptosis. Biochem J, 373(Pt 1), 201-210 (2003). (Pubitemid 36819515)
    • (2003) Biochemical Journal , vol.373 , Issue.1 , pp. 201-210
    • Beviglia, L.1    Golubovskaya, V.2    Xu, L.3    Yang, X.4    Craven, R.J.5    Cance, W.G.6
  • 48
    • 0035965234 scopus 로고    scopus 로고
    • Suppression of chemically induced apoptosis but not necrosis of renal proximal tubular epithelial (LLC-PK1) cells by focal adhesion kinase (FAK). Role of FAK in maintaining focal adhesion organization after acute renal cell injury
    • B. van De Water, F. Houtepen, M. Huigsloot and I. B. Tijdens: Suppression of chemically induced apoptosis but not necrosis of renal proximal tubular epithelial (LLC-PK1) cells by focal adhesion kinase (FAK). Role of FAK in maintaining focal adhesion organization after acute renal cell injury. J Biol Chem, 276(39), 36183-36193 (2001).
    • (2001) J Biol Chem , vol.276 , Issue.39 , pp. 36183-36193
    • Van De Water, B.1    Houtepen, F.2    Huigsloot, M.3    Tijdens, I.B.4
  • 49
    • 0038048222 scopus 로고    scopus 로고
    • FAK regulates biological processes important for the pathogenesis of cancer
    • DOI 10.1023/A:1023725029589
    • V. Gabarra-Niecko, M. D. Schaller and J. M. Dunty: FAK regulates biological processes important for the pathogenesis of cancer. Cancer Metastasis Rev, 22(4), 359- 74 (2003). (Pubitemid 36791892)
    • (2003) Cancer and Metastasis Reviews , vol.22 , Issue.4 , pp. 359-374
    • Gabarra-Niecko, V.1    Schaller, M.D.2    Dunty, J.M.3
  • 50
    • 1642302311 scopus 로고    scopus 로고
    • Activated Src increases adhesion, survival and α2-integrin expression in human breast cancer cells
    • DOI 10.1042/BJ20031392
    • H. B. Park, V. Golubovskaya, L. Xu, X. Yang, J. W. Lee, S. Scully, 2nd, R. J. Craven and W. G. Cance: Activated Src increases adhesion, survival and alpha2- integrin expression in human breast cancer cells. Biochem J, 378(Pt 2), 559-567 (2004). (Pubitemid 38367245)
    • (2004) Biochemical Journal , vol.378 , Issue.2 , pp. 559-567
    • Park, H.B.1    Golubovskaya, V.2    Xu, L.3    Yang, X.4    Lee, J.W.5    Scully II, S.6    Craven, R.J.7    Cance, W.G.8
  • 51
    • 0034717285 scopus 로고    scopus 로고
    • Anti-apoptotic role of focal adhesion kinase (FAK): Induction of inhibitor-of-apoptosis proteins and apoptosis suppression by the overexpression of FAK in a human leukemic cell line, HL-60
    • DOI 10.1074/jbc.275.21.16309
    • Y. Sonoda, Y. Matsumoto, M. Funakoshi, D. Yamamoto, S. K. Hanks and T. Kasahara: Anti-apoptotic Role of Focal Adhesion Kinase (FAK). Induction of inhibitor-of-apoptosis proteins and apoptosis suppression by the overexpression of fak in a human leukemic cell line, HL-60. J Biol Chem, 275(21), 16309-16315 (2000). (Pubitemid 30366946)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.21 , pp. 16309-16315
    • Sonoda, Y.1    Matsumoto, Y.2    Funakoshi, M.3    Yamamoto, D.4    Hanks, S.K.5    Kasahara, T.6
  • 53
    • 0012430640 scopus 로고    scopus 로고
    • Activated c-Src rescues cell rounding and loss of adhesion caused by attenuation of the focal adhesion kinase in human breast cancer cells
    • H. B. Park, L.-H. Xu, X. Yang and W. G. Cance: Activated c-Src rescues cell rounding and loss of adhesion caused by attenuation of the focal adhesion kinase in human breast cancer cells. Surg. Forum, L, 346-7 (1999).
    • (1999) Surg. Forum , vol.50 , pp. 346-347
    • Park, H.B.1    Xu, L.-H.2    Yang, X.3    Cance, W.G.4
  • 54
    • 0842281489 scopus 로고    scopus 로고
    • Multiple connections link FAK to cell motility and invasion
    • DOI 10.1016/j.gde.2003.12.002
    • D. D. Schlaepfer and S. K. Mitra: Multiple connections link FAK to cell motility and invasion. Curr Opin Genet Dev, 14(1), 92-101 (2004). (Pubitemid 38167483)
    • (2004) Current Opinion in Genetics and Development , vol.14 , Issue.1 , pp. 92-101
    • Schlaepfer, D.D.1    Mitra, S.K.2
  • 55
    • 0035948579 scopus 로고    scopus 로고
    • Biochemical signals and biological responses elicited by the focal adhesion kinase
    • DOI 10.1016/S0167-4889(01)00123-9, PII S0167488901001239
    • M. D. Schaller: Biochemical signals and biological responses elicited by the focal adhesion kinase. Biochim Biophys Acta, 1540(1), 1-21 (2001). (Pubitemid 32710044)
    • (2001) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1540 , Issue.1 , pp. 1-21
    • Schaller, M.D.1
  • 56
    • 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(19), 7079-90 (2001). (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
  • 58
    • 0032820782 scopus 로고    scopus 로고
    • Required role of focal adhesion kinase (FAK) for integrin-stimulated cell migration
    • D. J. Sieg, C. R. Hauck and D. D. Schlaepfer: Required role of focal adhesion kinase (FAK) for integrin-stimulated cell migration. J Cell Sci, 112(Pt), 2677-2691 (1999). (Pubitemid 29429791)
    • (1999) Journal of Cell Science , vol.112 , Issue.16 , pp. 2677-2691
    • Sieg, D.J.1    Hauck, C.R.2    Schlaepfer, D.D.3
  • 59
    • 0027428367 scopus 로고
    • Identification of sequences required for the efficient localization of the Focal Adhesion Kinase, pp125(FAK), to cellular focal adhesions
    • DOI 10.1083/jcb.123.4.993
    • J. D. Hildebrand, M. D. Schaller and J. T. Parsons: Identification of sequences required for the efficient localization of the focal adhesion kinase, pp125FAK, to cellular focal adhesions. Journal of Cell Biology, 123(4), 993-1005 (1993). (Pubitemid 23333585)
    • (1993) Journal of Cell Biology , vol.123 , Issue.4 , pp. 993-1005
    • Hildebrand, J.D.1    Schaller, M.D.2    Parsons, J.T.3
  • 61
    • 33745049204 scopus 로고    scopus 로고
    • Src SH2 arginine 175 is required for cell motility: Specific focal adhesion kinase targeting and focal adhesion assembly function
    • DOI 10.1128/MCB.01147-05
    • M. G. Yeo, M. A. Partridge, E. J. Ezratty, Q. Shen, G. G. Gundersen and E. E. Marcantonio: Src SH2 arginine 175 is required for cell motility: specific focal adhesion kinase targeting and focal adhesion assembly function. Mol Cell Biol, 26(12), 4399-4409 (2006). (Pubitemid 43877562)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.12 , pp. 4399-4409
    • Yeo, M.G.1    Partridge, M.A.2    Ezratty, E.J.3    Shen, Q.4    Gundersen, G.G.5    Marcantonio, E.E.6
  • 62
    • 0033617357 scopus 로고    scopus 로고
    • Requirement of phosphatidylinositol 3-kinase in focal adhesion kinasepromoted cell migration
    • H. R. Reiske, S. C. Kao, L. A. Cary, J. L. Guan, J. F. Lai and H. C. Chen: Requirement of phosphatidylinositol 3-kinase in focal adhesion kinasepromoted cell migration. J Biol Chem, 274(18), 12361- 12366 (1999).
    • (1999) J Biol Chem , vol.274 , Issue.18 , pp. 12361-12366
    • Reiske, H.R.1    Kao, S.C.2    Cary, L.A.3    Guan, J.L.4    Lai, J.F.5    Chen, H.C.6
  • 63
    • 0032486198 scopus 로고    scopus 로고
    • Inhibition of cell migration, spreading, and focal adhesions by tumor suppressor PTEN
    • DOI 10.1126/science.280.5369.1614
    • M. Tamura, J. Gu, K. Matsumoto, S. Aota, R. Parsons and K. M. Yamada: Inhibition of cell migration, spreading, and focal adhesions by tumor suppressor PTEN. Science, 280(5369), 1614-1617 (1998). (Pubitemid 28277707)
    • (1998) Science , vol.280 , Issue.5369 , pp. 1614-1617
    • Tamura, M.1    Gu, J.2    Matsumoto, K.3    Aota, S.-I.4    Parsons, R.5    Yamada, K.M.6
  • 64
    • 0033575287 scopus 로고    scopus 로고
    • PTEN interactions with focal adhesion kinase and suppression of the extracellular matrix-dependent phosphatidylinositol 3-kinase/Akt cell survival pathway
    • M. Tamura, J. Gu, E. H. Danen, T. Takino, S. Miyamoto and K. M. Yamada: PTEN interactions with focal adhesion kinase and suppression of the extracellular matrix-dependent phosphatidylinositol 3-kinase/Akt cell survival pathway. J Biol Chem, 274(29), 20693-703 (1999).
    • (1999) J Biol Chem , vol.274 , Issue.29 , pp. 20693-20703
    • Tamura, M.1    Gu, J.2    Danen, E.H.3    Takino, T.4    Miyamoto, S.5    Yamada, K.M.6
  • 65
    • 27744458852 scopus 로고    scopus 로고
    • FAK signaling is critical for ErbB-2/ErbB-3 receptor cooperation for oncogenic transformation and invasion
    • DOI 10.1083/jcb.200504124
    • N. Benlimame, Q. He, S. Jie, D. Xiao, Y. J. Xu, M. Loignon, D. D. Schlaepfer and M. A. Alaoui-Jamali: FAK signaling is critical for ErbB-2/ErbB-3 receptor cooperation for oncogenic transformation and invasion. J Cell Biol, 171(3), 505-516 (2005). (Pubitemid 41586939)
    • (2005) Journal of Cell Biology , vol.171 , Issue.3 , pp. 505-516
    • Benlimame, N.1    He, Q.2    Jie, S.3    Xiao, D.4    Ying, J.X.5    Loignon, M.6    Schlaepfer, D.D.7    Alaoui-Jamali, M.A.8
  • 68
    • 8644263977 scopus 로고    scopus 로고
    • Overexpression of focal adhesion kinase in vascular endothelial cells promotes angiogenesis in transgenic mice
    • DOI 10.1016/j.cardiores.2004.07.012, PII S0008636304003281
    • X. Peng, H. Ueda, H. Zhou, T. Stokol, T. L. Shen, A. Alcaraz, T. Nagy, J. D. Vassalli and J. L. Guan: Overexpression of focal adhesion kinase in vascular endothelial cells promotes angiogenesis in transgenic mice. Cardiovasc Res, 64(3), 421-430 (2004). (Pubitemid 39505421)
    • (2004) Cardiovascular Research , vol.64 , Issue.3 , pp. 421-430
    • Peng, X.1    Ueda, H.2    Zhou, H.3    Stokol, T.4    Shen, T.-L.5    Alcaraz, A.6    Nagy, T.7    Vassalli, J.-D.8    Guan, J.-L.9
  • 71
    • 33748286819 scopus 로고    scopus 로고
    • Integrin-regulated FAK-Src signaling in normal and cancer cells
    • DOI 10.1016/j.ceb.2006.08.011, PII S0955067406001220
    • S. K. Mitra and D. D. Schlaepfer: Integrin-regulated FAK-Src signaling in normal and cancer cells. Curr Opin Cell Biol 18, 516-523 (2006). (Pubitemid 44332916)
    • (2006) Current Opinion in Cell Biology , vol.18 , Issue.5 , pp. 516-523
    • Mitra, S.K.1    Schlaepfer, D.D.2
  • 72
    • 0032547796 scopus 로고    scopus 로고
    • Extracellular matrix survival signals transduced by focal adhesion kinase suppress p53-mediated apoptosis
    • DOI 10.1083/jcb.143.2.547
    • D. Ilic, E. A. Almeida, D. D. Schlaepfer, P. Dazin, S. Aizawa and C. H. Damsky: Extracellular matrix survival signals transduced by focal adhesion kinase suppress p53- mediated apoptosis. J Cell Biol, 143(2), 547-560 (1998). (Pubitemid 28487870)
    • (1998) Journal of Cell Biology , vol.143 , Issue.2 , pp. 547-560
    • Ilic, D.1    Almeida, E.A.C.2    Schlaepfer, D.D.3    Dazin, P.4    Aizawa, S.5    Damsky, C.H.6
  • 74
    • 0030941458 scopus 로고    scopus 로고
    • P53, the cellular gatekeeper for growth and division
    • DOI 10.1016/S0092-8674(00)81871-1
    • A. J. Levine: p53, the cellular gatekeeper for growth and division. Cell, 88(3), 323-31 (1997). (Pubitemid 27131374)
    • (1997) Cell , vol.88 , Issue.3 , pp. 323-331
    • Levine, A.J.1
  • 80
    • 0036625964 scopus 로고    scopus 로고
    • The promise and obstacle of p53 as a cancer therapeutic agent
    • DOI 10.2174/1566524023362474
    • A. C. Willis and X. Chen: The promise and obstacle of p53 as a cancer therapeutic agent. Curr Mol Med, 2(4), 329- 345 (2002). (Pubitemid 35452883)
    • (2002) Current Molecular Medicine , vol.2 , Issue.4 , pp. 329-345
    • Willis, A.C.1    Chen, X.2
  • 81
    • 1542646380 scopus 로고    scopus 로고
    • Restoring p53-dependent tumor suppression
    • W. Wang, F. Rastinejad and W. S. El-Deiry: Restoring p53-dependent tumor suppression. Cancer Biol Ther, 2(4 Suppl 1), S55-63 (2003).
    • (2003) Cancer Biol Ther , vol.2 , Issue.4 SUPPL. 1
    • Wang, W.1    Rastinejad, F.2    El-Deiry, W.S.3
  • 82
    • 0025312728 scopus 로고
    • A genetic model for colorectal tumorigenesis
    • E. R. Fearon and B. Vogelstein: A genetic model for colorectal tumorigenesis. Cell, 61(5), 759-767 (1990).
    • (1990) Cell , vol.61 , Issue.5 , pp. 759-767
    • Fearon, E.R.1    Vogelstein, B.2
  • 83
    • 0032192140 scopus 로고    scopus 로고
    • The complexity of p53 modulation: Emerging patterns from divergent signals
    • A. J. Giaccia and M. B. Kastan: The complexity of p53 modulation: emerging patterns from divergent signals. Genes Dev, 12(19), 2973-2983 (1998). (Pubitemid 28469299)
    • (1998) Genes and Development , vol.12 , Issue.19 , pp. 2973-2983
    • Giaccia, A.J.1    Kastan, M.B.2
  • 84
    • 0036479115 scopus 로고    scopus 로고
    • Transcriptional repression of the anti-apoptotic survivin gene by wild type p53
    • DOI 10.1074/jbc.M106643200
    • W. H. Hoffman, S. Biade, J. T. Zilfou, J. Chen and M. Murphy: Transcriptional repression of the anti-apoptotic survivin gene by wild type p53. J Biol Chem, 277(5), 3247- 3257 (2002). (Pubitemid 34953189)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.5 , pp. 3247-3257
    • Hoffman, W.H.1    Biade, S.2    Zilfou, J.T.3    Chen, J.4    Murphy, M.5
  • 85
    • 0035843156 scopus 로고    scopus 로고
    • Negative regulation of bcl-2 expression by p53 in hematopoietic cells
    • DOI 10.1038/sj.onc.1204067
    • Y. Wu, J. W. Mehew, C. A. Heckman, M. Arcinas and L. M. Boxer: Negative regulation of bcl-2 expression by p53 in hematopoietic cells. Oncogene, 20(2), 240-251 (2001). (Pubitemid 32150269)
    • (2001) Oncogene , vol.20 , Issue.2 , pp. 240-251
    • Wu, Y.1    Mehew, J.W.2    Heckman, C.A.3    Arcinas, M.4    Boxer, L.M.5
  • 86
    • 0035810054 scopus 로고    scopus 로고
    • Regulation of the G2/M transition by p53
    • DOI 10.1038/sj.onc.1204252
    • W. R. Taylor and G. R. Stark: Regulation of the G2/M transition by p53. Oncogene, 20(15), 1803-1815 (2001). (Pubitemid 32458690)
    • (2001) Oncogene , vol.20 , Issue.15 , pp. 1803-1815
    • Taylor, W.R.1    Stark, G.R.2
  • 89
    • 0029803281 scopus 로고    scopus 로고
    • Wild-type p53 negatively regulates the expression of a microtubule- associated protein
    • M. Murphy, A. Hinman and A. J. Levine: Wild-type p53 negatively regulates the expression of a microtubuleassociated protein. Genes Dev, 10(23), 2971-2980 (1996). (Pubitemid 26412524)
    • (1996) Genes and Development , vol.10 , Issue.23 , pp. 2971-2980
    • Murphy, M.1    Hinman, A.2    Levine, A.J.3
  • 92
    • 0036433351 scopus 로고    scopus 로고
    • The focal adhesion kinase amino-terminal domain localises to nuclei and intercellular junctions in HEK 293 and MDCK cells independently of tyrosine 397 and the carboxy-terminal domain
    • DOI 10.1016/S0006-291X(02)02547-0, PII S0006291X02025470
    • A. Stewart, C. Ham and I. Zachary: The focal adhesion kinase amino-terminal domain localises to nuclei and intercellular junctions in HEK 293 and MDCK cells independently of tyrosine 397 and the carboxy-terminal domain. Biochem Biophys Res Commun, 299(1), 62-73 (2002). (Pubitemid 35366036)
    • (2002) Biochemical and Biophysical Research Communications , vol.299 , Issue.1 , pp. 62-73
    • Stewart, A.1    Ham, C.2    Zachary, I.3
  • 93
    • 0347356250 scopus 로고    scopus 로고
    • Nuclear import of N-terminal FAK by activation of the FcεRI receptor in RBL-2H3 cells
    • DOI 10.1016/j.bbrc.2003.12.055
    • G. Jones and G. Stewart: Nuclear import of N-terminal FAK by activation of the FcepsilonRI receptor in RBL-2H3 cells. Biochem Biophys Res Commun, 314(1), 39-45 (2004). (Pubitemid 38058366)
    • (2004) Biochemical and Biophysical Research Communications , vol.314 , Issue.1 , pp. 39-45
    • Jones, G.1    Stewart, G.2
  • 94
    • 0034610067 scopus 로고    scopus 로고
    • Nuclear localization and apoptotic regulation of an amino-terminal domain focal adhesion kinase fragment in endothelial cells
    • M. Lobo and I. Zachary: Nuclear localization and apoptotic regulation of an amino-terminal domain focal adhesion kinase fragment in endothelial cells. Biochem Biophys Res Commun, 276(3), 1068-1074 (2000).
    • (2000) Biochem Biophys Res Commun , vol.276 , Issue.3 , pp. 1068-1074
    • Lobo, M.1    Zachary, I.2
  • 95
    • 4644250606 scopus 로고    scopus 로고
    • Cytoplasmic p53: Bax and forward
    • J. E. Chipuk and D. R. Green: Cytoplasmic p53: Bax and Forward. Cell Cycle, 3(4), 429-431 (2004). (Pubitemid 40278229)
    • (2004) Cell Cycle , vol.3 , Issue.4 , pp. 429-431
    • Chipuk, J.E.1    Green, D.R.2
  • 96
    • 41649107660 scopus 로고    scopus 로고
    • The 7-amino-acid site in the proline-rich region of the N-terminal domain of p53 is involved in the interaction with FAK and is critical for p53 functioning
    • DOI 10.1042/BJ20071657
    • V. Golubovskaya, R. Finch, M. Zheng, E. V. Kurenova and W. G. Cance: The 7 amino-acid site in the proline-rich region of the N-terminal domain of p53 is involved in interaction with FAK and is critical for p53 functioning. Biochem J, 411, 151-160, (2008). (Pubitemid 351482357)
    • (2008) Biochemical Journal , vol.411 , Issue.1 , pp. 151-160
    • Golubovskaya, V.M.1    Finch, R.2    Zheng, M.3    Kurenova, E.V.4    Cance, W.G.5
  • 97
    • 14944377114 scopus 로고    scopus 로고
    • Functional analysis of focal adhesion kinase (FAK) reduction by small inhibitory RNAs
    • E. K. Han, T. McGonigal, J. Wang, V. L. Giranda and Y. Luo: Functional analysis of focal adhesion kinase (FAK) reduction by small inhibitory RNAs. Anticancer Res, 24(6), 3899-3905 (2004). (Pubitemid 40468683)
    • (2004) Anticancer Research , vol.24 , Issue.6 , pp. 3899-3905
    • Han, E.K.-H.1    McGonigal, T.2    Wang, J.3    Giranda, V.L.4    Luo, Y.5
  • 100
    • 41649106314 scopus 로고    scopus 로고
    • TAE226-Induced apoptosis in breast cancer cells with overexpressed Src or EGFR
    • V. M. Golubovskaya, C. Virnig and W. G. Cance: TAE226-Induced apoptosis in breast cancer cells with overexpressed Src or EGFR. Mol Carcinog 46(6), 488-96 (2007).
    • (2007) Mol Carcinog , vol.46 , Issue.6 , pp. 488-496
    • Golubovskaya, V.M.1    Virnig, C.2    Cance, W.G.3
  • 102
    • 46949105858 scopus 로고    scopus 로고
    • FAK and IGF-IR interact to provide survival signals in human pancreatic adenocarcinoma cells
    • DOI 10.1093/carcin/bgn026
    • W. Liu, D. A. Bloom, W. G. Cance, E. V. Kurenova, V. M. Golubovskaya and S. N. Hochwald: Fak And Igf-Ir Interact To Provide Survival Signals In Human Pancreatic Adenocarcinoma Cells. Carcinogenesis 29(6), 1096-107 (2008). (Pubitemid 351958687)
    • (2008) Carcinogenesis , vol.29 , Issue.6 , pp. 1096-1107
    • Liu, W.1    Bloom, D.A.2    Cance, W.G.3    Kurenova, E.V.4    Golubovskaya, V.M.5    Hochwald, S.N.6
  • 105
    • 43049114924 scopus 로고    scopus 로고
    • Dual focal adhesion kinase/Pyk2 inhibitor has positive effects on bone tumors: Implications for bone metastases
    • DOI 10.1002/cncr.23429
    • C. M. Bagi, G. W. Roberts and C. J. Andresen: Dual focal adhesion kinase/Pyk2 inhibitor has positive effects on bone tumors: implications for bone metastases. Cancer, 112(10), 2313-21 (2008). (Pubitemid 351628644)
    • (2008) Cancer , vol.112 , Issue.10 , pp. 2313-2321
    • Bagi, C.M.1    Roberts, G.W.2    Andresen, C.J.3
  • 106
    • 22244443786 scopus 로고    scopus 로고
    • P53 activation by small molecules: Application in oncology
    • DOI 10.1021/jm058174k
    • L. T. Vassilev: p53 Activation by small molecules: application in oncology. J Med Chem, 48(14), 4491-4499 (2005). (Pubitemid 40993409)
    • (2005) Journal of Medicinal Chemistry , vol.48 , Issue.14 , pp. 4491-4499
    • Vassilev, L.T.1
  • 107
    • 0032562289 scopus 로고    scopus 로고
    • Targeting the receptor-G(q) interface to inhibit in vivo pressure overload myocardial hypertrophy
    • DOI 10.1126/science.280.5363.574
    • S. A. Akhter, L. M. Luttrell, H. A. Rockman, G. Iaccarino, R. J. Lefkowitz and W. J. Koch: Targeting the receptor-Gq interface to inhibit in vivo pressure overload myocardial hypertrophy. Science, 280(5363), 574-577 (1998). (Pubitemid 28227758)
    • (1998) Science , vol.280 , Issue.5363 , pp. 574-577
    • Akhter, S.A.1    Luttrell, L.M.2    Rockman, H.A.3    Iaccarino, G.4    Lefkowitz, R.J.5    Koch, W.J.6
  • 108
    • 0032849010 scopus 로고    scopus 로고
    • Affinity-driven peptide selection of an NFAT inhibitor more selective than cyclosporin A
    • DOI 10.1126/science.285.5436.2129
    • J. Aramburu, M. B. Yaffe, C. Lopez-Rodriguez, L. C. Cantley, P. G. Hogan and A. Rao: Affinity-driven peptide selection of an NFAT inhibitor more selective than cyclosporin A. Science, 285(5436), 2129-33 (1999). (Pubitemid 29451431)
    • (1999) Science , vol.285 , Issue.5436 , pp. 2129-2133
    • Aramburu, J.1    Yaffe, M.B.2    Lopez-Rodriguez, C.3    Cantley, L.C.4    Hogan, P.G.5    Rao, A.6
  • 109
    • 0034284715 scopus 로고    scopus 로고
    • Selective inhibition of NFkappaB activation by a peptide that blocks the interaction of NEMO with the IkappaB kinase complex
    • M. J. May, F. D'Acquisto, L. A. Madge, J. Glockner, J. S. Pober and S. Ghosh: Selective inhibition of NFkappaB activation by a peptide that blocks the interaction of NEMO with the IkappaB kinase complex. Science, 289(5484), 1550-1554 (2000).
    • (2000) Science , vol.289 , Issue.5484 , pp. 1550-1554
    • May, M.J.1    D'acquisto, F.2    Madge, L.A.3    Glockner, J.4    Pober, J.S.5    Ghosh, S.6
  • 110
    • 79959731151 scopus 로고    scopus 로고
    • E. van Rooij, P. A. Doevendans, C. C. de Theije, F. A. Babiker, J. D. Molkentin and L. J. de Windt: Requirement of nuclear factor of
    • E. van Rooij, P. A. Doevendans, C. C. de Theije, F. A. Babiker, J. D. Molkentin and L. J. de Windt: Requirement of nuclear factor of.
  • 112
    • 0037174635 scopus 로고    scopus 로고
    • Treatment of ischemic brain damage by perturbing NMDA receptor-PSD-95 protein interactions
    • DOI 10.1126/science.1072873
    • M. Aarts, Y. Liu, L. Liu, S. Besshoh, M. Arundine, J. W. Gurd, Y. T. Wang, M. W. Salter and M. Tymianski: Treatment of ischemic brain damage by perturbing NMDA receptor- PSD-95 protein interactions. Science, 298(5594), 846-850 (2002). (Pubitemid 35231541)
    • (2002) Science , vol.298 , Issue.5594 , pp. 846-850
    • Aarts, M.1    Liu, Y.2    Liu, L.3    Besshoh, S.4    Arundine, M.5    Gurd, J.W.6    Wang, Y.-T.7    Salter, M.W.8    Tymianski, M.9
  • 113
    • 79959708481 scopus 로고    scopus 로고
    • PYK2 inhibition of p53 as an adaptive and intrinsic mechanism facilitating cell proliferation and survival
    • Epub ahead of print
    • S. T. Lim, N. L. Miller, J. O. Nam, X. L. Chen, Y. Lim and D. D. Schlaepfer: PYK2 inhibition of p53 as an adaptive and intrinsic mechanism facilitating cell proliferation and survival. J Biol Chem (2009) [Epub ahead of print].
    • (2009) J Biol Chem
    • Lim, S.T.1    Miller, N.L.2    Nam, J.O.3    Chen, X.L.4    Lim, Y.5    Schlaepfer, D.D.6
  • 114
    • 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(23), 7405-7416 (2008).
    • (2008) J Med Chem , vol.51 , Issue.23 , 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


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