메뉴 건너뛰기




Volumn 124, Issue 6, 2011, Pages 879-891

Kindlin-2 regulates podocyte adhesion and fibronectin matrix deposition through interactions with phosphoinositides and integrins

Author keywords

Fibronectin; Integrin; Kindlin; Podocyte; TGF beta

Indexed keywords

BINDING PROTEIN; FIBRONECTIN; INTEGRIN; KINDLIN 2; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE; TRANSFORMING GROWTH FACTOR BETA1; UNCLASSIFIED DRUG;

EID: 79952802913     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.076976     Document Type: Article
Times cited : (89)

References (55)
  • 1
    • 0141569607 scopus 로고    scopus 로고
    • Podocyte biology and the emerging understanding of podocyte diseases
    • DOI 10.1159/000072917
    • Barisoni, L. and Mundel, P. (2003). Podocyte biology and the emerging understanding of podocyte diseases. Am. J. Nephrol. 23, 353-360. (Pubitemid 37116935)
    • (2003) American Journal of Nephrology , vol.23 , Issue.5 , pp. 353-360
    • Barisoni, L.1    Mundel, P.2
  • 2
  • 3
    • 1442331993 scopus 로고    scopus 로고
    • Integrin activation
    • Calderwood, D. A. (2004). Integrin activation. J. Cell Sci. 117, 657-666.
    • (2004) J. Cell Sci. , vol.117 , pp. 657-666
    • Calderwood, D.A.1
  • 4
    • 30344443955 scopus 로고    scopus 로고
    • Prediction of CASP6 structures using automated Robetta protocols
    • Chivian, D., Kim, D. E., Malmstrom, L., Schonbrun, J., Rohl, C. A. and Baker, D. (2005). Prediction of CASP6 structures using automated Robetta protocols. Proteins 61 Suppl. 7, 157-166.
    • (2005) Proteins , vol.61 , Issue.SUPPL. 7 , pp. 157-166
    • Chivian, D.1    Kim, D.E.2    Malmstrom, L.3    Schonbrun, J.4    Rohl, C.A.5    Baker, D.6
  • 5
  • 6
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J. and Bax, A. (1995). NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 7
    • 41949127144 scopus 로고    scopus 로고
    • Kindlin-2 is an essential component of intercalated discs and is required for vertebrate cardiac structure and function
    • Dowling, J. J., Gibbs, E., Russell, M., Goldman, D., Minarcik, J., Golden, J. A. and Feldman, E. L. (2008a). Kindlin-2 is an essential component of intercalated discs and is required for vertebrate cardiac structure and function. Circ. Res. 102, 423-431.
    • (2008) Circ. Res. , vol.102 , pp. 423-431
    • Dowling, J.J.1    Gibbs, E.2    Russell, M.3    Goldman, D.4    Minarcik, J.5    Golden, J.A.6    Feldman, E.L.7
  • 8
    • 48249112975 scopus 로고    scopus 로고
    • Kindlin-2 is required for myocyte elongation and is essential for myogenesis
    • Dowling, J. J., Vreede, A. P., Kim, S., Golden, J. and Feldman, E. L. (2008b). Kindlin-2 is required for myocyte elongation and is essential for myogenesis. BMC Cell Biol. 9, 36.
    • (2008) BMC Cell Biol. , vol.9 , pp. 36
    • Dowling, J.J.1    Vreede, A.P.2    Kim, S.3    Golden, J.4    Feldman, E.L.5
  • 9
    • 34848907421 scopus 로고    scopus 로고
    • Actin up: Regulation of podocyte structure and function by components of the actin cytoskeleton
    • DOI 10.1016/j.tcb.2007.06.006, PII S0962892407001675
    • Faul, C., Asanuma, K., Yanagida-Asanuma, E., Kim, K. and Mundel, P. (2007). Actin up: regulation of podocyte structure and function by components of the actin cytoskeleton. Trends Cell Biol. 17, 428-437. (Pubitemid 47499042)
    • (2007) Trends in Cell Biology , vol.17 , Issue.9 , pp. 428-437
    • Faul, C.1    Asanuma, K.2    Yanagida-Asanuma, E.3    Kim, K.4    Mundel, P.5
  • 12
    • 46149093439 scopus 로고    scopus 로고
    • Structural Basis for the Autoinhibition of Talin in Regulating Integrin Activation
    • DOI 10.1016/j.molcel.2008.06.011, PII S1097276508004292
    • Goksoy, E., Ma, Y. Q., Wang, X., Kong, X., Perera, D., Plow, E. F. and Qin, J. (2008). Structural basis for the autoinhibition of talin in regulating integrin activation. Mol. Cell 31, 124-133. (Pubitemid 351905930)
    • (2008) Molecular Cell , vol.31 , Issue.1 , pp. 124-133
    • Goksoy, E.1    Ma, Y.-Q.2    Wang, X.3    Kong, X.4    Perera, D.5    Plow, E.F.6    Qin, J.7
  • 13
    • 0031915139 scopus 로고    scopus 로고
    • Thrombospondin signaling of FA disassembly requires activation of phosphoinositide 3-kinase
    • Greenwood, J. A., Pallero, M. A., Theibert, A. B. and Murphy-Ullrich, J. E. (1998). Thrombospondin signaling of FA disassembly requires activation of phosphoinositide 3-kinase. J. Biol. Chem. 273, 1755-1763.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1755-1763
    • Greenwood, J.A.1    Pallero, M.A.2    Theibert, A.B.3    Murphy-Ullrich, J.E.4
  • 14
    • 0034618121 scopus 로고    scopus 로고
    • Restructuring of fa plaques by pi 3-kinase: Regulation by ptdins (3,4,5-p)3 binding to {alpha}-actinin
    • Greenwood, J. A., Theibert, A. B., Prestwich, G. D. and Murphy-Ullrich, J. E. (2000). Restructuring of fa plaques by pi 3-kinase: regulation by ptdins (3,4,5-p)3 binding to {alpha}-actinin. J. Cell Biol. 150, 627-642.
    • (2000) J. Cell Biol. , vol.150 , pp. 627-642
    • Greenwood, J.A.1    Theibert, A.B.2    Prestwich, G.D.3    Murphy-Ullrich, J.E.4
  • 15
    • 0036673109 scopus 로고    scopus 로고
    • Regulation of fibronectin matrix deposition and cell proliferation by the PINCH-ILK-CH-ILKBP complex
    • Guo, L. and Wu, C. (2002). Regulation of fibronectin matrix deposition and cell proliferation by the PINCH-ILK-CH-ILKBP complex. FASEB J. 16, 1298-1300.
    • (2002) FASEB J. , vol.16 , pp. 1298-1300
    • Guo, L.1    Wu, C.2
  • 16
    • 66449119343 scopus 로고    scopus 로고
    • Kindlin-1 and -2 directly bind the C-terminal region of beta integrin cytoplasmic tails and exert integrin-specific activation effects
    • Harburger, D. S., Bouaouina, M. and Calderwood, D. A. (2009). Kindlin-1 and -2 directly bind the C-terminal region of beta integrin cytoplasmic tails and exert integrin-specific activation effects. J. Biol. Chem. 284, 11485-11497.
    • (2009) J. Biol. Chem. , vol.284 , pp. 11485-11497
    • Harburger, D.S.1    Bouaouina, M.2    Calderwood, D.A.3
  • 17
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes, R. O. (2002). Integrins: bidirectional, allosteric signaling machines. Cell 110, 673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 18
    • 0032530384 scopus 로고    scopus 로고
    • Identification and analysis of PH domain-containing targets of phosphatidylinositol 3-kinase using a novel in vivo assay in yeast
    • Isakoff, S. J., Cardozo, T., Andreev, J., Li, Z., Ferguson, K. M., Abagyan, R., Lemmon, M. A., Aronheim, A. and Skolnik, E. Y. (1998). Identification and analysis of PH domain-containing targets of phosphatidylinositol 3-kinase using a novel in vivo assay in yeast. EMBO J. 17, 5374-5387.
    • (1998) EMBO J. , vol.17 , pp. 5374-5387
    • Isakoff, S.J.1    Cardozo, T.2    Andreev, J.3    Li, Z.4    Ferguson, K.M.5    Abagyan, R.6    Lemmon, M.A.7    Aronheim, A.8    Skolnik, E.Y.9
  • 19
    • 2342486055 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinases and the regulation of platelet function
    • Jackson, S. P., Yap, C. L. and Anderson, K. E. (2004). Phosphoinositide 3-kinases and the regulation of platelet function. Biochem. Soc. Trans. 32, 387-392.
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 387-392
    • Jackson, S.P.1    Yap, C.L.2    Anderson, K.E.3
  • 20
    • 0029943605 scopus 로고    scopus 로고
    • Membrane localization of phosphatidylinositol 3-kinase is sufficient to activate multiple signal-transducing kinase pathways
    • Klippel, A., Reinhard, C., Kavanaugh, W. M., Apell, G., Escobedo, M. A. and Williams, L. T. (1996). Membrane localization of phosphatidylinositol 3-kinase is sufficient to activate multiple signal-transducing kinase pathways. Mol. Cell. Biol. 16, 4117-4127.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4117-4127
    • Klippel, A.1    Reinhard, C.2    Kavanaugh, W.M.3    Apell, G.4    Escobedo, M.A.5    Williams, L.T.6
  • 21
    • 0029050557 scopus 로고
    • Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation
    • Kovacsovics, T., Bachelot, C., Toker, A., Vlahos, C., Duckworth, B., Cantley, L. and Hartwig, J. (1995). Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation. J. Biol. Chem. 270, 11358-11366.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11358-11366
    • Kovacsovics, T.1    Bachelot, C.2    Toker, A.3    Vlahos, C.4    Duckworth, B.5    Cantley, L.6    Hartwig, J.7
  • 22
    • 77649181584 scopus 로고    scopus 로고
    • The role of kindlins in cell biology and relevance to human disease
    • Lai-Cheong, J. E., Parsons, M. and McGrath, J. A. (2010). The role of kindlins in cell biology and relevance to human disease. Int. J. Biochem. Cell Biol. 42, 595-603.
    • (2010) Int. J. Biochem. Cell Biol. , vol.42 , pp. 595-603
    • Lai-Cheong, J.E.1    Parsons, M.2    McGrath, J.A.3
  • 23
    • 57049169143 scopus 로고    scopus 로고
    • Kindlins: Essential regulators of integrin signalling and cell-matrix adhesion
    • Larjava, H., Plow, E. F. and Wu, C. (2008). Kindlins: essential regulators of integrin signalling and cell-matrix adhesion. EMBO Rep. 9, 1203-1208.
    • (2008) EMBO Rep. , vol.9 , pp. 1203-1208
    • Larjava, H.1    Plow, E.F.2    Wu, C.3
  • 24
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • Lemmon, M. A. (2008). Membrane recognition by phospholipid-binding domains. Nat. Rev. Mol. Cell Biol. 9, 99-111.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 99-111
    • Lemmon, M.A.1
  • 25
    • 0034663568 scopus 로고    scopus 로고
    • Signal-dependent membrane targeting by pleckstrin homology (PH) domains
    • Lemmon, M. A. and Ferguson, K. M. (2000). Signal-dependent membrane targeting by pleckstrin homology (PH) domains. Biochem. J. 350, 1-18.
    • (2000) Biochem. J. , vol.350 , pp. 1-18
    • Lemmon, M.A.1    Ferguson, K.M.2
  • 26
    • 39549098861 scopus 로고    scopus 로고
    • Epithelial-to-mesenchymal transition is a potential pathway leading to podocyte dysfunction and proteinuria
    • DOI 10.2353/ajpath.2008.070057
    • Li, Y., Kang, Y. S., Dai, C., Kiss, L. P., Wen, X. and Liu, Y. (2008). Epithelial-to-mesenchymal transition is a potential pathway leading to podocyte dysfunction and proteinuria. Am. J. Pathol. 172, 299-308. (Pubitemid 351282018)
    • (2008) American Journal of Pathology , vol.172 , Issue.2 , pp. 299-308
    • Li, Y.1    Kang, Y.S.2    Dai, C.3    Kiss, L.P.4    Wen, X.5    Liu, Y.6
  • 27
    • 15844363687 scopus 로고    scopus 로고
    • Activated conformations of very late activation integrins detected by a group of antibodies (HUTS) specific for a novel regulatory region (355-425) of the common beta1 chain
    • DOI 10.1074/jbc.271.19.11067
    • Luque, A., Gomez, M., Puzon, W., Takada, Y., Sanchez-Madrid, F. and Cabanas, C. (1996). Activated conformations of very late activation integrins detected by a group of antibodies (HUTS) specific for a novel regulatory region (355-425) of the common beta 1 chain. J. Biol. Chem. 271, 11067-11075. (Pubitemid 26155933)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.19 , pp. 11067-11075
    • Luque, A.1    Gomez, M.2    Puzon, W.3    Takada, Y.4    Sanchez-Madrid, F.5    Cabanas, C.6
  • 28
    • 34250768894 scopus 로고    scopus 로고
    • Platelet integrin alpha(IIb)beta(3): Activation mechanisms
    • Ma, Y. Q., Qin, J. and Plow, E. F. (2007). Platelet integrin alpha(IIb)beta(3): activation mechanisms. J. Thromb. Haemost. 5, 1345-1352.
    • (2007) J. Thromb. Haemost. , vol.5 , pp. 1345-1352
    • Ma, Y.Q.1    Qin, J.2    Plow, E.F.3
  • 29
    • 43149085289 scopus 로고    scopus 로고
    • Kindlin-2 (Mig-2): A co-activator of beta3 integrins
    • Ma, Y. Q., Qin, J., Wu, C. and Plow, E. F. (2008). Kindlin-2 (Mig-2): a co-activator of beta3 integrins. J. Cell Biol. 181, 439-446.
    • (2008) J. Cell Biol. , vol.181 , pp. 439-446
    • Ma, Y.Q.1    Qin, J.2    Wu, C.3    Plow, E.F.4
  • 31
    • 66149128873 scopus 로고    scopus 로고
    • The tail of integrins, talin, and kindlins
    • Moser, M., Legate, K. R., Zent, R. and Fassler, R. (2009). The tail of integrins, talin, and kindlins. Science 324, 895-899.
    • (2009) Science , vol.324 , pp. 895-899
    • Moser, M.1    Legate, K.R.2    Zent, R.3    Fassler, R.4
  • 32
    • 33750520931 scopus 로고    scopus 로고
    • Matrix-specific suppression of integrin activation in shear stress signaling
    • Orr, A. W., Ginsberg, M. H., Shattil, S. J., Deckmyn, H. and Schwartz, M. A. (2006). Matrix-specific suppression of integrin activation in shear stress signaling. Mol. Biol. Cell 17, 4686-4697.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4686-4697
    • Orr, A.W.1    Ginsberg, M.H.2    Shattil, S.J.3    Deckmyn, H.4    Schwartz, M.A.5
  • 33
    • 0033618460 scopus 로고    scopus 로고
    • Mechanisms and consequences of affinity modulation of integrin alpha(V)beta(3) detected with a novel patch-engineered monovalent ligand
    • Pampori, N., Hato, T., Stupack, D. G., Aidoudi, S., Cheresh, D. A., Nemerow, G. R. and Shattil, S. J. (1999). Mechanisms and consequences of affinity modulation of integrin alpha(V)beta(3) detected with a novel patch-engineered monovalent ligand. J. Biol. Chem. 274, 21609-21616.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21609-21616
    • Pampori, N.1    Hato, T.2    Stupack, D.G.3    Aidoudi, S.4    Cheresh, D.A.5    Nemerow, G.R.6    Shattil, S.J.7
  • 34
    • 34548707077 scopus 로고    scopus 로고
    • Increased cytoplasmic level of migfilin is associated with higher grades of human leiomyosarcoma
    • DOI 10.1111/j.1365-2559.2007.02791.x
    • Papachristou, D. J., Gkretsi, V., Tu, Y., Shi, X., Chen, K., Larjava, H., Rao, U. N. and Wu, C. (2007). Increased cytoplasmic level of migfilin is associated with higher grades of human leiomyosarcoma. Histopathology 51, 499-508. (Pubitemid 47437823)
    • (2007) Histopathology , vol.51 , Issue.4 , pp. 499-508
    • Papachristou, D.J.1    Gkretsi, V.2    Tu, Y.3    Shi, X.4    Chen, K.5    Larjava, H.6    Rao, U.N.M.7    Wu, C.8
  • 35
    • 0037207471 scopus 로고    scopus 로고
    • Cell biology of the glomerular podocyte
    • Pavenstadt, H., Kriz, W. and Kretzler, M. (2003). Cell biology of the glomerular podocyte. Physiol. Rev. 83, 253-307. (Pubitemid 36459882)
    • (2003) Physiological Reviews , vol.83 , Issue.1 , pp. 253-307
    • Pavenstadt, H.1    Kriz, W.2    Kretzler, M.3
  • 36
    • 69549114537 scopus 로고    scopus 로고
    • Kindling the flame of integrin activation and function with kindlins
    • Plow, E. F., Qin, J. and Byzova, T. (2009). Kindling the flame of integrin activation and function with kindlins. Curr. Opin. Hematol. 16, 323-328.
    • (2009) Curr. Opin. Hematol. , vol.16 , pp. 323-328
    • Plow, E.F.1    Qin, J.2    Byzova, T.3
  • 37
    • 0034632070 scopus 로고    scopus 로고
    • The UNC-112 gene in Caenorhabditis elegans encodes a novel component of cell-matrix adhesion structures required for integrin localization in the muscle cell membrane
    • Rogalski, T. M., Mullen, G. P., Gilbert, M. M., Williams, B. D. and Moerman, D. G. (2000). The UNC-112 gene in Caenorhabditis elegans encodes a novel component of cell-matrix adhesion structures required for integrin localization in the muscle cell membrane. J. Cell Biol. 150, 253-264.
    • (2000) J. Cell Biol. , vol.150 , pp. 253-264
    • Rogalski, T.M.1    Mullen, G.P.2    Gilbert, M.M.3    Williams, B.D.4    Moerman, D.G.5
  • 39
    • 33747852615 scopus 로고    scopus 로고
    • Glomerular epithelial cells transform to myofibroblasts: Early but not late removal of TGF-beta1 reverses transformation
    • Sam, R., Wanna, L., Gudehithlu, K. P., Garber, S. L., Dunea, G., Arruda, J. A. and Singh, A. K. (2006). Glomerular epithelial cells transform to myofibroblasts: early but not late removal of TGF-beta1 reverses transformation. Transl Res 148, 142-148.
    • (2006) Transl Res , vol.148 , pp. 142-148
    • Sam, R.1    Wanna, L.2    Gudehithlu, K.P.3    Garber, S.L.4    Dunea, G.5    Arruda, J.A.6    Singh, A.K.7
  • 40
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede, T., Kopp, J., Guex, N. and Peitsch, M. C. (2003). SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31, 3381-3385.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 41
    • 34547120497 scopus 로고    scopus 로고
    • The MIG-2/integrin interaction strengthens cell-matrix adhesion and modulates cell motility
    • DOI 10.1074/jbc.M611680200
    • Shi, X., Ma, Y. Q., Tu, Y., Chen, K., Wu, S., Fukuda, K., Qin, J., Plow, E. F. and Wu, C. (2007). The MIG-2/integrin interaction strengthens cell-matrix adhesion and modulates cell motility. J. Biol. Chem. 282, 20455-20466. (Pubitemid 47100027)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.28 , pp. 20455-20466
    • Shi, X.1    Ma, Y.-Q.2    Tu, Y.3    Chen, K.4    Wu, S.5    Fukuda, K.6    Qin, J.7    Plow, E.F.8    Wu, C.9
  • 42
    • 0029583193 scopus 로고
    • A role for phosphatidylinositol 3-kinase in the regulation of beta1 integrin activity by the CD2 antigen
    • DOI 10.1083/jcb.131.6.1867
    • Shimizu, Y., Mobley, J., Finkelstein, L. and Chan, A. (1995). A role for phosphatidylinositol 3-kinase in the regulation of beta 1 integrin activity by the CD2 antigen. J. Cell Biol. 131, 1867-1880. (Pubitemid 26007982)
    • (1995) Journal of Cell Biology , vol.131 , Issue.6 II , pp. 1867-1880
    • Shimizu, Y.1    Mobley, J.L.2    Finkelstein, L.D.3    Chan, A.S.H.4
  • 44
    • 0037418837 scopus 로고    scopus 로고
    • Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation
    • DOI 10.1016/S0092-8674(03)00163-6
    • Tu, Y., Wu, S., Shi, X., Chen, K. and Wu, C. (2003). Migfilin and mig-2 link FAs to filamin and the actin cytoskeleton and function in cell shape modulation. Cell 113, 37-47. (Pubitemid 36411958)
    • (2003) Cell , vol.113 , Issue.1 , pp. 37-47
    • Tu, Y.1    Wu, S.2    Shi, X.3    Chen, K.4    Wu, C.5
  • 45
    • 33747877557 scopus 로고    scopus 로고
    • The Kindlins: Subcellular localization and expression during murine development
    • DOI 10.1016/j.yexcr.2006.06.030, PII S0014482706002266
    • Ussar, S., Wang, H. V., Linder, S., Fassler, R. and Moser, M. (2006). The Kindlins: subcellular localization and expression during murine development. Exp. Cell Res. 312, 3142-3151. (Pubitemid 44292664)
    • (2006) Experimental Cell Research , vol.312 , Issue.16 , pp. 3142-3151
    • Ussar, S.1    Wang, H.-V.2    Linder, S.3    Fassler, R.4    Moser, M.5
  • 47
    • 33751574283 scopus 로고    scopus 로고
    • Mutational analysis on the function of the SWAP-70 PH domain
    • DOI 10.1007/s11010-006-9236-1
    • Wakamatsu, I., Ihara, S. and Fukui, Y. (2006). Mutational analysis on the function of the SWAP-70 PH domain. Mol. Cell. Biochem. 293, 137-145. (Pubitemid 44843008)
    • (2006) Molecular and Cellular Biochemistry , vol.293 , Issue.1-2 , pp. 137-145
    • Wakamatsu, I.1    Ihara, S.2    Fukui, Y.3
  • 48
    • 48249125437 scopus 로고    scopus 로고
    • Transmembrane and cytoplasmic domains in integrin activation and protein-protein interactions
    • Review
    • Wegener, K. L. and Campbell, I. D. (2008). Transmembrane and cytoplasmic domains in integrin activation and protein-protein interactions (Review). Mol. Mem. Biol. 25, 376-387.
    • (2008) Mol. Mem. Biol. , vol.25 , pp. 376-387
    • Wegener, K.L.1    Campbell, I.D.2
  • 50
    • 34250361947 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of proteinuria in diabetic nephropathy
    • Wolf, G. and Ziyadeh, F. N. (2007). Cellular and molecular mechanisms of proteinuria in diabetic nephropathy. Nephron Physiol. 106, p26-31.
    • (2007) Nephron Physiol. , vol.106 , pp. 26-31
    • Wolf, G.1    Ziyadeh, F.N.2
  • 51
    • 0027422170 scopus 로고
    • The alpha 5 beta 1 integrin fibronectin receptor, but not the alpha 5 cytoplasmic domain, functions in an early and essential step in fibronectin matrix assembly
    • Wu, C., Bauer, J. S., Juliano, R. L. and McDonald, J. A. (1993). The alpha 5 beta 1 integrin fibronectin receptor, but not the alpha 5 cytoplasmic domain, functions in an early and essential step in fibronectin matrix assembly. J. Biol. Chem. 268, 21883-21888.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21883-21888
    • Wu, C.1    Bauer, J.S.2    Juliano, R.L.3    McDonald, J.A.4
  • 52
    • 0028786294 scopus 로고
    • Integrin activation and cytoskeletal interaction are essential for the assembly of a fibronectin matrix
    • Wu, C., Keivens, V. M., O'Toole, T. E., McDonald, J. A. and Ginsberg, M. H. (1995). Integrin activation and cytoskeletal interaction are essential for the assembly of a fibronectin matrix. Cell 83, 715-724.
    • (1995) Cell , vol.83 , pp. 715-724
    • Wu, C.1    Keivens, V.M.2    O'Toole, T.E.3    McDonald, J.A.4    Ginsberg, M.H.5
  • 53
    • 70449566822 scopus 로고    scopus 로고
    • Structure of an integrin alphaIIb beta3 transmembrane-cytoplasmic heterocomplex provides insight into integrin activation
    • Yang, J., Ma, Y. Q., Page, R. C., Misra, S., Plow, E. F. and Qin, J. (2009). Structure of an integrin alphaIIb beta3 transmembrane-cytoplasmic heterocomplex provides insight into integrin activation. Proc. Natl. Acad. Sci. USA 106, 17729-17734.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 17729-17734
    • Yang, J.1    Ma, Y.Q.2    Page, R.C.3    Misra, S.4    Plow, E.F.5    Qin, J.6
  • 54
    • 0029964243 scopus 로고    scopus 로고
    • Phosphoinositide 3-Kinase and p85/Phosphoinositide 3-Kinase in Platelets
    • Zhang, J., Zhang, J., Shattil, S. J., Cunningham, M. C. and Rittenhouse, S. E. (1996). Phosphoinositide 3-Kinase and p85/Phosphoinositide 3-Kinase in Platelets. J. Biol. Chem. 271, 6265-6272.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6265-6272
    • Zhang, J.1    Zhang, J.2    Shattil, S.J.3    Cunningham, M.C.4    Rittenhouse, S.E.5
  • 55
    • 38949151661 scopus 로고    scopus 로고
    • Pathogenesis of the podocytopathy and proteinuria in diabetic glomerulopathy
    • DOI 10.2174/157339908783502370
    • Ziyadeh, F. N. and Wolf, G. (2008). Pathogenesis of the podocytopathy and proteinuria in diabetic glomerulopathy. Curr. Diabetes Rev 4, 39-45. (Pubitemid 351210971)
    • (2008) Current Diabetes Reviews , vol.4 , Issue.1 , pp. 39-45
    • Ziyadeh, F.N.1    Wolf, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.