메뉴 건너뛰기




Volumn 57, Issue 8, 2009, Pages 842-848

Particularly interesting cysteine- and histidine-rich protein in cardiac development and remodeling

Author keywords

Cardiomyopathy; Focal adhesion; Myocardial remodeling; Neural crest; PINCH

Indexed keywords

CELL PROTEIN; CYSTEINE; HISTIDINE; INTEGRIN; LIM PROTEIN; PROTEIN PINCH 1; UNCLASSIFIED DRUG;

EID: 74249119019     PISSN: 17088267     EISSN: None     Source Type: Journal    
DOI: 10.2310/JIM.0b013e3181c5e31d     Document Type: Conference Paper
Times cited : (9)

References (95)
  • 1
    • 24344442980 scopus 로고    scopus 로고
    • N(i)ck and the ILK: Network wiring at cell-matrix adhesions
    • Wu C. PINCH, N(i)ck and the ILK: network wiring at cell-matrix adhesions. Trends Cell Biol. 2005;15:460-466.
    • (2005) Trends Cell Biol. , vol.15 , pp. 460-466
    • Pinch, W.C.1
  • 3
    • 0345803932 scopus 로고    scopus 로고
    • PINCH-1 is an obligate partner of integrin-linked kinase (ILK) functioning in cell shape modulation, motility, and survival
    • Fukuda T, Chen K, Shi X, et al. PINCH-1 is an obligate partner of integrin-linked kinase (ILK) functioning in cell shape modulation, motility, and survival. J Biol Chem. 2003;278:51324-51333.
    • (2003) J Biol Chem. , vol.278 , pp. 51324-51333
    • Fukuda, T.1    Chen, K.2    Shi, X.3
  • 4
    • 4744340477 scopus 로고    scopus 로고
    • Distinct roles of two structurally closely related focal adhesion proteins, alpha-parvins and beta-parvins, in regulation of cell morphology and survival
    • Zhang Y, Chen K, Tu Y, et al. Distinct roles of two structurally closely related focal adhesion proteins, alpha-parvins and beta-parvins, in regulation of cell morphology and survival. J Biol Chem. 2004;279: 41695-41705.
    • (2004) J Biol Chem. , vol.279 , pp. 41695-41705
    • Zhang, Y.1    Chen, K.2    Tu, Y.3
  • 5
    • 23744490092 scopus 로고    scopus 로고
    • PINCH1 regulates cell-matrix and cell-cell adhesions, cell polarity and cell survival during the peri-implantation stage
    • Li S, Bordoy R, Stanchi F, et al. PINCH1 regulates cell-matrix and cell-cell adhesions, cell polarity and cell survival during the peri-implantation stage. J Cell Sci. 2005;118:2913-2921.
    • (2005) J Cell Sci. , vol.118 , pp. 2913-2921
    • Li, S.1    Bordoy, R.2    Stanchi, F.3
  • 6
    • 16244413957 scopus 로고    scopus 로고
    • PINCH1 plays an essential role in early murine embryonic development but is dispensable in ventricular cardiomyocytes
    • Liang X, Zhou Q, Li X, et al. PINCH1 plays an essential role in early murine embryonic development but is dispensable in ventricular cardiomyocytes. Mol Cell Biol. 2005;25:3056-3062.
    • (2005) Mol Cell Biol. , vol.25 , pp. 3056-3062
    • Liang, X.1    Zhou, Q.2    Li, X.3
  • 7
    • 0033986923 scopus 로고    scopus 로고
    • Bi-directional signal transduction by integrin receptors
    • Coppolino MG, Dedhar S. Bi-directional signal transduction by integrin receptors. Int J Biochem Cell Biol. 2000;32:171-188.
    • (2000) Int J Biochem Cell Biol. , vol.32 , pp. 171-188
    • Coppolino, M.G.1    Dedhar, S.2
  • 8
    • 0032530482 scopus 로고    scopus 로고
    • Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase
    • Delcommenne M, Tan C, Gray V, et al. Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase. Proc Natl Acad Sci U S A. 1998;95:11211-11216.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 11211-11216
    • Delcommenne, M.1    Tan, C.2    Gray, V.3
  • 9
    • 0030026679 scopus 로고    scopus 로고
    • Regulation of cell adhesion and anchorage-dependent growth by a new beta 1-integrinYlinked protein kinase
    • Hannigan GE, Leung-Hagesteijn C, Fitz-Gibbon L, et al. Regulation of cell adhesion and anchorage-dependent growth by a new beta 1-integrinYlinked protein kinase. Nature. 1996;379:91-96.
    • (1996) Nature , vol.379 , pp. 91-96
    • Hannigan, G.E.1    Leung-Hagesteijn, C.2    Fitz-Gibbon, L.3
  • 10
    • 0037377167 scopus 로고    scopus 로고
    • PINCH2 is a new five LIM domain protein, homologous to PINCH and localized to focal adhesions
    • Braun A, Bordoy R, Stanchi F, et al. PINCH2 is a new five LIM domain protein, homologous to PINCH and localized to focal adhesions. Exp Cell Res. 2003;284:239-250.
    • (2003) Exp Cell Res. , vol.284 , pp. 239-250
    • Braun, A.1    Bordoy, R.2    Stanchi, F.3
  • 11
    • 0033020670 scopus 로고    scopus 로고
    • The LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cells
    • Tu Y, Li F, Goicoechea S, et al. The LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cells. Mol Cell Biol. 1999;19:2425-2434.
    • (1999) Mol Cell Biol. , vol.19 , pp. 2425-2434
    • Tu, Y.1    Li, F.2    Goicoechea, S.3
  • 12
    • 0037064063 scopus 로고    scopus 로고
    • Characterization of PINCH-2, a new focal adhesion protein that regulates the PINCH-1YILK interaction, cell spreading, and migration
    • Zhang Y, Chen K, Guo L, et al. Characterization of PINCH-2, a new focal adhesion protein that regulates the PINCH-1YILK interaction, cell spreading, and migration. J Biol Chem. 2002;277:38328-38338.
    • (2002) J Biol Chem. , vol.277 , pp. 38328-38338
    • Zhang, Y.1    Chen, K.2    Guo, L.3
  • 13
    • 0035126590 scopus 로고    scopus 로고
    • A 42 kDa focal adhesion protein, related to the alpha-actinin superfamily
    • Olski TM, Noegel AA, Korenbaum EP. A 42 kDa focal adhesion protein, related to the alpha-actinin superfamily. J Cell Sci. 2001;114:525-538.
    • (2001) J Cell Sci. , vol.114 , pp. 525-538
    • Olski, T.M.1    Noegel, A.A.2    Korenbaum, E.P.3
  • 14
    • 0035972170 scopus 로고    scopus 로고
    • A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading
    • Tu Y, Huang Y, Zhang Y, et al. A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading. J Cell Biol. 2001;153:585-598.
    • (2001) J Cell Biol. , vol.153 , pp. 585-598
    • Tu, Y.1    Huang, Y.2    Zhang, Y.3
  • 15
    • 0035844879 scopus 로고    scopus 로고
    • A novel integrin-linked kinasebinding protein, affixin, is involved in the early stage of cell-substrate interaction
    • Yamaji S, Suzuki A, Sugiyama Y, et al. A novel integrin-linked kinasebinding protein, affixin, is involved in the early stage of cell-substrate interaction. J Cell Biol. 2001;153:1251-1264.
    • (2001) J Cell Biol. , vol.153 , pp. 1251-1264
    • Yamaji, S.1    Suzuki, A.2    Sugiyama, Y.3
  • 16
    • 0034739856 scopus 로고    scopus 로고
    • Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion
    • Nikolopoulos SN, Turner CE. Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion. J Cell Biol. 2000;151:1435-1448.
    • (2000) J Cell Biol. , vol.151 , pp. 1435-1448
    • Nikolopoulos, S.N.1    Turner, C.E.2
  • 17
    • 0035968234 scopus 로고    scopus 로고
    • Integrin-linked kinase (ILK) binding to paxillin LD1 motif regulates ILK localization to focal adhesions
    • Nikolopoulos SN, Turner CE. Integrin-linked kinase (ILK) binding to paxillin LD1 motif regulates ILK localization to focal adhesions. J Biol Chem. 2001;276:23499-23505.
    • (2001) J Biol Chem. , vol.276 , pp. 23499-23505
    • Nikolopoulos, S.N.1    Turner, C.E.2
  • 18
    • 0344012484 scopus 로고    scopus 로고
    • Integration of cell attachment, cytoskeletal localization, and signaling by integrin-linked kinase (ILK), CH-ILKBP, and the tumor suppressor PTEN
    • Attwell S, Mills J, Troussard A, et al. Integration of cell attachment, cytoskeletal localization, and signaling by integrin-linked kinase (ILK), CH-ILKBP, and the tumor suppressor PTEN. Mol Biol Cell. 2003;14:4813-4825.
    • (2003) Mol Biol Cell. , vol.14 , pp. 4813-4825
    • Attwell, S.1    Mills, J.2    Troussard, A.3
  • 19
    • 0038148536 scopus 로고    scopus 로고
    • Reduced chondrocyte proliferation and chondrodysplasia in mice lacking the integrin-linked kinase in chondrocytes
    • Terpstra L, Prud'homme J, Arabian A, et al. Reduced chondrocyte proliferation and chondrodysplasia in mice lacking the integrin-linked kinase in chondrocytes. J Cell Biol. 2003;162:139-148.
    • (2003) J Cell Biol. , vol.162 , pp. 139-148
    • Terpstra, L.1    Prud'homme, J.2    Arabian, A.3
  • 20
    • 4644322059 scopus 로고    scopus 로고
    • ILK is required for the assembly of matrix-forming adhesions and capillary morphogenesis in endothelial cells
    • Vouret-Craviari V, Boulter E, Grall D, et al. ILK is required for the assembly of matrix-forming adhesions and capillary morphogenesis in endothelial cells. J Cell Sci. 2004;117:4559-4569.
    • (2004) J Cell Sci. , vol.117 , pp. 4559-4569
    • Vouret-Craviari, V.1    Boulter, E.2    Grall, D.3
  • 21
    • 9144270454 scopus 로고    scopus 로고
    • Regulation of tumor angiogenesis by integrin-linked kinase (ILK)
    • Tan C, Cruet-Hennequart S, Troussard A, et al. Regulation of tumor angiogenesis by integrin-linked kinase (ILK). Cancer Cell. 2004;5: 79-90.
    • (2004) Cancer Cell. , vol.5 , pp. 79-90
    • Tan, C.1    Cruet-Hennequart, S.2    Troussard, A.3
  • 22
    • 0034724443 scopus 로고    scopus 로고
    • Inhibition of integrin-linked kinase (ILK) suppresses activation of protein kinase B/Akt and induces cell cycle arrest and apoptosis of PTEN-mutant prostate cancer cells
    • Persad S, Attwell S, Gray V, et al. Inhibition of integrin-linked kinase (ILK) suppresses activation of protein kinase B/Akt and induces cell cycle arrest and apoptosis of PTEN-mutant prostate cancer cells. Proc Natl Acad Sci U S A. 2000;97:3207-3212.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 3207-3212
    • Persad, S.1    Attwell, S.2    Gray, V.3
  • 23
    • 0034601436 scopus 로고    scopus 로고
    • The integrin-linked kinase (ILK) suppresses anoikis
    • Attwell S, Roskelley C, Dedhar S. The integrin-linked kinase (ILK) suppresses anoikis. Oncogene. 2000;19:3811-3815.
    • (2000) Oncogene , vol.19 , pp. 3811-3815
    • Attwell, S.1    Roskelley, C.2    Dedhar, S.3
  • 24
    • 0037315101 scopus 로고    scopus 로고
    • Essential role for integrin linked kinase in Akt-mediated integrin survival signaling in hippocampal neurons
    • Gary DS, Milhavet O, Camandola S, et al. Essential role for integrin linked kinase in Akt-mediated integrin survival signaling in hippocampal neurons. J Neurochem. 2003;84:878-890.
    • (2003) J Neurochem. , vol.84 , pp. 878-890
    • Gary, D.S.1    Milhavet, O.2    Camandola, S.3
  • 25
    • 4444305175 scopus 로고    scopus 로고
    • Integrin-linked kinase regulates endothelial cell survival and vascular development
    • Friedrich EB, Liu E, Sinha S, et al. Integrin-linked kinase regulates endothelial cell survival and vascular development. Mol Cell Biol. 2004;24:8134-8144.
    • (2004) Mol Cell Biol. , vol.24 , pp. 8134-8144
    • Friedrich, E.B.1    Liu, E.2    Sinha, S.3
  • 26
    • 13944256944 scopus 로고    scopus 로고
    • Inhibition of integrin-linked kinase by a selective small molecule inhibitor, QLT0254, inhibits the PI3K/PKB/mTOR, Stat3, and FKHR pathways and tumor growth, and enhances gemcitabine-induced apoptosis in human orthotopic primary pancreatic cancer xenografts
    • Yau CY, Wheeler JJ, Sutton KL, et al. Inhibition of integrin-linked kinase by a selective small molecule inhibitor, QLT0254, inhibits the PI3K/PKB/mTOR, Stat3, and FKHR pathways and tumor growth, and enhances gemcitabine-induced apoptosis in human orthotopic primary pancreatic cancer xenografts. Cancer Res. 2005;65:1497-1504.
    • (2005) Cancer Res. , vol.65 , pp. 1497-1504
    • Yau, C.Y.1    Wheeler, J.J.2    Sutton, K.L.3
  • 27
    • 19944411156 scopus 로고    scopus 로고
    • Inhibition of ILK in PTEN-mutant human glioblastomas inhibits PKB/Akt activation, induces apoptosis, and delays tumor growth
    • Edwards LA, Thiessen B, Dragowska WH, et al. Inhibition of ILK in PTEN-mutant human glioblastomas inhibits PKB/Akt activation, induces apoptosis, and delays tumor growth. Oncogene. 2005;24:3596-3605.
    • (2005) Oncogene , vol.24 , pp. 3596-3605
    • Edwards, L.A.1    Thiessen, B.2    Dragowska, W.H.3
  • 29
  • 30
    • 0345687500 scopus 로고    scopus 로고
    • Positional control of cell fate through joint integrin/receptor protein kinase signaling
    • Giancotti FG, Tarone G. Positional control of cell fate through joint integrin/receptor protein kinase signaling. Annu Rev Cell Dev Biol. 2003;19:173-206.
    • (2003) Annu Rev Cell Dev Biol. , vol.19 , pp. 173-206
    • Giancotti, F.G.1    Tarone, G.2
  • 31
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes RO. Integrins: bidirectional, allosteric signaling machines. Cell. 2002;110:673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 32
    • 0035969233 scopus 로고    scopus 로고
    • Integrin-linked kinase (ILK) and its interactors: A new paradigm for the coupling of extracellular matrix to actin cytoskeleton and signaling complexes
    • Wu C, Dedhar S. Integrin-linked kinase (ILK) and its interactors: a new paradigm for the coupling of extracellular matrix to actin cytoskeleton and signaling complexes. J Cell Biol. 2001;155:505-510.
    • (2001) J Cell Biol. , vol.155 , pp. 505-510
    • Wu, C.1    Dedhar, S.2
  • 33
    • 0032516094 scopus 로고    scopus 로고
    • Cell adhesion and the integrin-linked kinase regulate the LEF-1 and beta-catenin signaling pathways
    • Novak A, Hsu SC, Leung-Hagesteijn C, et al. Cell adhesion and the integrin-linked kinase regulate the LEF-1 and beta-catenin signaling pathways. Proc Natl Acad Sci U S A. 1998;95:4374-4379.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 4374-4379
    • Novak, A.1    Hsu, S.C.2    Leung-Hagesteijn, C.3
  • 34
    • 0027933818 scopus 로고
    • A new LIM protein containing an autoepitope homologous to "senescent cell antigen"
    • Rearden A. A new LIM protein containing an autoepitope homologous to "senescent cell antigen". Biochem Biophys Res Commun. 1994;201: 1124-1131.
    • (1994) Biochem Biophys Res Commun. , vol.201 , pp. 1124-1131
    • Rearden, A.1
  • 35
    • 0033545214 scopus 로고    scopus 로고
    • A conserved LIM protein that affects muscular adherens junction integrity and mechanosensory function in Caenorhabditis elegans
    • Hobert O, Moerman DG, Clark KA, et al. A conserved LIM protein that affects muscular adherens junction integrity and mechanosensory function in Caenorhabditis elegans. J Cell Biol. 1999;144:45-57.
    • (1999) J Cell Biol. , vol.144 , pp. 45-57
    • Hobert, O.1    Moerman, D.G.2    Clark, K.A.3
  • 36
    • 0033378656 scopus 로고    scopus 로고
    • Integrin-linked kinase is localized to cell-matrix focal adhesions but not cell-cell adhesion sites and the focal adhesion localization of integrin-linked kinase is regulated by the PINCH-binding ANK repeats
    • Li F, Zhang Y, Wu C. Integrin-linked kinase is localized to cell-matrix focal adhesions but not cell-cell adhesion sites and the focal adhesion localization of integrin-linked kinase is regulated by the PINCH-binding ANK repeats. J Cell Sci. 1999;112(pt 24):4589-4599.
    • (1999) J Cell Sci. , vol.112 , Issue.PART 24 , pp. 4589-4599
    • Li, F.1    Zhang, Y.2    Wu, C.3
  • 37
    • 23044505280 scopus 로고    scopus 로고
    • Molecular dissection of PINCH-1 reveals a mechanism of coupling and uncoupling of cell shape modulation and survival
    • Xu Z, Fukuda T, Li Y, et al. Molecular dissection of PINCH-1 reveals a mechanism of coupling and uncoupling of cell shape modulation and survival. J Biol Chem. 2005;280:27631-27637.
    • (2005) J Biol Chem. , vol.280 , pp. 27631-27637
    • Xu, Z.1    Fukuda, T.2    Li, Y.3
  • 38
    • 30544431602 scopus 로고    scopus 로고
    • Consequences of loss of PINCH2 expression in mice
    • Stanchi F, Bordoy R, Kudlacek O, et al. Consequences of loss of PINCH2 expression in mice. J Cell Sci. 2005;118:5899-5910.
    • (2005) J Cell Sci. , vol.118 , pp. 5899-5910
    • Stanchi, F.1    Bordoy, R.2    Kudlacek, O.3
  • 39
    • 69549097709 scopus 로고    scopus 로고
    • Targeted ablation of PINCH1 and PINCH2 from murine myocardium results in dilated cardiomyopathy and early postnatal lethality
    • Accepted
    • Liang XQ, Sun YF, Ye MQ, et al. Targeted ablation of PINCH1 and PINCH2 from murine myocardium results in dilated cardiomyopathy and early postnatal lethality. Circulation. 2009; Accepted
    • (2009) Circulation
    • Liang, X.Q.1    Sun, Y.F.2    Ye, M.Q.3
  • 40
    • 0031772910 scopus 로고    scopus 로고
    • Nck-2, a novel Src homology2/3Ycontaining adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase-signaling pathways
    • Tu Y, Li F, Wu C. Nck-2, a novel Src homology2/3Ycontaining adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase-signaling pathways. Mol Biol Cell. 1998;9:3367-3382.
    • (1998) Mol Biol Cell. , vol.9 , pp. 3367-3382
    • Tu, Y.1    Li, F.2    Wu, C.3
  • 41
    • 0036015163 scopus 로고    scopus 로고
    • The Nck family of adapter proteins: Regulators of actin cytoskeleton
    • Buday L, Wunderlich L, Tamas P. The Nck family of adapter proteins: regulators of actin cytoskeleton. Cell Signal. 2002;14:723-731.
    • (2002) Cell Signal. , vol.14 , pp. 723-731
    • Buday, L.1    Wunderlich, L.2    Tamas, P.3
  • 42
    • 0035473460 scopus 로고    scopus 로고
    • Nck/Dock: An adapter between cell surface receptors and the actin cytoskeleton
    • Li W, Fan J, Woodley DT. Nck/Dock: an adapter between cell surface receptors and the actin cytoskeleton. Oncogene. 2001;20:6403-6417.
    • (2001) Oncogene , vol.20 , pp. 6403-6417
    • Li, W.1    Fan, J.2    Woodley, D.T.3
  • 43
    • 0037743516 scopus 로고    scopus 로고
    • Structural and functional insights into PINCH LIM4 domain-mediated integrin signaling
    • Velyvis A, Vaynberg J, Yang Y, et al. Structural and functional insights into PINCH LIM4 domain-mediated integrin signaling. Nat Struct Biol. 2003;10:558-564.
    • (2003) Nat Struct Biol. , vol.10 , pp. 558-564
    • Velyvis, A.1    Vaynberg, J.2    Yang, Y.3
  • 44
    • 0038383014 scopus 로고    scopus 로고
    • The murine Nck SH2/SH3 adaptors are important for the development of mesoderm-derived embryonic structures and for regulating the cellular actin network
    • Bladt F, Aippersbach E, Gelkop S, et al. The murine Nck SH2/SH3 adaptors are important for the development of mesoderm-derived embryonic structures and for regulating the cellular actin network. Mol Cell Biol. 2003;23:4586-4597.
    • (2003) Mol Cell Biol. , vol.23 , pp. 4586-4597
    • Bladt, F.1    Aippersbach, E.2    Gelkop, S.3
  • 45
    • 0026658729 scopus 로고
    • Isolation of rsp-1, a novel cDNAcapable of suppressing v-Ras transformation
    • Cutler ML, Bassin RH, Zanoni L, et al. Isolation of rsp-1, a novel cDNAcapable of suppressing v-Ras transformation. Mol Cell Biol. 1992;12: 3750-3756.
    • (1992) Mol Cell Biol. , vol.12 , pp. 3750-3756
    • Cutler, M.L.1    Bassin, R.H.2    Zanoni, L.3
  • 46
    • 0029092309 scopus 로고
    • The Ras suppressor RSU-1 localizes to 10p13 and its expression in the U251 glioblastoma cell line correlates with a decrease in growth rate and tumorigenic potential
    • Tsuda T, Marinetti MR, Masuelli L, et al. The Ras suppressor RSU-1 localizes to 10p13 and its expression in the U251 glioblastoma cell line correlates with a decrease in growth rate and tumorigenic potential. Oncogene. 1995;11:397-403.
    • (1995) Oncogene , vol.11 , pp. 397-403
    • Tsuda, T.1    Marinetti, M.R.2    Masuelli, L.3
  • 47
    • 18844394310 scopus 로고    scopus 로고
    • The Ras suppressor Rsu-1 binds to the LIM 5 domain of the adaptor protein PINCH1 and participates in adhesion-related functions
    • Dougherty GW, Chopp T, Qi SM, et al. The Ras suppressor Rsu-1 binds to the LIM 5 domain of the adaptor protein PINCH1 and participates in adhesion-related functions. Exp Cell Res. 2005;306: 168-179.
    • (2005) Exp Cell Res. , vol.306 , pp. 168-179
    • Dougherty, G.W.1    Chopp, T.2    Qi, S.M.3
  • 48
    • 49249096493 scopus 로고    scopus 로고
    • The Rsu-1-PINCH1-ILK complex is regulated by Ras activation in tumor cells
    • Dougherty GW, Jose C, Gimona M, et al. The Rsu-1-PINCH1-ILK complex is regulated by Ras activation in tumor cells. Eur J Cell Biol. 2008;87:721-734.
    • (2008) Eur J Cell Biol. , vol.87 , pp. 721-734
    • Dougherty, G.W.1    Jose, C.2    Gimona, M.3
  • 49
    • 11244299748 scopus 로고    scopus 로고
    • The integrin effector PINCH regulates JNK activity and epithelial migration in concert with Ras suppressor 1
    • Kadrmas JL, Smith MA, Clark KA, et al. The integrin effector PINCH regulates JNK activity and epithelial migration in concert with Ras suppressor 1. J Cell Biol. 2004;167:1019-1024.
    • (2004) J Cell Biol. , vol.167 , pp. 1019-1024
    • Kadrmas, J.L.1    Smith, M.A.2    Clark, K.A.3
  • 50
    • 9644281738 scopus 로고    scopus 로고
    • Thymosin beta4 activates integrin-linked kinase and promotes cardiac cell migration, survival and cardiac repair
    • Bock-Marquette I, Saxena A, White MD, et al. Thymosin beta4 activates integrin-linked kinase and promotes cardiac cell migration, survival and cardiac repair. Nature. 2004;432:466-472.
    • (2004) Nature , vol.432 , pp. 466-472
    • Bock-Marquette, I.1    Saxena, A.2    White, M.D.3
  • 51
    • 35349031022 scopus 로고    scopus 로고
    • Thymosin beta4 is cardioprotective after myocardial infarction
    • Srivastava D, Saxena A, Michael Dimaio J, et al. Thymosin beta4 is cardioprotective after myocardial infarction. Ann N Y Acad Sci. 2007;1112:161-170.
    • (2007) Ann N y Acad Sci. , vol.1112 , pp. 161-170
    • Srivastava, D.1    Saxena, A.2    Michael Dimaio, J.3
  • 52
    • 0038409304 scopus 로고    scopus 로고
    • Analysis of PINCH function in Drosophila demonstrates its requirement in integrin-dependent cellular processes
    • Clark KA, McGrail M, Beckerle MC. Analysis of PINCH function in Drosophila demonstrates its requirement in integrin-dependent cellular processes. Development. 2003;130:2611-2621.
    • (2003) Development , vol.130 , pp. 2611-2621
    • Clark, K.A.1    McGrail, M.2    Beckerle, M.C.3
  • 53
    • 0028990430 scopus 로고
    • Characterization of beta pat-3 heterodimers, a family of essential integrin receptors in C. elegans
    • Gettner SN, Kenyon C, Reichardt LF. Characterization of beta pat-3 heterodimers, a family of essential integrin receptors in C. elegans. J Cell Biol. 1995;129:1127-1141.
    • (1995) J Cell Biol. , vol.129 , pp. 1127-1141
    • Gettner, S.N.1    Kenyon, C.2    Reichardt, L.F.3
  • 54
    • 0037076211 scopus 로고    scopus 로고
    • C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes
    • Mackinnon AC, Qadota H, Norman KR, et al. C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes. Curr Biol. 2002;12:787-797.
    • (2002) Curr Biol. , vol.12 , pp. 787-797
    • MacKinnon, A.C.1    Qadota, H.2    Norman, K.R.3
  • 55
    • 0024965992 scopus 로고
    • The function of PS integrins during Drosophila embryogenesis
    • Leptin M, Bogaert T, Lehmann R, et al. The function of PS integrins during Drosophila embryogenesis. Cell. 1989;56:401-408.
    • (1989) Cell , vol.56 , pp. 401-408
    • Leptin, M.1    Bogaert, T.2    Lehmann, R.3
  • 56
    • 0023990945 scopus 로고
    • The lethalmyospheroid gene of Drosophila encodes a membrane protein homologous to vertebrate integrin beta subunits
    • MacKrell AJ, Blumberg B, Haynes SR, et al. The lethalmyospheroid gene of Drosophila encodes a membrane protein homologous to vertebrate integrin beta subunits. Proc Natl Acad Sci U S A. 1988;85:2633-2637.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 2633-2637
    • MacKrell, A.J.1    Blumberg, B.2    Haynes, S.R.3
  • 57
    • 0035809918 scopus 로고    scopus 로고
    • Drosophila integrin-linked kinase is required at sites of integrin adhesion to link the cytoskeleton to the plasma membrane
    • Zervas CG, Gregory SL, Brown NH. Drosophila integrin-linked kinase is required at sites of integrin adhesion to link the cytoskeleton to the plasma membrane. J Cell Biol. 2001;152:1007-1018.
    • (2001) J Cell Biol. , vol.152 , pp. 1007-1018
    • Zervas, C.G.1    Gregory, S.L.2    Brown, N.H.3
  • 58
    • 0026451739 scopus 로고
    • Establishment and organization of germ layers in the gastrulating mouse embryo
    • discussion 42-129
    • Tam PP, Beddington RS. Establishment and organization of germ layers in the gastrulating mouse embryo. Ciba Found Symp. 1992;165:27-41; discussion 42-129
    • (1992) Ciba Found Symp. , vol.165 , pp. 27-41
    • Tam, P.P.1    Beddington, R.S.2
  • 59
    • 0028818755 scopus 로고
    • Signals for death and survival: A two-step mechanism for cavitation in the vertebrate embryo
    • Coucouvanis E, Martin GR. Signals for death and survival: a two-step mechanism for cavitation in the vertebrate embryo. Cell. 1995;83:279-287.
    • (1995) Cell , vol.83 , pp. 279-287
    • Coucouvanis, E.1    Martin, G.R.2
  • 60
    • 0033950910 scopus 로고    scopus 로고
    • Altered synthesis of laminin 1 and absence of basement membrane component deposition in (beta)1 integrinYdeficient embryoid bodies
    • Aumailley M, Pesch M, Tunggal L, et al. Altered synthesis of laminin 1 and absence of basement membrane component deposition in (beta)1 integrinYdeficient embryoid bodies. J Cell Sci. 2000;113(pt 2): 259-268.
    • (2000) J Cell Sci. , vol.113 , Issue.PART 2 , pp. 259-268
    • Aumailley, M.1    Pesch, M.2    Tunggal, L.3
  • 61
    • 0028979154 scopus 로고
    • Consequences of lack of beta 1 integrin gene expression in mice
    • Fassler R, Meyer M. Consequences of lack of beta 1 integrin gene expression in mice. Genes Dev. 1995;9:1896-1908.
    • (1995) Genes Dev. , vol.9 , pp. 1896-1908
    • Fassler, R.1    Meyer, M.2
  • 62
    • 0037166935 scopus 로고    scopus 로고
    • Matrix assembly, regulation, and survival functions of laminin and its receptors in embryonic stem cell differentiation
    • Li S, Harrison D, Carbonetto S, et al. Matrix assembly, regulation, and survival functions of laminin and its receptors in embryonic stem cell differentiation. J Cell Biol. 2002;157:1279-1290.
    • (2002) J Cell Biol. , vol.157 , pp. 1279-1290
    • Li, S.1    Harrison, D.2    Carbonetto, S.3
  • 63
    • 0345103747 scopus 로고    scopus 로고
    • Integrin-linked kinase (ILK) is required for polarizing the epiblast, cell adhesion, and controlling actin accumulation
    • Sakai T, Li S, Docheva D, et al. Integrin-linked kinase (ILK) is required for polarizing the epiblast, cell adhesion, and controlling actin accumulation. Genes Dev. 2003;17:926-940.
    • (2003) Genes Dev. , vol.17 , pp. 926-940
    • Sakai, T.1    Li, S.2    Docheva, D.3
  • 64
    • 0028979153 scopus 로고
    • Deletion of beta 1 integrins in mice results in inner cell mass failure and peri-implantation lethality
    • Stephens LE, Sutherland AE, Klimanskaya IV, et al. Deletion of beta 1 integrins in mice results in inner cell mass failure and peri-implantation lethality. Genes Dev. 1995;9:1883-1895.
    • (1995) Genes Dev. , vol.9 , pp. 1883-1895
    • Stephens, L.E.1    Sutherland, A.E.2    Klimanskaya, I.V.3
  • 65
  • 66
    • 0029142767 scopus 로고
    • Neural crest and cardiovascular patterning
    • Kirby ML, Waldo KL. Neural crest and cardiovascular patterning. Circ Res. 1995;77:211-215.
    • (1995) Circ Res. , vol.77 , pp. 211-215
    • Kirby, M.L.1    Waldo, K.L.2
  • 67
    • 0034010326 scopus 로고    scopus 로고
    • Fate of the mammalian cardiac neural crest
    • Jiang X, Rowitch DH, Soriano P, et al. Fate of the mammalian cardiac neural crest. Development. 2000;127:1607-1616.
    • (2000) Development , vol.127 , pp. 1607-1616
    • Jiang, X.1    Rowitch, D.H.2    Soriano, P.3
  • 68
    • 0020640517 scopus 로고
    • Neural crest cells contribute to normal aorticopulmonary septation
    • Kirby ML, Gale TF, Stewart DE. Neural crest cells contribute to normal aorticopulmonary septation. Science. 1983;220:1059-1061.
    • (1983) Science , vol.220 , pp. 1059-1061
    • Kirby, M.L.1    Gale, T.F.2    Stewart, D.E.3
  • 69
    • 0025943867 scopus 로고
    • Temporospatial study of the migration and distribution of cardiac neural crest in quail-chick chimeras
    • Miyagawa-Tomita S, Waldo K, Tomita H, et al. Temporospatial study of the migration and distribution of cardiac neural crest in quail-chick chimeras. Am J Anat. 1991;192:79-88.
    • (1991) Am J Anat. , vol.192 , pp. 79-88
    • Miyagawa-Tomita, S.1    Waldo, K.2    Tomita, H.3
  • 70
    • 0031040876 scopus 로고    scopus 로고
    • Pax3 is required for cardiac neural crest migration in the mouse: Evidence from the splotch (Sp2H) mutant
    • Conway SJ, Henderson DJ, Copp AJ. Pax3 is required for cardiac neural crest migration in the mouse: evidence from the splotch (Sp2H) mutant. Development. 1997;124:505-514.
    • (1997) Development , vol.124 , pp. 505-514
    • Conway, S.J.1    Henderson, D.J.2    Copp, A.J.3
  • 71
    • 0034030119 scopus 로고    scopus 로고
    • Migration of cardiac neural crest cells in Splotch embryos
    • Epstein JA, Li J, Lang D, et al. Migration of cardiac neural crest cells in Splotch embryos. Development. 2000;127:1869-1878.
    • (2000) Development , vol.127 , pp. 1869-1878
    • Epstein, J.A.1    Li, J.2    Lang, D.3
  • 72
    • 0038485530 scopus 로고    scopus 로고
    • Heart development: Molecular insights into cardiac specification and early morphogenesis
    • Brand T. Heart development: molecular insights into cardiac specification and early morphogenesis. Dev Biol. 2003;258:1-19.
    • (2003) Dev Biol. , vol.258 , pp. 1-19
    • Brand, T.1
  • 73
    • 0025833053 scopus 로고
    • Velocardiofacial (Shprintzen) syndrome: An important syndrome for the dysmorphologist to recognise
    • Lipson AH, Yuille D, Angel M, et al. Velocardiofacial (Shprintzen) syndrome: an important syndrome for the dysmorphologist to recognise. J Med Genet. 1991;28:596-604.
    • (1991) J Med Genet. , vol.28 , pp. 596-604
    • Lipson, A.H.1    Yuille, D.2    Angel, M.3
  • 74
    • 0028349997 scopus 로고
    • Targeted disruption of the neurofibromatosis type-1 gene leads to developmental abnormalities in heart and various neural crest-derived tissues
    • Brannan CI, Perkins AS, Vogel KS, et al. Targeted disruption of the neurofibromatosis type-1 gene leads to developmental abnormalities in heart and various neural crest-derived tissues. Genes Dev. 1994;8: 1019-1029.
    • (1994) Genes Dev. , vol.8 , pp. 1019-1029
    • Brannan, C.I.1    Perkins, A.S.2    Vogel, K.S.3
  • 75
    • 0033605704 scopus 로고    scopus 로고
    • Requirement of type III TGF-beta receptor for endocardial cell transformation in the heart
    • Brown CB, Boyer AS, Runyan RB, et al. Requirement of type III TGF-beta receptor for endocardial cell transformation in the heart. Science. 1999;283:2080-2082.
    • (1999) Science , vol.283 , pp. 2080-2082
    • Brown, C.B.1    Boyer, A.S.2    Runyan, R.B.3
  • 77
    • 33947502551 scopus 로고    scopus 로고
    • Pinch1 is required for normal development of cranial and cardiac neural crest-derived structures
    • Liang X, Sun Y, Schneider J, et al. Pinch1 is required for normal development of cranial and cardiac neural crest-derived structures. Circ Res. 2007;100:527-535.
    • (2007) Circ Res. , vol.100 , pp. 527-535
    • Liang, X.1    Sun, Y.2    Schneider, J.3
  • 78
    • 33644969879 scopus 로고    scopus 로고
    • PINCH-1 expression during early avian embryogenesis: Implications for neural crest and heart development
    • Martinsen BJ, Neumann AN, Frasier AJ, et al. PINCH-1 expression during early avian embryogenesis: implications for neural crest and heart development. Dev Dyn. 2006;235:152-162.
    • (2006) Dev Dyn. , vol.235 , pp. 152-162
    • Martinsen, B.J.1    Neumann, A.N.2    Frasier, A.J.3
  • 79
    • 33747812887 scopus 로고    scopus 로고
    • Aneurysm syndromes caused by mutations in the TGF-beta receptor
    • Loeys BL, Schwarze U, Holm T, et al. Aneurysm syndromes caused by mutations in the TGF-beta receptor. N Engl J Med. 2006;355: 788-798.
    • (2006) N Engl J Med. , vol.355 , pp. 788-798
    • Loeys, B.L.1    Schwarze, U.2    Holm, T.3
  • 80
    • 3543013177 scopus 로고    scopus 로고
    • Heterozygous TGFBR2 mutations in Marfan syndrome
    • Mizuguchi T, Collod-Beroud G, Akiyama T, et al. Heterozygous TGFBR2 mutations in Marfan syndrome. Nat Genet. 2004;36:855-860.
    • (2004) Nat Genet. , vol.36 , pp. 855-860
    • Mizuguchi, T.1    Collod-Beroud, G.2    Akiyama, T.3
  • 81
    • 0037373277 scopus 로고    scopus 로고
    • Dysregulation of TGF-beta activation contributes to pathogenesis in Marfan syndrome
    • Neptune ER, Frischmeyer PA, Arking DE, et al. Dysregulation of TGF-beta activation contributes to pathogenesis in Marfan syndrome. Nat Genet. 2003;33:407-411.
    • (2003) Nat Genet. , vol.33 , pp. 407-411
    • Neptune, E.R.1    Frischmeyer, P.A.2    Arking, D.E.3
  • 82
    • 14644418529 scopus 로고    scopus 로고
    • Inactivation of TGFbeta signaling in neural crest stem cells leads to multiple defects reminiscent of DiGeorge syndrome
    • Wurdak H, Ittner LM, Lang KS, et al. Inactivation of TGFbeta signaling in neural crest stem cells leads to multiple defects reminiscent of DiGeorge syndrome. Genes Dev. 2005;19:530-535.
    • (2005) Genes Dev. , vol.19 , pp. 530-535
    • Wurdak, H.1    Ittner, L.M.2    Lang, K.S.3
  • 83
    • 0029966491 scopus 로고    scopus 로고
    • Antibodies to the Type II TGFbeta receptor block cell activation and migration during atrioventricular cushion transformation in the heart
    • Brown CB, Boyer AS, Runyan RB, et al. Antibodies to the Type II TGFbeta receptor block cell activation and migration during atrioventricular cushion transformation in the heart. Dev Biol. 1996;174:248-257.
    • (1996) Dev Biol. , vol.174 , pp. 248-257
    • Brown, C.B.1    Boyer, A.S.2    Runyan, R.B.3
  • 84
    • 0022410203 scopus 로고
    • Intercalated discs of mammalian heart: A review of structure and function
    • Forbes MS, Sperelakis N. Intercalated discs of mammalian heart: a review of structure and function. Tissue Cell. 1985;17:605-648.
    • (1985) Tissue Cell. , vol.17 , pp. 605-648
    • Forbes, M.S.1    Sperelakis, N.2
  • 86
    • 0036228744 scopus 로고    scopus 로고
    • Intercellular adhesion, signalling and the cytoskeleton
    • E101YE108
    • Jamora C, Fuchs E. Intercellular adhesion, signalling and the cytoskeleton. Nat Cell Biol. 2002;4:E101YE108.
    • (2002) Nat Cell Biol. , vol.4
    • Jamora, C.1    Fuchs, E.2
  • 87
    • 28344439885 scopus 로고    scopus 로고
    • Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and regulates actin-filament assembly
    • Drees F, Pokutta S, Yamada S, et al. Alpha-catenin is a molecular switch that binds E-cadherinYbeta-catenin and regulates actin-filament assembly. Cell. 2005;123:903-915.
    • (2005) Cell , vol.123 , pp. 903-915
    • Drees, F.1    Pokutta, S.2    Yamada, S.3
  • 88
    • 0030000980 scopus 로고    scopus 로고
    • Cadherin-catenin complex: Protein interactions and their implications for cadherin function
    • Aberle H, Schwartz H, Kemler R. Cadherin-catenin complex: protein interactions and their implications for cadherin function. J Cell Biochem. 1996;61:514-523.
    • (1996) J Cell Biochem. , vol.61 , pp. 514-523
    • Aberle, H.1    Schwartz, H.2    Kemler, R.3
  • 89
    • 0037237653 scopus 로고    scopus 로고
    • Dilated cardiomyopathy: A disease of the intercalated disc?
    • Perriard JC, Hirschy A, Ehler E. Dilated cardiomyopathy: a disease of the intercalated disc? Trends Cardiovasc Med. 2003;13:30-38.
    • (2003) Trends Cardiovasc Med. , vol.13 , pp. 30-38
    • Perriard, J.C.1    Hirschy, A.2    Ehler, E.3
  • 90
    • 0031042948 scopus 로고    scopus 로고
    • Developmental defects in mouse embryos lacking N-cadherin
    • Radice GL, Rayburn H, Matsunami H, et al. Developmental defects in mouse embryos lacking N-cadherin. Dev Biol. 1997;181:64-78.
    • (1997) Dev Biol. , vol.181 , pp. 64-78
    • Radice, G.L.1    Rayburn, H.2    Matsunami, H.3
  • 91
    • 0031024666 scopus 로고    scopus 로고
    • Dissociated spatial patterning of gap junctions and cell adhesion junctions during postnatal differentiation of ventricular myocardium
    • Angst BD, Khan LU, Severs NJ, et al. Dissociated spatial patterning of gap junctions and cell adhesion junctions during postnatal differentiation of ventricular myocardium. Circ Res. 1997;80: 88-94.
    • (1997) Circ Res. , vol.80 , pp. 88-94
    • Angst, B.D.1    Khan, L.U.2    Severs, N.J.3
  • 92
    • 30044442758 scopus 로고    scopus 로고
    • Establishment of cardiac cytoarchitecture in the developing mouse heart
    • Hirschy A, Schatzmann F, Ehler E, et al. Establishment of cardiac cytoarchitecture in the developing mouse heart. Dev Biol. 2006;289: 430-441.
    • (2006) Dev Biol. , vol.289 , pp. 430-441
    • Hirschy, A.1    Schatzmann, F.2    Ehler, E.3
  • 93
    • 0037040839 scopus 로고    scopus 로고
    • Cardiac myocyte-specific excision of the beta1 integrin gene results in myocardial fibrosis and cardiac failure
    • Shai SY, Harpf AE, Babbitt CJ, et al. Cardiac myocyte-specific excision of the beta1 integrin gene results in myocardial fibrosis and cardiac failure. Circ Res. 2002;90:458-464.
    • (2002) Circ Res. , vol.90 , pp. 458-464
    • Shai, S.Y.1    Harpf, A.E.2    Babbitt, C.J.3
  • 94
    • 33748278519 scopus 로고    scopus 로고
    • Targeted ablation of ILK from the murine heart results in dilated cardiomyopathy and spontaneous heart failure
    • White DE, Coutu P, Shi YF, et al. Targeted ablation of ILK from the murine heart results in dilated cardiomyopathy and spontaneous heart failure. Genes Dev. 2006;20:2355-2360.
    • (2006) Genes Dev. , vol.20 , pp. 2355-2360
    • White, D.E.1    Coutu, P.2    Shi, Y.F.3
  • 95
    • 59649110883 scopus 로고    scopus 로고
    • Cardiac fibroblasts regulate myocardial proliferation through beta1 integrin signaling
    • Ieda M, Tsuchihashi T, Ivey KN, et al. Cardiac fibroblasts regulate myocardial proliferation through beta1 integrin signaling. Dev Cell. 2009;16:233-244.
    • (2009) Dev Cell. , vol.16 , pp. 233-244
    • Ieda, M.1    Tsuchihashi, T.2    Ivey, K.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.