메뉴 건너뛰기




Volumn 63, Issue 1, 2006, Pages 25-35

The parvins

Author keywords

actinin; Actin cytoskeleton; Cell migration; ILK; Parvin; Paxillin; PINCH; Survival

Indexed keywords

ALPHA ACTININ; ALPHA PARVIN; BETA PARVIN; INTEGRIN LINKED KINASE; LIM PROTEIN; PAXILLIN; PROTEIN; PROTEIN PINCH 1; RAC1 PROTEIN; UNCLASSIFIED DRUG;

EID: 30744472136     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-005-5355-1     Document Type: Review
Times cited : (82)

References (63)
  • 1
    • 0034739856 scopus 로고    scopus 로고
    • Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion
    • Nikolopoulos S. N. and Turner C. E. (2000) Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion. J. Cell. Biol. 151: 1435-1448
    • (2000) J. Cell. Biol. , vol.151 , pp. 1435-1448
    • Nikolopoulos, S.N.1    Turner, C.E.2
  • 2
    • 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., Hua Y. and Wu C. (2001) A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading. J. Cell. Biol. 153: 585-598
    • (2001) J. Cell. Biol. , vol.153 , pp. 585-598
    • Tu, Y.1    Huang, Y.2    Zhang, Y.3    Hua, Y.4    Wu, C.5
  • 3
    • 0035844879 scopus 로고    scopus 로고
    • A novel integrin-linked kinase-binding protein, affixin, is involved in the early stage of cell-substrate interaction
    • Yamaji S., Suzuki A., Sugiyama Y., Koide Y., Yoshida M., Kanamori H. et al. (2001) A novel integrin-linked kinase-binding protein, affixin, is involved in the early stage of cell-substrate interaction. J. Cell. Biol. 153: 1251-1264
    • (2001) J. Cell. Biol. , vol.153 , pp. 1251-1264
    • Yamaji, S.1    Suzuki, A.2    Sugiyama, Y.3    Koide, Y.4    Yoshida, M.5    Kanamori, H.6
  • 4
    • 0035126590 scopus 로고    scopus 로고
    • Parvin, a 42 kDa focal adhesion protein, related to the alpha-actinin superfamily
    • Olski T. M., Noegel A. A. and Korenbaum E. (2001) Parvin, a 42 kDa focal adhesion protein, related to the alpha-actinin superfamily. J. Cell. Sci. 114: 525-538
    • (2001) J. Cell. Sci. , vol.114 , pp. 525-538
    • Olski, T.M.1    Noegel, A.A.2    Korenbaum, E.3
  • 5
    • 0037850992 scopus 로고    scopus 로고
    • C. elegans PAT-6/actopaxin plays a critical role in the assembly of integrin adhesion complexes in vivo
    • Lin X., Qadota H., Moerman D. G. and Williams B. D. (2003) C. elegans PAT-6/actopaxin plays a critical role in the assembly of integrin adhesion complexes in vivo. Curr. Biol. 13: 922-932
    • (2003) Curr. Biol. , vol.13 , pp. 922-932
    • Lin, X.1    Qadota, H.2    Moerman, D.G.3    Williams, B.D.4
  • 6
  • 7
    • 0035861205 scopus 로고    scopus 로고
    • Genomic organization and expression profile of the parvin family of focal adhesion proteins in mice and humans
    • Korenbaum E., Olski T. M. and Noegel A. A. (2001) Genomic organization and expression profile of the parvin family of focal adhesion proteins in mice and humans. Gene 279: 69-79
    • (2001) Gene , vol.279 , pp. 69-79
    • Korenbaum, E.1    Olski, T.M.2    Noegel, A.A.3
  • 10
    • 0030026679 scopus 로고    scopus 로고
    • Regulation of cell adhesion and anchorage-dependent growth by a new beta 1-integrin-linked protein kinase
    • Hannigan G. E., Leung-Hagesteijn C., Fitz-Gibbon L., Coppolino M. G., Radeva G., Filmus J. et al. (1996) Regulation of cell adhesion and anchorage-dependent growth by a new beta 1-integrin-linked protein kinase. Nature 379: 91-96
    • (1996) Nature , vol.379 , pp. 91-96
    • Hannigan, G.E.1    Leung-Hagesteijn, C.2    Fitz-Gibbon, L.3    Coppolino, M.G.4    Radeva, G.5    Filmus, J.6
  • 11
    • 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. and Dedhar S. (2001) 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. 155: 505-510
    • (2001) J. Cell. Biol. , vol.155 , pp. 505-510
    • Wu, C.1    Dedhar, S.2
  • 13
    • 11144225205 scopus 로고    scopus 로고
    • Integrin-linked kinase: A cancer therapeutic target unique among its ILK
    • Hannigan G., Troussard A. A. and Dedhar S. (2005) Integrin-linked kinase: a cancer therapeutic target unique among its ILK. Nat. Rev. Cancer 5: 51-63
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 51-63
    • Hannigan, G.1    Troussard, A.A.2    Dedhar, S.3
  • 14
    • 0037059789 scopus 로고    scopus 로고
    • Molecular dissection of actopaxin-integrin-linked kinase-Paxillin interactions and their role in subcellular localization
    • Nikolopoulos S. N. and Turner C. E. (2002) Molecular dissection of actopaxin-integrin-linked kinase-Paxillin interactions and their role in subcellular localization. J. Biol. Chem. 277: 1568-1575
    • (2002) J. Biol. Chem. , vol.277 , pp. 1568-1575
    • Nikolopoulos, S.N.1    Turner, C.E.2
  • 15
    • 0037090578 scopus 로고    scopus 로고
    • Actopaxin is phosphorylated during mitosis and is a substrate for cyclin B1/cdc2 kinase
    • Curtis M., Nikolopoulos S. N. and Turner C. E. (2002) Actopaxin is phosphorylated during mitosis and is a substrate for cyclin B1/cdc2 kinase. Biochem. J. 363: 233-242
    • (2002) Biochem. J. , vol.363 , pp. 233-242
    • Curtis, M.1    Nikolopoulos, S.N.2    Turner, C.E.3
  • 16
    • 24344449538 scopus 로고    scopus 로고
    • Formation and phosphorylation of the PINCH-1-integrin linked kinase-{alpha}-parvin complex are important for regulation of renal glomerular podocyte adhesion, architecture and survival
    • Yang Y., Guo L., Blattner S. M., Mundel P., Kretzler M. and Wu C. (2005) Formation and phosphorylation of the PINCH-1-integrin linked kinase-{alpha}-parvin complex are important for regulation of renal glomerular podocyte adhesion, architecture and survival. J. Am. Soc. Nephrol. 16: 1966-1976
    • (2005) J. Am. Soc. Nephrol. , vol.16 , pp. 1966-1976
    • Yang, Y.1    Guo, L.2    Blattner, S.M.3    Mundel, P.4    Kretzler, M.5    Wu, C.6
  • 17
    • 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. and Wu C. (2004) 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. 279: 41695-41705
    • (2004) J. Biol. Chem. , vol.279 , pp. 41695-41705
    • Zhang, Y.1    Chen, K.2    Tu, Y.3    Wu, C.4
  • 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., Wu C. and Dedhar S. (2003) Integration of cell attachment, cytoskeletal localization and signaling by integrin-linked kinase (ILK), CH-ILKBP and the tumor suppressor PTEN. Mol. Biol. Cell 14: 4813-4825
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4813-4825
    • Attwell, S.1    Mills, J.2    Troussard, A.3    Wu, C.4    Dedhar, S.5
  • 19
    • 0037115611 scopus 로고    scopus 로고
    • Assembly of the PINCH-ILK-CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites
    • Zhang Y., Chen K., Tu Y., Velyvis A., Yang Y., Qin J. et al. (2002) Assembly of the PINCH-ILK-CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites. J. Cell. Sci. 115: 4777-4786
    • (2002) J. Cell. Sci. , vol.115 , pp. 4777-4786
    • Zhang, Y.1    Chen, K.2    Tu, Y.3    Velyvis, A.4    Yang, Y.5    Qin, J.6
  • 20
    • 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. and Wu C. (1999) The LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cells. Mol. Cell. Biol. 19: 2425-2434
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2425-2434
    • Tu, Y.1    Li, F.2    Goicoechea, S.3    Wu, C.4
  • 21
    • 0033379103 scopus 로고    scopus 로고
    • Integrin-linked kinase and PINCH: Partners in regulation of cell-extracellular matrix interaction and signal transduction
    • Wu C. (1999) Integrin-linked kinase and PINCH: partners in regulation of cell-extracellular matrix interaction and signal transduction. J. Cell. Sci. 112 (Pt 24): 4485-4489
    • (1999) J. Cell. Sci. , vol.112 , Issue.24 PART , pp. 4485-4489
    • Wu, C.1
  • 22
    • 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. and Wu C. (2003) PINCH-1 is an obligate partner of integrin-linked kinase (ILK) functioning in cell shape modulation, motility and survival. J. Biol. Chem. 278: 51324-51333
    • (2003) J. Biol. Chem. , vol.278 , pp. 51324-51333
    • Fukuda, T.1    Chen, K.2    Shi, X.3    Wu, C.4
  • 23
    • 0034529411 scopus 로고    scopus 로고
    • Paxillin interactions
    • Turner C. E. (2000) Paxillin interactions. J. Cell. Sci. 113 Pt 23: 4139-4140
    • (2000) J. Cell. Sci. , vol.113 , Issue.23 PART , pp. 4139-4140
    • Turner, C.E.1
  • 24
    • 0033666291 scopus 로고    scopus 로고
    • Paxillin and focal adhesion signalling
    • Turner C. E. (2000) Paxillin and focal adhesion signalling. Nat. Cell Biol. 2: E231-236
    • (2000) Nat. Cell Biol. , vol.2
    • Turner, C.E.1
  • 25
    • 20444400572 scopus 로고    scopus 로고
    • Actopaxin interacts with TESK1 to regulate cell spreading on fibronectin
    • LaLonde D. P., Brown M. C., Bouverat B. P. and Turner C. E. (2005) Actopaxin interacts with TESK1 to regulate cell spreading on fibronectin. J. Biol. Chem. 280: 21680-21688
    • (2005) J. Biol. Chem. , vol.280 , pp. 21680-21688
    • LaLonde, D.P.1    Brown, M.C.2    Bouverat, B.P.3    Turner, C.E.4
  • 26
    • 18844451747 scopus 로고    scopus 로고
    • Sprouty-4 negatively regulates cell spreading by inhibiting the kinase activity of testicular protein kinase
    • Tsumura Y., Toshima J., Leeksma O. C., Ohashi K. and Mizuno K. (2005) Sprouty-4 negatively regulates cell spreading by inhibiting the kinase activity of testicular protein kinase. Biochem. J. 387: 627-637
    • (2005) Biochem. J. , vol.387 , pp. 627-637
    • Tsumura, Y.1    Toshima, J.2    Leeksma, O.C.3    Ohashi, K.4    Mizuno, K.5
  • 27
    • 0035900680 scopus 로고    scopus 로고
    • Binding of 14-3-3beta regulates the kinase activity and subcellular localization of testicular protein kinase 1
    • Toshima J. Y., Toshima J., Watanabe T. and Mizuno K. (2001) Binding of 14-3-3beta regulates the kinase activity and subcellular localization of testicular protein kinase 1. J. Biol. Chem. 276: 43471-43481
    • (2001) J. Biol. Chem. , vol.276 , pp. 43471-43481
    • Toshima, J.Y.1    Toshima, J.2    Watanabe, T.3    Mizuno, K.4
  • 28
  • 29
    • 2542468783 scopus 로고    scopus 로고
    • Affixin interacts with alpha-actinin and mediates integrin signaling for reorganization of F-actin induced by initial cell-substrate interaction
    • Yamaji S., Suzuki A., Kanamori H., Mishima W., Yoshimi R., Takasaki H. et al. (2004) Affixin interacts with alpha-actinin and mediates integrin signaling for reorganization of F-actin induced by initial cell-substrate interaction. J. Cell. Biol. 165: 539-551
    • (2004) J. Cell. Biol. , vol.165 , pp. 539-551
    • Yamaji, S.1    Suzuki, A.2    Kanamori, H.3    Mishima, W.4    Yoshimi, R.5    Takasaki, H.6
  • 30
    • 0037439424 scopus 로고    scopus 로고
    • Interaction of alphaPIX (ARHGEF6) with beta-parvin (PARVB) suggests an involvement of alphaPIX in integrin-mediated signaling
    • Rosenberger G., Jantke I., Gal A. and Kutsche K. (2003) Interaction of alphaPIX (ARHGEF6) with beta-parvin (PARVB) suggests an involvement of alphaPIX in integrin-mediated signaling. Hum. Mol. Genet. 12: 155-167
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 155-167
    • Rosenberger, G.1    Jantke, I.2    Gal, A.3    Kutsche, K.4
  • 32
    • 0035516140 scopus 로고    scopus 로고
    • Transmembrane crosstalk between the extracellular matrix - Cytoskeleton crosstalk
    • Geiger B., Bershadsky A., Pankov R. and Yamada K. M. (2001) Transmembrane crosstalk between the extracellular matrix - cytoskeleton crosstalk. Nat. Rev. Mol. Cell. Biol. 2: 793-805
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 793-805
    • Geiger, B.1    Bershadsky, A.2    Pankov, R.3    Yamada, K.M.4
  • 33
    • 0036673109 scopus 로고    scopus 로고
    • Regulation of fibronectin matrix deposition and cell proliferation by the PINCH-ILK-CH-IL-KBP complex
    • Guo L. and Wu C. (2002) Regulation of fibronectin matrix deposition and cell proliferation by the PINCH-ILK-CH-IL-KBP complex. FASEB J. 16: 1298-1300
    • (2002) FASEB J. , vol.16 , pp. 1298-1300
    • Guo, L.1    Wu, C.2
  • 34
    • 0035968234 scopus 로고    scopus 로고
    • Integrin-linked kinase (ILK) binding to paxillin LD1 motif regulates ILK localization to focal adhesions
    • Nikolopoulos S. N. and Turner C. E. (2001) Integrin-linked kinase (ILK) binding to paxillin LD1 motif regulates ILK localization to focal adhesions. J. Biol. Chem. 276: 23499-23505
    • (2001) J. Biol. Chem. , vol.276 , pp. 23499-23505
    • Nikolopoulos, S.N.1    Turner, C.E.2
  • 35
    • 4544371915 scopus 로고    scopus 로고
    • Phosphorylation of actopaxin regulates cell spreading and migration
    • Clarke D. M., Brown M. C., LaLonde D. P. and Turner C. E. (2004) Phosphorylation of actopaxin regulates cell spreading and migration. J. Cell. Biol. 166: 901-912
    • (2004) J. Cell. Biol. , vol.166 , pp. 901-912
    • Clarke, D.M.1    Brown, M.C.2    LaLonde, D.P.3    Turner, C.E.4
  • 36
    • 27944479854 scopus 로고    scopus 로고
    • RHO GTPases: Biochemistry and biology
    • Jaffe A. B. and Hall A. (2005) RHO GTPases: biochemistry and biology. Annu. Rev. Cell Dev. Biol. 21: 247-269
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 247-269
    • Jaffe, A.B.1    Hall, A.2
  • 37
    • 12144291549 scopus 로고    scopus 로고
    • The first CH domain of affixin activates Cdc42 and Rac1 through alphaPIX, a Cdc42/Rac1-specific guanine nucleotide exchanging factor
    • Mishima W., Suzuki A., Yamaji S., Yoshimi R., Ueda A., Kaneko T. et al. (2004) The first CH domain of affixin activates Cdc42 and Rac1 through alphaPIX, a Cdc42/Rac1-specific guanine nucleotide exchanging factor. Genes Cells 9: 193-204
    • (2004) Genes Cells , vol.9 , pp. 193-204
    • Mishima, W.1    Suzuki, A.2    Yamaji, S.3    Yoshimi, R.4    Ueda, A.5    Kaneko, T.6
  • 38
    • 14844310304 scopus 로고    scopus 로고
    • AlphaPIX associates with calpain 4, the small subunit of calpain, and has a dual role in integrin-mediated cell spreading
    • Rosenberger G., Gal A. and Kutsche K. (2005) AlphaPIX associates with calpain 4, the small subunit of calpain, and has a dual role in integrin-mediated cell spreading. J. Biol. Chem. 280: 6879-6889
    • (2005) J. Biol. Chem. , vol.280 , pp. 6879-6889
    • Rosenberger, G.1    Gal, A.2    Kutsche, K.3
  • 39
    • 0035793946 scopus 로고    scopus 로고
    • Identification and kinetic analysis of the interaction between Nck-2 and DOCK180
    • Tu Y., Kucik D. F. and Wu C. (2001) Identification and kinetic analysis of the interaction between Nck-2 and DOCK180. FEBS Lett. 491: 193-199
    • (2001) FEBS Lett. , vol.491 , pp. 193-199
    • Tu, Y.1    Kucik, D.F.2    Wu, C.3
  • 40
    • 0031772910 scopus 로고    scopus 로고
    • Nck-2, a novel Src homology2/3-containing adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase-signaling pathways
    • Tu Y., Li F. and Wu C. (1998) Nck-2, a novel Src homology2/3-containing adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase-signaling pathways. Mol. Biol. Cell. 9: 3367-3382
    • (1998) Mol. Biol. Cell. , vol.9 , pp. 3367-3382
    • Tu, Y.1    Li, F.2    Wu, C.3
  • 42
    • 13944249955 scopus 로고    scopus 로고
    • Structure of an ultraweak protein-protein complex and its crucial role in regulation of cell morphology and motility
    • Vaynberg J., Fukuda T., Chen K., Vinogradova O., Velyvis A., Tu Y. et al. (2005) Structure of an ultraweak protein-protein complex and its crucial role in regulation of cell morphology and motility. Mol. Cell 17: 513-523
    • (2005) Mol. Cell , vol.17 , pp. 513-523
    • Vaynberg, J.1    Fukuda, T.2    Chen, K.3    Vinogradova, O.4    Velyvis, A.5    Tu, Y.6
  • 43
    • 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., Zha X., Qin J. and Wu C. (2005) Molecular dissection of PINCH-1 reveals a mechanism of coupling and uncoupling of cell shape modulation and survival. J. Biol. Chem. 280: 27631-27637
    • (2005) J. Biol. Chem. , vol.280 , pp. 27631-27637
    • Xu, Z.1    Fukuda, T.2    Li, Y.3    Zha, X.4    Qin, J.5    Wu, C.6
  • 44
    • 0037417416 scopus 로고    scopus 로고
    • CH-ILKBP regulates cell survival by facilitating the membrane translocation of protein kinase B/Akt
    • Fukuda T., Guo L., Shi X. and Wu C. (2003) CH-ILKBP regulates cell survival by facilitating the membrane translocation of protein kinase B/Akt. J. Cell. Biol. 160: 1001-1008
    • (2003) J. Cell. Biol. , vol.160 , pp. 1001-1008
    • Fukuda, T.1    Guo, L.2    Shi, X.3    Wu, C.4
  • 45
    • 3042708179 scopus 로고    scopus 로고
    • The PINCH-ILK-parvin complexes: Assembly, functions and regulation
    • Wu C. (2004) The PINCH-ILK-parvin complexes: assembly, functions and regulation. Biochim. Biophys. Acta 1692: 55-62
    • (2004) Biochim. Biophys. Acta , vol.1692 , pp. 55-62
    • Wu, C.1
  • 46
    • 0035920145 scopus 로고    scopus 로고
    • Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: Critical roles for kinase activity and amino acids arginine 211 and serine 343
    • Persad S., Attwell S., Gray V., Mawji N., Deng J. T., Leung D. et al. (2001) Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: critical roles for kinase activity and amino acids arginine 211 and serine 343. J. Biol. Chem. 276: 27462-27469
    • (2001) J. Biol. Chem. , vol.276 , pp. 27462-27469
    • Persad, S.1    Attwell, S.2    Gray, V.3    Mawji, N.4    Deng, J.T.5    Leung, D.6
  • 47
    • 25144434380 scopus 로고    scopus 로고
    • Assembly and signaling of adhesion complexes
    • Sepulveda J., Gkretsi V. and Wu C. (2005) Assembly and signaling of adhesion complexes. Curr. Top. Dev. Biol. 68: 183-225
    • (2005) Curr. Top. Dev. Biol. , vol.68 , pp. 183-225
    • Sepulveda, J.1    Gkretsi, V.2    Wu, C.3
  • 48
    • 0035833261 scopus 로고    scopus 로고
    • Obscurin, a giant sarcomeric Rho guanine nucleotide exchange factor protein involved in sarcomere assembly
    • Young P., Ehler E. and Gautel M. (2001) Obscurin, a giant sarcomeric Rho guanine nucleotide exchange factor protein involved in sarcomere assembly. J. Cell Biol. 154: 123-136
    • (2001) J. Cell Biol. , vol.154 , pp. 123-136
    • Young, P.1    Ehler, E.2    Gautel, M.3
  • 49
    • 0141868811 scopus 로고    scopus 로고
    • Rapid response of cardiac obscurin gene cluster to aortic stenosis: Differential activation of Rho-GEF and MLCK and involvement in hypertrophic growth
    • Borisov A. B., Raeker M. O., Kontrogianni-Konstantopoulos A., Yang K., Kurnit D. M., Bloch R. J. et al. (2003) Rapid response of cardiac obscurin gene cluster to aortic stenosis: differential activation of Rho-GEF and MLCK and involvement in hypertrophic growth. Biochem. Biophys. Res. Commun. 310: 910-918
    • (2003) Biochem. Biophys. Res. Commun. , vol.310 , pp. 910-918
    • Borisov, A.B.1    Raeker, M.O.2    Kontrogianni-Konstantopoulos, A.3    Yang, K.4    Kurnit, D.M.5    Bloch, R.J.6
  • 50
    • 4143108034 scopus 로고    scopus 로고
    • Dynamics of obscurin localization during differentiation and remodeling of cardiac myocytes: Obscurin as an integrator of myofibrillar structure
    • Borisov A. B., Kontrogianni-Konstantopoulos A., Bloch R. J., Westfall M. V. and Russell M. W. (2004) Dynamics of obscurin localization during differentiation and remodeling of cardiac myocytes: obscurin as an integrator of myofibrillar structure. J. Histochem. Cytochem. 52: 1117-1127
    • (2004) J. Histochem. Cytochem. , vol.52 , pp. 1117-1127
    • Borisov, A.B.1    Kontrogianni-Konstantopoulos, A.2    Bloch, R.J.3    Westfall, M.V.4    Russell, M.W.5
  • 51
    • 27144445241 scopus 로고    scopus 로고
    • Role of the integrin-linked kinase/PINCH1/alpha-parvin complex in cardiac myocyte hypertrophy
    • Sep. 10 [Epub ahead of print]
    • Chen H., Huang X. N., Yan W., Chen K., Guo L., Tummalapali L. et al. (2005) Role of the integrin-linked kinase/PINCH1/alpha-parvin complex in cardiac myocyte hypertrophy. Lab. Invest. Sep. 10 [Epub ahead of print]
    • (2005) Lab. Invest.
    • Chen, H.1    Huang, X.N.2    Yan, W.3    Chen, K.4    Guo, L.5    Tummalapali, L.6
  • 52
    • 0032167411 scopus 로고    scopus 로고
    • A requirement for the rac1 GTPase in the signal transduction pathway leading to cardiac myocyte hypertrophy
    • Pracyk J. B., Tanaka K., Hegland D. D., Kim K. S., Sethi R., Rovira I. I. et al. (1998) A requirement for the rac1 GTPase in the signal transduction pathway leading to cardiac myocyte hypertrophy. J. Clin. Invest. 102: 929-937
    • (1998) J. Clin. Invest. , vol.102 , pp. 929-937
    • Pracyk, J.B.1    Tanaka, K.2    Hegland, D.D.3    Kim, K.S.4    Sethi, R.5    Rovira, I.I.6
  • 54
    • 0038724824 scopus 로고    scopus 로고
    • The role of integrin-linked kinase (ILK) in cancer progression
    • Persad S. and Dedhar S. (2003) The role of integrin-linked kinase (ILK) in cancer progression. Cancer Metastasis Rev. 22: 375-384
    • (2003) Cancer Metastasis Rev. , vol.22 , pp. 375-384
    • Persad, S.1    Dedhar, S.2
  • 55
    • 0034214364 scopus 로고    scopus 로고
    • A region of deletion on chromosome 22q13 is common to human breast and colorectal cancers
    • Castells A., Gusella J. F., Ramesh V. and Rustgi A. K. (2000) A region of deletion on chromosome 22q13 is common to human breast and colorectal cancers. Cancer Res. 60: 2836-2839
    • (2000) Cancer Res. , vol.60 , pp. 2836-2839
    • Castells, A.1    Gusella, J.F.2    Ramesh, V.3    Rustgi, A.K.4
  • 57
    • 0035152114 scopus 로고    scopus 로고
    • The distribution and regulation of integrin-linked kinase in normal and diabetic kidneys
    • Guo L., Sanders P. W., Woods A. and Wu C. (2001) The distribution and regulation of integrin-linked kinase in normal and diabetic kidneys. Am. J. Pathol. 159: 1735-1742
    • (2001) Am. J. Pathol. , vol.159 , pp. 1735-1742
    • Guo, L.1    Sanders, P.W.2    Woods, A.3    Wu, C.4
  • 59
    • 0034676338 scopus 로고    scopus 로고
    • The integrin linked kinase (ILK) induces an invasive phenotype via AP-1 transcription factor-dependent upregulation of matrix metalloproteinase 9 (MMP-9)
    • Troussard A. A., Costello P., Yoganathan T. N., Kumagai S., Roskelley C. D. and Dedhar S. (2000) The integrin linked kinase (ILK) induces an invasive phenotype via AP-1 transcription factor-dependent upregulation of matrix metalloproteinase 9 (MMP-9). Oncogene 19: 5444-5452
    • (2000) Oncogene , vol.19 , pp. 5444-5452
    • Troussard, A.A.1    Costello, P.2    Yoganathan, T.N.3    Kumagai, S.4    Roskelley, C.D.5    Dedhar, S.6
  • 60
    • 0036661041 scopus 로고    scopus 로고
    • Identification of a signal transduction pathway that regulates MMP-9 mRNA expression in glomerular injury
    • von Luttichau I., Djafarzadeh R., Henger A., Cohen C. D., Mojaat A., Jochum M. et al. (2002) Identification of a signal transduction pathway that regulates MMP-9 mRNA expression in glomerular injury. Biol. Chem. 383: 1271-1275
    • (2002) Biol. Chem. , vol.383 , pp. 1271-1275
    • Von Luttichau, I.1    Djafarzadeh, R.2    Henger, A.3    Cohen, C.D.4    Mojaat, A.5    Jochum, M.6
  • 62
    • 0141720342 scopus 로고    scopus 로고
    • Role for integrin-linked kinase in mediating tubular epithelial to mesenchymal transition and renal interstitial fibrogenesis
    • Li Y., Yang J., Dai C., Wu C. and Liu Y. (2003) Role for integrin-linked kinase in mediating tubular epithelial to mesenchymal transition and renal interstitial fibrogenesis. J. Clin. Invest. 112: 503-516
    • (2003) J. Clin. Invest. , vol.112 , pp. 503-516
    • Li, Y.1    Yang, J.2    Dai, C.3    Wu, C.4    Liu, Y.5
  • 63
    • 0037418837 scopus 로고    scopus 로고
    • Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation
    • Tu Y., Wu S., Shi X., Chen K. and Wu C. (2003) Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation. Cell 113: 37-47
    • (2003) Cell , vol.113 , pp. 37-47
    • Tu, Y.1    Wu, S.2    Shi, X.3    Chen, K.4    Wu, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.