메뉴 건너뛰기




Volumn 112, Issue 4, 2003, Pages 503-516

Erratum: Role for integrin-linked kinase in mediating tubular epithelial to mesenchymal transition and renal interstitial fibrogenesis (Journal of Clinical Investigation (2003) 112 (503-516) doi:10.1172/JCI200317913);Role for integrin-linked kinase in mediating tubular epithelial to mesenchymal transition and renal interstitial fibrogenesis

Author keywords

[No Author keywords available]

Indexed keywords

FIBRONECTIN; GELATINASE A; INTEGRIN LINKED KINASE; MATRIGEL; SMAD PROTEIN; TRANSFORMING GROWTH FACTOR BETA1; UVOMORULIN; ANDROSTANE DERIVATIVE; BIOMATERIAL; COLLAGEN; DNA BINDING PROTEIN; ENZYME INHIBITOR; GELATINASE B; INTEGRIN-LINKED KINASE; LAMININ; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; PROTEIN SERINE THREONINE KINASE; PROTEOGLYCAN; SMAD2 PROTEIN; SMAD2 PROTEIN, HUMAN; SMAD2 PROTEIN, MOUSE; TGFB1 PROTEIN, HUMAN; TGFB1 PROTEIN, MOUSE; TRANSACTIVATOR PROTEIN; TRANSFORMING GROWTH FACTOR BETA; WORTMANNIN;

EID: 0141720342     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI200317913C1     Document Type: Erratum
Times cited : (356)

References (55)
  • 2
    • 0034785496 scopus 로고    scopus 로고
    • Dissection of key events in tubular epithelial to myofibroblast transition and its implications in renal interstitial fibrosis
    • Yang, J., and Liu, Y. 2001. Dissection of key events in tubular epithelial to myofibroblast transition and its implications in renal interstitial fibrosis. Am. J. Pathol. 159:1465-1475.
    • (2001) Am. J. Pathol. , vol.159 , pp. 1465-1475
    • Yang, J.1    Liu, Y.2
  • 3
    • 0036322007 scopus 로고    scopus 로고
    • Evidence that fibroblasts derive from epithelium during tissue fibrosis
    • doi:10.1172/JCI200215518
    • Iwano, M., et al. 2002. Evidence that fibroblasts derive from epithelium during tissue fibrosis. J. Clin. Invest. 110:341-350. doi:10.1172/JCI200215518.
    • (2002) J. Clin. Invest. , vol.110 , pp. 341-350
    • Iwano, M.1
  • 4
    • 0036854980 scopus 로고    scopus 로고
    • Disruption of tissue-type plasminogen activator gene in mice reduces renal interstitial fibrosis in obstructive nephropathy
    • doi:10.1172/JCI200216219
    • Yang, J., et al. 2002. Disruption of tissue-type plasminogen activator gene in mice reduces renal interstitial fibrosis in obstructive nephropathy. J. Clin. Invest. 110:1525-1538. doi:10.1172/JCI200216219.
    • (2002) J. Clin. Invest. , vol.110 , pp. 1525-1538
    • Yang, J.1
  • 5
    • 0034799176 scopus 로고    scopus 로고
    • Renal fibrosis: Collagen composition and assembly regulates epithelial-mesenchymal transdifferentiation
    • Zeisberg, M., et al. 2001. Renal fibrosis: collagen composition and assembly regulates epithelial-mesenchymal transdifferentiation. Am. J. Pathol. 159:1313-1321.
    • (2001) Am. J. Pathol. , vol.159 , pp. 1313-1321
    • Zeisberg, M.1
  • 6
    • 0036138824 scopus 로고    scopus 로고
    • Blockage of tubular epithelial to myofibroblast transition by hepatocyte growth factor prevents renal interstitial fibrosis
    • Yang, J., and Liu, Y. 2002. Blockage of tubular epithelial to myofibroblast transition by hepatocyte growth factor prevents renal interstitial fibrosis. J. Am. Soc. Nephrol. 13:96-107.
    • (2002) J. Am. Soc. Nephrol. , vol.13 , pp. 96-107
    • Yang, J.1    Liu, Y.2
  • 7
    • 0030670132 scopus 로고    scopus 로고
    • Early role of Fspl in epithelial-mesenchymal transformation
    • Okada, H., Danoff, T.M., Kalluri, R., and Neilson, E.G. 1997. Early role of Fspl in epithelial-mesenchymal transformation. Am. J. Physiol. 273:F563-F574.
    • (1997) Am. J. Physiol. , vol.273
    • Okada, H.1    Danoff, T.M.2    Kalluri, R.3    Neilson, E.G.4
  • 8
    • 0032842887 scopus 로고    scopus 로고
    • Transforming growth factor-beta regulates tubular epithelial-myofibroblast transdifferentiation in vitro
    • Fan, J.M., et al. 1999. Transforming growth factor-beta regulates tubular epithelial-myofibroblast transdifferentiation in vitro. Kidney Int. 56:1455-1467.
    • (1999) Kidney Int. , vol.56 , pp. 1455-1467
    • Fan, J.M.1
  • 9
    • 0036233040 scopus 로고    scopus 로고
    • Role of basic fibroblast growth factor-2 in epithelial-mesenchymal transformation
    • Strutz, F., et al. 2002. Role of basic fibroblast growth factor-2 in epithelial-mesenchymal transformation. Kidney Int. 61:1714-1728.
    • (2002) Kidney Int. , vol.61 , pp. 1714-1728
    • Strutz, F.1
  • 10
    • 0036785218 scopus 로고    scopus 로고
    • Hepatocyte growth factor gene therapy and angiotensin II blockade synergistically attenuate renal interstitial fibrosis in mice
    • Yang, J., Dai, C., and Liu, Y. 2002. Hepatocyte growth factor gene therapy and angiotensin II blockade synergistically attenuate renal interstitial fibrosis in mice. J. Am. Soc. Nephrol. 13:2464-2477.
    • (2002) J. Am. Soc. Nephrol. , vol.13 , pp. 2464-2477
    • Yang, J.1    Dai, C.2    Liu, Y.3
  • 11
    • 0030975645 scopus 로고    scopus 로고
    • TGF-beta in kidney fibrosis: A target for gene therapy
    • Border, W.A., and Noble, N.A. 1997. TGF-beta in kidney fibrosis: a target for gene therapy. Kidney Int. 51:1388-1396.
    • (1997) Kidney Int. , vol.51 , pp. 1388-1396
    • Border, W.A.1    Noble, N.A.2
  • 12
    • 0036786834 scopus 로고    scopus 로고
    • TGF-β1 signaling in renal disease
    • Bottinger, E.P., and Bitzer, M. 2002. TGF-β1 signaling in renal disease. J. Am. Soc. Nephrol. 13:2600-2610.
    • (2002) J. Am. Soc. Nephrol. , vol.13 , pp. 2600-2610
    • Bottinger, E.P.1    Bitzer, M.2
  • 14
    • 0033638127 scopus 로고    scopus 로고
    • Molecular basis of renal fibrosis
    • Eddy, A.A. 2000. Molecular basis of renal fibrosis. Pediatr. Nephrol. 15:290-301.
    • (2000) Pediatr. Nephrol. , vol.15 , pp. 290-301
    • Eddy, A.A.1
  • 15
    • 0032540207 scopus 로고    scopus 로고
    • Transforming growth factor-beta receptor types I and II are expressed in renal tubules and are increased after chronic unilateral ureteral obstruction
    • Sutaria, P.M., Ohebshalom, M., McCaffrey, T.A., Vaughan, E.D., Jr., and Felsen, D. 1998. Transforming growth factor-beta receptor types I and II are expressed in renal tubules and are increased after chronic unilateral ureteral obstruction. Life Sci. 62:1965-1972.
    • (1998) Life Sci. , vol.62 , pp. 1965-1972
    • Sutaria, P.M.1    Ohebshalom, M.2    McCaffrey, T.A.3    Vaughan Jr., E.D.4    Felsen, D.5
  • 16
    • 0034903605 scopus 로고    scopus 로고
    • ILK interactions
    • Wu, C. 2001. ILK interactions. J. Cell Sci. 114:2549-2550.
    • (2001) J. Cell Sci. , vol.114 , pp. 2549-2550
    • Wu, C.1
  • 17
    • 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
  • 18
    • 0032787837 scopus 로고    scopus 로고
    • Integrin-linked kinase (ILK): A regulator of integrin and growth-factor signalling
    • Dedhar, S., Williams, B., and Hannigan, G. 1999. Integrin-linked kinase (ILK): a regulator of integrin and growth-factor signalling. Trends Cell Biol. 9:319-323.
    • (1999) Trends Cell Biol. , vol.9 , pp. 319-323
    • Dedhar, S.1    Williams, B.2    Hannigan, G.3
  • 19
    • 0034104592 scopus 로고    scopus 로고
    • Cell-substrate interactions and signaling through ILK
    • Dedhar, S. 2000. Cell-substrate interactions and signaling through ILK. Curr. Opin. Cell Biol. 12:250-256.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 250-256
    • Dedhar, S.1
  • 20
    • 0031962084 scopus 로고    scopus 로고
    • Integrin-linked protein kinase regulates fibronectin matrix assembly. E-cadherin expression, and tumorigenicity
    • Wu, C., et al. 1998. Integrin-linked protein kinase regulates fibronectin matrix assembly, E-cadherin expression, and tumorigenicity. J. Biol. Chem. 273:528-536.
    • (1998) J. Biol. Chem. , vol.273 , pp. 528-536
    • Wu, C.1
  • 21
    • 0035432903 scopus 로고    scopus 로고
    • Integrin-linked kinase as a as a candidate downstream effector in proteinuria
    • Kretzler, M., et al. 2001. Integrin-linked kinase as a as a candidate downstream effector in proteinuria. FASEB J 15:1843-1845.
    • (2001) FASEB J. , vol.15 , pp. 1843-1845
    • Kretzler, M.1
  • 22
    • 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
  • 23
    • 0030611757 scopus 로고    scopus 로고
    • Identification of Smad7, a TGFbeta-inducible antagonist of TGF-beta signalling
    • Nakao, A., et al. 1997. Identification of Smad7, a TGFbeta-inducible antagonist of TGF-beta signalling. Nature. 389:631-635.
    • (1997) Nature , vol.389 , pp. 631-635
    • Nakao, A.1
  • 24
    • 0033789680 scopus 로고    scopus 로고
    • The transcription factor snail is a repressor of E-cadherin gene expression in epithelial tumour cells
    • Batlle, E., et al. 2000. The transcription factor snail is a repressor of E-cadherin gene expression in epithelial tumour cells. Nat. Cell Biol. 2:84-89.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 84-89
    • Batlle, E.1
  • 25
    • 0031105408 scopus 로고    scopus 로고
    • Cell lines with extended in vitro growth potential from human renal proximal tubule: Characterization, response to inducers, and comparison with established cell lines
    • Racusen, L.C., et al. 1997. Cell lines with extended in vitro growth potential from human renal proximal tubule: characterization, response to inducers, and comparison with established cell lines. J. Lab. Clin. Med. 129:318-329.
    • (1997) J. Lab. Clin. Med. , vol.129 , pp. 318-329
    • Racusen, L.C.1
  • 26
    • 0032750817 scopus 로고    scopus 로고
    • Hepatocyte growth factor promotes renal epithelial cell survival by dual mechanisms
    • Liu, Y. 1999. Hepatocyte growth factor promotes renal epithelial cell survival by dual mechanisms. Am. J. Physiol. 277:F624-F633.
    • (1999) Am. J. Physiol. , vol.277
    • Liu, Y.1
  • 27
    • 0037849935 scopus 로고    scopus 로고
    • Transforming growth factor-β1 potentiates renal tubular epithelial cell death by a mechanism independent of Smad signaling
    • Dai, C., Yang, J., and Liu, Y. 2003. Transforming growth factor-β1 potentiates renal tubular epithelial cell death by a mechanism independent of Smad signaling. J. Biol. Chem. 278:12537-12545.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12537-12545
    • Dai, C.1    Yang, J.2    Liu, Y.3
  • 28
    • 0034912450 scopus 로고    scopus 로고
    • PAI-1 deficiency attenuates the fibrogenic response to ureteral obstruction
    • Oda, T., et al. 2001. PAI-1 deficiency attenuates the fibrogenic response to ureteral obstruction. Kidney Int. 60:587-596.
    • (2001) Kidney Int. , vol.60 , pp. 587-596
    • Oda, T.1
  • 30
    • 0028832482 scopus 로고
    • Renoprotective effect of enalapril in uninephrectomized spontaneously hypertensive rats with neonatal streptozotocin-induced diabetes
    • Sato, Y., et al. 1995. Renoprotective effect of enalapril in uninephrectomized spontaneously hypertensive rats with neonatal streptozotocin-induced diabetes. Diabetes Res. Clin. Pract. 29:153-161.
    • (1995) Diabetes Res. Clin. Pract. , vol.29 , pp. 153-161
    • Sato, Y.1
  • 31
    • 0032911053 scopus 로고    scopus 로고
    • Up-regulation of hepatocyte growth factor receptor: An amplification and targeting mechanism for hepatocyte growth factor action in acute renal failure
    • Liu, Y., et al. 1999. Up-regulation of hepatocyte growth factor receptor: an amplification and targeting mechanism for hepatocyte growth factor action in acute renal failure. Kidney Int. 55:442-453.
    • (1999) Kidney Int. , vol.55 , pp. 442-453
    • Liu, Y.1
  • 32
    • 13344270369 scopus 로고
    • The molecular architecture of focal adhesions
    • Jockusch, B.M., et al. 1995. The molecular architecture of focal adhesions. Annu. Rev. Cell Dev. Biol. 11:379-416.
    • (1995) Annu. Rev. Cell Dev. Biol. , vol.11 , pp. 379-416
    • Jockusch, B.M.1
  • 33
    • 0034702253 scopus 로고    scopus 로고
    • Cloning of an isoform of integrin-linked kinase (ILK) that is upregulated in HT-144 melanoma cells following TGF-beta1 stimulation
    • Janji, B., Melchior, C., Vallar, L., and Kieffer, N. 2000. Cloning of an isoform of integrin-linked kinase (ILK) that is upregulated in HT-144 melanoma cells following TGF-beta1 stimulation. Oncogene. 19:3069-3077.
    • (2000) Oncogene , vol.19 , pp. 3069-3077
    • Janji, B.1    Melchior, C.2    Vallar, L.3    Kieffer, N.4
  • 34
    • 0036587571 scopus 로고    scopus 로고
    • Transforming growth factor beta signal transduction
    • Dennler, S., Goumans, M.J., and ten Dijke, P. 2002. Transforming growth factor beta signal transduction. J. Leukoc. Biol. 71:731-740.
    • (2002) J. Leukoc. Biol. , vol.71 , pp. 731-740
    • Dennler, S.1    Goumans, M.J.2    Ten Dijke, P.3
  • 35
    • 0034574298 scopus 로고    scopus 로고
    • How cells read TGF-beta signals
    • Massague, J. 2000. How cells read TGF-beta signals. Nat. Rev. Mol. Cell Biol. 1:169-178.
    • (2000) Nat. Rev. Mol. Cell Biol. , vol.1 , pp. 169-178
    • Massague, J.1
  • 36
    • 0036014928 scopus 로고    scopus 로고
    • Smad7 inhibits fibrotic effect of TGF-beta on renal tubular epithelial cells by blocking smad2 activation
    • Li, J.H., et al. 2002. Smad7 inhibits fibrotic effect of TGF-beta on renal tubular epithelial cells by blocking smad2 activation. J. Am. Soc. Nephrol. 13:1464-1472.
    • (2002) J. Am. Soc. Nephrol. , vol.13 , pp. 1464-1472
    • Li, J.H.1
  • 37
    • 0035185853 scopus 로고    scopus 로고
    • Transforming growth factor-beta1 mediates epithelial to mesenchymal transdifferentiation through a RhoA-dependent mechanism
    • Bhowmick, N.A., et al. 2001. Transforming growth factor-beta1 mediates epithelial to mesenchymal transdifferentiation through a RhoA-dependent mechanism. Mol. Biol. Cell 12:27-36.
    • (2001) Mol. Biol. Cell. , vol.12 , pp. 27-36
    • Bhowmick, N.A.1
  • 38
    • 0036617188 scopus 로고    scopus 로고
    • TGFbeta3-induced activation of RhoA/Rho-kinase pathway is necessary but not sufficient for epithelio-mesenchymal transdifferentiation: Implications for palatogenesis
    • Kaartinen, V., Haataja, L., Nagy, A., Heisterkamp, N., and Groffen, J. 2002. TGFbeta3-induced activation of RhoA/Rho-kinase pathway is necessary but not sufficient for epithelio-mesenchymal transdifferentiation: implications for palatogenesis. Int. J. Mol. Med. 9:563-570.
    • (2002) Int. J. Mol. Med. , vol.9 , pp. 563-570
    • Kaartinen, V.1    Haataja, L.2    Nagy, A.3    Heisterkamp, N.4    Groffen, J.5
  • 39
    • 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
  • 40
    • 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
  • 41
    • 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
  • 42
    • 0035950544 scopus 로고    scopus 로고
    • Mammary epithelial-specific expression of the integrin-linked kinase (ILK) results in the induction of mammary gland hyperplasias and tumors in transgenic mice
    • White, D.E., Cardiff, R.D., Dedhar, S., and Muller, W.J. 2001 Mammary epithelial-specific expression of the integrin-linked kinase (ILK) results in the induction of mammary gland hyperplasias and tumors in transgenic mice. Oncogene. 20:7064-7072.
    • (2001) Oncogene , vol.20 , pp. 7064-7072
    • White, D.E.1    Cardiff, R.D.2    Dedhar, S.3    Muller, W.J.4
  • 43
    • 0032827029 scopus 로고    scopus 로고
    • Embryonic renal epithelia: Induction, nephrogenesis, and cell differentiation
    • Horster, M.F., Braun, G.S., and Huber, S.M. 1999. Embryonic renal epithelia: induction, nephrogenesis, and cell differentiation. Physiol. Rev. 79:1157-1191.
    • (1999) Physiol. Rev. , vol.79 , pp. 1157-1191
    • Horster, M.F.1    Braun, G.S.2    Huber, S.M.3
  • 44
    • 0032819810 scopus 로고    scopus 로고
    • Cadherins and their connections: Adhesion junctions have broader functions
    • Steinberg, M.S., and McNutt, P.M. 1999. Cadherins and their connections: adhesion junctions have broader functions. Curr. Opin. Cell Biol. 11:554-560.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 554-560
    • Steinberg, M.S.1    McNutt, P.M.2
  • 45
    • 0037032804 scopus 로고    scopus 로고
    • Composition and formation of intercellular junctions in epithelial cells
    • Knust E., and Bossinger, O. 2002. Composition and formation of intercellular junctions in epithelial cells. Science. 298:1955-1959.
    • (2002) Science , vol.298 , pp. 1955-1959
    • Knust, E.1    Bossinger, O.2
  • 46
    • 0033784843 scopus 로고    scopus 로고
    • The transcription factor snail controls epithelial-mesenchymal transitions by repressing E-cadherin expression
    • Cano, A., et al. 2000. The transcription factor snail controls epithelial-mesenchymal transitions by repressing E-cadherin expression. Nat. Cell Biol 2:76-83.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 76-83
    • Cano, A.1
  • 47
    • 0035804215 scopus 로고    scopus 로고
    • Inhibition of integrin linked kinase (ILK) suppresses beta-catenin-Lef/Tcf-dependent transcription and expression of the E-cadherin repressor, snail, in APC-/-human colon carcinoma cells
    • Tan, C., et al. 2001. Inhibition of integrin linked kinase (ILK) suppresses beta-catenin-Lef/Tcf-dependent transcription and expression of the E-cadherin repressor, snail, in APC-/- human colon carcinoma cells. Oncogene. 20:133-140.
    • (2001) Oncogene , vol.20 , pp. 133-140
    • Tan, C.1
  • 48
    • 0030943367 scopus 로고    scopus 로고
    • Localization of fibronectin matrix assembly sites on fibroblasts and endothelial cells
    • Christopher, R.A., Kowalczyk, A.P., and McKeown-Longo, P.J. 1997. Localization of fibronectin matrix assembly sites on fibroblasts and endothelial cells. J. Cell Sci. 110:569-581.
    • (1997) J. Cell Sci. , vol.110 , pp. 569-581
    • Christopher, R.A.1    Kowalczyk, A.P.2    McKeown-Longo, P.J.3
  • 49
    • 0034611008 scopus 로고    scopus 로고
    • Integrin dynamics and matrix assembly: Tensin-dependent translocation of alpha(5)beta(1) integrins promotes early fibronectin fibrillogenesis
    • Pankov, R., et al. 2000. Integrin dynamics and matrix assembly: tensin-dependent translocation of alpha(5)beta(1) integrins promotes early fibronectin fibrillogenesis. J. Cell Biol. 148:1075-1090.
    • (2000) J. Cell Biol. , vol.148 , pp. 1075-1090
    • Pankov, R.1
  • 50
    • 0037107551 scopus 로고    scopus 로고
    • Fibronectin at a glance
    • Pankov, R., and Yamada, KM. 2002. Fibronectin at a glance. J. Cell Sci. 115:3861-3863.
    • (2002) J. Cell Sci. , vol.115 , pp. 3861-3863
    • Pankov, R.1    Yamada, K.M.2
  • 51
    • 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
  • 52
    • 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., et al. 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
  • 53
    • 0035844257 scopus 로고    scopus 로고
    • Ca2+-independent smooth muscle contraction. A novel function for integrin-linked kinase
    • Deng, J.T., Van Lierop, J.E., Sutherland, C., and Walsh, M.P. 2001. Ca2+-independent smooth muscle contraction. A novel function for integrin-linked kinase. J. Biol. Chem. 276:16365-16373.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16365-16373
    • Deng, J.T.1    Van Lierop, J.E.2    Sutherland, C.3    Walsh, M.P.4
  • 54
    • 0035661067 scopus 로고    scopus 로고
    • Advanced glycation end products cause epithelial-myofibroblast transdifferentiation via the receptor for advanced glycation end products (RAGE)
    • doi:10.1172/JCI200111951
    • Oldfield, M.D., et al. 2001. Advanced glycation end products cause epithelial-myofibroblast transdifferentiation via the receptor for advanced glycation end products (RAGE). J. Clin. Invest. 108:1853-1863. doi:10.1172/JCI200111951.
    • (2001) J. Clin. Invest. , vol.108 , pp. 1853-1863
    • Oldfield, M.D.1
  • 55
    • 0035990920 scopus 로고    scopus 로고
    • Integrin-linked kinase, a promising cancer therapeutic target: Biochemical and biological properties
    • Yoganathan, N., et al. 2002. Integrin-linked kinase, a promising cancer therapeutic target: biochemical and biological properties. Pharmacol. Ther. 93:233-242.
    • (2002) Pharmacol. Ther. , vol.93 , pp. 233-242
    • Yoganathan, N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.