메뉴 건너뛰기




Volumn 1812, Issue 10, 2011, Pages 1322-1326

Polycystins, focal adhesions and extracellular matrix interactions

Author keywords

Autosomal dominant; Extracellular matrix; Focal adhesion; Mechanosensory; Polycystic kidney disease; Polycystin

Indexed keywords

ALPHA ACTININ; CRK ASSOCIATED SUBSTRATE PROTEIN; LAMININ; PAXILLIN; POLYCYSTIN 1; POLYCYSTIN 2; PROTEIN KINASE P60; TALIN; TENSIN; VINCULIN;

EID: 80052270877     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2011.03.003     Document Type: Review
Times cited : (60)

References (82)
  • 3
    • 0037320210 scopus 로고    scopus 로고
    • Autosomal dominant polycystic kidney disease: molecular genetics and pathophysiology
    • Sutters M., Germino G.G. Autosomal dominant polycystic kidney disease: molecular genetics and pathophysiology. J. Lab. Clin. Med. 2003, 141:91-101.
    • (2003) J. Lab. Clin. Med. , vol.141 , pp. 91-101
    • Sutters, M.1    Germino, G.G.2
  • 8
    • 34248151938 scopus 로고    scopus 로고
    • Role of primary cilia in the pathogenesis of polycystic kidney disease
    • Yoder B.K. Role of primary cilia in the pathogenesis of polycystic kidney disease. J. Am. Soc. Nephrol. 2007, 18:1381-1388.
    • (2007) J. Am. Soc. Nephrol. , vol.18 , pp. 1381-1388
    • Yoder, B.K.1
  • 10
    • 57149094707 scopus 로고    scopus 로고
    • Pkd1 inactivation induced in adulthood produces focal cystic disease
    • Takakura A., Contrino L., Beck A.W., Zhou J. Pkd1 inactivation induced in adulthood produces focal cystic disease. J. Am. Soc. Nephrol. 2008, 19:2351-2363.
    • (2008) J. Am. Soc. Nephrol. , vol.19 , pp. 2351-2363
    • Takakura, A.1    Contrino, L.2    Beck, A.W.3    Zhou, J.4
  • 11
    • 44349116202 scopus 로고    scopus 로고
    • Acute kidney injury and aberrant planar cell polarity induce cyst formation in mice lacking renal cilia
    • Patel V., Li L., Cobo-Stark P., Shao X., Somlo S., Lin F., Igarashi P. Acute kidney injury and aberrant planar cell polarity induce cyst formation in mice lacking renal cilia. Hum. Mol. Genet. 2008, 17:1578-1590.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 1578-1590
    • Patel, V.1    Li, L.2    Cobo-Stark, P.3    Shao, X.4    Somlo, S.5    Lin, F.6    Igarashi, P.7
  • 13
    • 0037884961 scopus 로고    scopus 로고
    • Kidney-specific inactivation of the KIF3A subunit of kinesin-II inhibits renal ciliogenesis and produces polycystic kidney disease
    • Lin F., Hiesberger T., Cordes K., Sinclair A.M., Goldstein L.S., Somlo S., Igarashi P. Kidney-specific inactivation of the KIF3A subunit of kinesin-II inhibits renal ciliogenesis and produces polycystic kidney disease. Proc. Natl. Acad. Sci. U. S. A. 2003, 100:5286-5291.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 5286-5291
    • Lin, F.1    Hiesberger, T.2    Cordes, K.3    Sinclair, A.M.4    Goldstein, L.S.5    Somlo, S.6    Igarashi, P.7
  • 15
    • 0026571382 scopus 로고
    • Abnormal extracellular matrix and excessive growth of human adult polycystic kidney disease epithelia
    • Wilson P.D., Hreniuk D., Gabow P.A. Abnormal extracellular matrix and excessive growth of human adult polycystic kidney disease epithelia. J. Cell. Physiol. 1992, 150:360-369.
    • (1992) J. Cell. Physiol. , vol.150 , pp. 360-369
    • Wilson, P.D.1    Hreniuk, D.2    Gabow, P.A.3
  • 16
    • 0018820721 scopus 로고
    • Ultrastructure and function of cysts from human adult polycystic kidneys
    • Cuppage F.E., Huseman R.A., Chapman A., Grantham J.J. Ultrastructure and function of cysts from human adult polycystic kidneys. Kidney Int. 1980, 17:372-381.
    • (1980) Kidney Int. , vol.17 , pp. 372-381
    • Cuppage, F.E.1    Huseman, R.A.2    Chapman, A.3    Grantham, J.J.4
  • 19
    • 0028293767 scopus 로고
    • Focal overexpression of collagen IV characterizes the initiation of epithelial changes in polycystic kidney disease
    • Schafer K., Bader M., Gretz N., Oberbaumer I., Bachmann S. Focal overexpression of collagen IV characterizes the initiation of epithelial changes in polycystic kidney disease. Exp. Nephrol. 1994, 2:190-195.
    • (1994) Exp. Nephrol. , vol.2 , pp. 190-195
    • Schafer, K.1    Bader, M.2    Gretz, N.3    Oberbaumer, I.4    Bachmann, S.5
  • 21
    • 0032831465 scopus 로고    scopus 로고
    • The PKD1 gene product, "polycystin-1," is a tyrosine-phosphorylated protein that colocalizes with alpha2beta1-integrin in focal clusters in adherent renal epithelia
    • Wilson P.D., Geng L., Li X., Burrow C.R. The PKD1 gene product, "polycystin-1," is a tyrosine-phosphorylated protein that colocalizes with alpha2beta1-integrin in focal clusters in adherent renal epithelia. Lab. Invest. 1999, 79:1311-1323.
    • (1999) Lab. Invest. , vol.79 , pp. 1311-1323
    • Wilson, P.D.1    Geng, L.2    Li, X.3    Burrow, C.R.4
  • 22
    • 0347357836 scopus 로고    scopus 로고
    • Polycystic kidney disease
    • Wilson P.D. Polycystic kidney disease. N. Engl. J. Med. 2004, 350:151-164.
    • (2004) N. Engl. J. Med. , vol.350 , pp. 151-164
    • Wilson, P.D.1
  • 23
    • 0142244215 scopus 로고    scopus 로고
    • Beta4 integrin and laminin 5 are aberrantly expressed in polycystic kidney disease: role in increased cell adhesion and migration
    • Joly D., Morel V., Hummel A., Ruello A., Nusbaum P., Patey N., Noel L.H., Rousselle P., Knebelmann B. Beta4 integrin and laminin 5 are aberrantly expressed in polycystic kidney disease: role in increased cell adhesion and migration. Am. J. Pathol. 2003, 163:1791-1800.
    • (2003) Am. J. Pathol. , vol.163 , pp. 1791-1800
    • Joly, D.1    Morel, V.2    Hummel, A.3    Ruello, A.4    Nusbaum, P.5    Patey, N.6    Noel, L.H.7    Rousselle, P.8    Knebelmann, B.9
  • 25
    • 16644384500 scopus 로고    scopus 로고
    • The gene expression profile of cyst epithelial cells in autosomal dominant polycystic kidney disease patients
    • Lee J.E., Park M.H., Park J.H. The gene expression profile of cyst epithelial cells in autosomal dominant polycystic kidney disease patients. J. Biochem. Mol. Biol. 2004, 37:612-617.
    • (2004) J. Biochem. Mol. Biol. , vol.37 , pp. 612-617
    • Lee, J.E.1    Park, M.H.2    Park, J.H.3
  • 26
    • 33646521976 scopus 로고    scopus 로고
    • Transcriptome analysis of a rat PKD model: Importance of genes involved in extracellular matrix metabolism
    • Riera M., Burtey S., Fontes M. Transcriptome analysis of a rat PKD model: Importance of genes involved in extracellular matrix metabolism. Kidney Int. 2006, 69:1558-1563.
    • (2006) Kidney Int. , vol.69 , pp. 1558-1563
    • Riera, M.1    Burtey, S.2    Fontes, M.3
  • 27
    • 77956465730 scopus 로고    scopus 로고
    • Cyst formation in the PKD2 (1-703) transgenic rat precedes deregulation of proliferation-related pathways
    • Koupepidou P., Felekkis K.N., Kranzlin B., Sticht C., Gretz N., Deltas C. Cyst formation in the PKD2 (1-703) transgenic rat precedes deregulation of proliferation-related pathways. BMC Nephrol. 2010, 11:23.
    • (2010) BMC Nephrol. , vol.11 , pp. 23
    • Koupepidou, P.1    Felekkis, K.N.2    Kranzlin, B.3    Sticht, C.4    Gretz, N.5    Deltas, C.6
  • 28
    • 33745866295 scopus 로고    scopus 로고
    • A hypomorphic mutation in the mouse laminin alpha5 gene causes polycystic kidney disease
    • Shannon M.B., Patton B.L., Harvey S.J., Miner J.H. A hypomorphic mutation in the mouse laminin alpha5 gene causes polycystic kidney disease. J. Am. Soc. Nephrol. 2006, 17:1913-1922.
    • (2006) J. Am. Soc. Nephrol. , vol.17 , pp. 1913-1922
    • Shannon, M.B.1    Patton, B.L.2    Harvey, S.J.3    Miner, J.H.4
  • 29
  • 30
    • 49949084432 scopus 로고    scopus 로고
    • Exploring mechanisms involved in renal tubular sensing of mechanical stretch following ureteric obstruction
    • Quinlan M.R., Docherty N.G., Watson R.W., Fitzpatrick J.M. Exploring mechanisms involved in renal tubular sensing of mechanical stretch following ureteric obstruction. Am. J. Physiol. Renal Physiol. 2008, 295:F1-F11.
    • (2008) Am. J. Physiol. Renal Physiol. , vol.295
    • Quinlan, M.R.1    Docherty, N.G.2    Watson, R.W.3    Fitzpatrick, J.M.4
  • 31
    • 0028869162 scopus 로고
    • Polycystic kidney disease: etiology, pathogenesis, and treatment
    • Martinez J.R., Grantham J.J. Polycystic kidney disease: etiology, pathogenesis, and treatment. Dis. Mon. 1995, 41:693-765.
    • (1995) Dis. Mon. , vol.41 , pp. 693-765
    • Martinez, J.R.1    Grantham, J.J.2
  • 33
    • 0029551130 scopus 로고
    • Intracranial aneurysms in polycystic kidney disease linked to chromosome 4
    • van Dijk M.A., Chang P.C., Peters D.J., Breuning M.H. Intracranial aneurysms in polycystic kidney disease linked to chromosome 4. J. Am. Soc. Nephrol. 1995, 6:1670-1673.
    • (1995) J. Am. Soc. Nephrol. , vol.6 , pp. 1670-1673
    • van Dijk, M.A.1    Chang, P.C.2    Peters, D.J.3    Breuning, M.H.4
  • 36
    • 75549089484 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of thoracic aortic aneurysms
    • El-Hamamsy I., Yacoub M.H. Cellular and molecular mechanisms of thoracic aortic aneurysms. Nat. Rev. Cardiol. 2009, 6:771-786.
    • (2009) Nat. Rev. Cardiol. , vol.6 , pp. 771-786
    • El-Hamamsy, I.1    Yacoub, M.H.2
  • 39
    • 0023924440 scopus 로고
    • Altered mRNA expression of basement membrane components in a murine model of polycystic kidney disease
    • Ebihara I., Killen P.D., Laurie G.W., Huang T., Yamada Y., Martin G.R., Brown K.S. Altered mRNA expression of basement membrane components in a murine model of polycystic kidney disease. Lab. Invest. 1988, 58:262-269.
    • (1988) Lab. Invest. , vol.58 , pp. 262-269
    • Ebihara, I.1    Killen, P.D.2    Laurie, G.W.3    Huang, T.4    Yamada, Y.5    Martin, G.R.6    Brown, K.S.7
  • 41
    • 58149354448 scopus 로고    scopus 로고
    • TRPCs, GPCRs Bayliss effect
    • Voets T., Nilius B. TRPCs, GPCRs Bayliss effect. Embo J. 2009, 28:4-5.
    • (2009) Embo J. , vol.28 , pp. 4-5
    • Voets, T.1    Nilius, B.2
  • 43
    • 33847357357 scopus 로고    scopus 로고
    • Molecular basis of the effects of mechanical stretch on vascular smooth muscle cells
    • Haga J.H., Li Y.S., Chien S. Molecular basis of the effects of mechanical stretch on vascular smooth muscle cells. J. Biomech. 2007, 40:947-960.
    • (2007) J. Biomech. , vol.40 , pp. 947-960
    • Haga, J.H.1    Li, Y.S.2    Chien, S.3
  • 44
    • 0030929882 scopus 로고    scopus 로고
    • Abdominal wall hernia in autosomal dominant polycystic kidney disease
    • Morris-Stiff G., Coles G., Moore R., Jurewicz A., Lord R. Abdominal wall hernia in autosomal dominant polycystic kidney disease. Br. J. Surg. 1997, 84:615-617.
    • (1997) Br. J. Surg. , vol.84 , pp. 615-617
    • Morris-Stiff, G.1    Coles, G.2    Moore, R.3    Jurewicz, A.4    Lord, R.5
  • 46
    • 38449114631 scopus 로고    scopus 로고
    • Increased occurrence of pericardial effusion in patients with autosomal dominant polycystic kidney disease
    • Qian Q., Hartman R.P., King B.F., Torres V.E. Increased occurrence of pericardial effusion in patients with autosomal dominant polycystic kidney disease. Clin. J. Am. Soc. Nephrol. 2007, 2:1223-1227.
    • (2007) Clin. J. Am. Soc. Nephrol. , vol.2 , pp. 1223-1227
    • Qian, Q.1    Hartman, R.P.2    King, B.F.3    Torres, V.E.4
  • 54
    • 33645889655 scopus 로고    scopus 로고
    • Substrate rigidity and force define form through tyrosine phosphatase and kinase pathways
    • Giannone G., Sheetz M.P. Substrate rigidity and force define form through tyrosine phosphatase and kinase pathways. Trends Cell Biol. 2006, 16:213-223.
    • (2006) Trends Cell Biol. , vol.16 , pp. 213-223
    • Giannone, G.1    Sheetz, M.P.2
  • 55
    • 40949165235 scopus 로고    scopus 로고
    • Actin stress fibers transmit and focus force to activate mechanosensitive channels
    • Hayakawa K., Tatsumi H., Sokabe M. Actin stress fibers transmit and focus force to activate mechanosensitive channels. J. Cell Sci. 2008, 121:496-503.
    • (2008) J. Cell Sci. , vol.121 , pp. 496-503
    • Hayakawa, K.1    Tatsumi, H.2    Sokabe, M.3
  • 56
    • 0344085884 scopus 로고    scopus 로고
    • Cystic diseases of the kidney: role of adhesion molecules in normal and abnormal tubulogenesis
    • Wilson P.D., Burrow C.R. Cystic diseases of the kidney: role of adhesion molecules in normal and abnormal tubulogenesis. Exp. Nephrol. 1999, 7:114-124.
    • (1999) Exp. Nephrol. , vol.7 , pp. 114-124
    • Wilson, P.D.1    Burrow, C.R.2
  • 57
    • 0034672628 scopus 로고    scopus 로고
    • Modification of the composition of polycystin-1 multiprotein complexes by calcium and tyrosine phosphorylation
    • Geng L., Burrow C.R., Li H.P., Wilson P.D. Modification of the composition of polycystin-1 multiprotein complexes by calcium and tyrosine phosphorylation. Biochim. Biophys. Acta 2000, 1535:21-35.
    • (2000) Biochim. Biophys. Acta , vol.1535 , pp. 21-35
    • Geng, L.1    Burrow, C.R.2    Li, H.P.3    Wilson, P.D.4
  • 58
    • 33748748479 scopus 로고    scopus 로고
    • The polycystin 1-C-terminal fragment stimulates ERK-dependent spreading of renal epithelial cells
    • Joly D., Ishibe S., Nickel C., Yu Z., Somlo S., Cantley L.G. The polycystin 1-C-terminal fragment stimulates ERK-dependent spreading of renal epithelial cells. J. Biol. Chem. 2006, 281:26329-26339.
    • (2006) J. Biol. Chem. , vol.281 , pp. 26329-26339
    • Joly, D.1    Ishibe, S.2    Nickel, C.3    Yu, Z.4    Somlo, S.5    Cantley, L.G.6
  • 59
    • 0036137793 scopus 로고    scopus 로고
    • Interaction of the leucine-rich repeats of polycystin-1 with extracellular matrix proteins: possible role in cell proliferation
    • Malhas A.N., Abuknesha R.A., Price R.G. Interaction of the leucine-rich repeats of polycystin-1 with extracellular matrix proteins: possible role in cell proliferation. J. Am. Soc. Nephrol. 2002, 13:19-26.
    • (2002) J. Am. Soc. Nephrol. , vol.13 , pp. 19-26
    • Malhas, A.N.1    Abuknesha, R.A.2    Price, R.G.3
  • 61
    • 0035978520 scopus 로고    scopus 로고
    • The polycystin-1C-type lectin domain binds carbohydrate in a calcium-dependent manner, and interacts with extracellular matrix proteins in vitro
    • Weston B.S., Bagneris C., Price R.G., Stirling J.L. The polycystin-1C-type lectin domain binds carbohydrate in a calcium-dependent manner, and interacts with extracellular matrix proteins in vitro. Biochim. Biophys. Acta 2001, 1536:161-176.
    • (2001) Biochim. Biophys. Acta , vol.1536 , pp. 161-176
    • Weston, B.S.1    Bagneris, C.2    Price, R.G.3    Stirling, J.L.4
  • 62
    • 0033555277 scopus 로고    scopus 로고
    • The structure of a PKD domain from polycystin-1: implications for polycystic kidney disease
    • Bycroft M., Bateman A., Clarke J., Hamill S.J., Sandford R., Thomas R.L., Chothia C. The structure of a PKD domain from polycystin-1: implications for polycystic kidney disease. EMBO J. 1999, 18:297-305.
    • (1999) EMBO J. , vol.18 , pp. 297-305
    • Bycroft, M.1    Bateman, A.2    Clarke, J.3    Hamill, S.J.4    Sandford, R.5    Thomas, R.L.6    Chothia, C.7
  • 63
    • 61349193896 scopus 로고    scopus 로고
    • Hydrolysis of insoluble collagen by deseasin MCP-01 from deep-sea Pseudoalteromonas sp. SM9913: collagenolytic characters, collagen-binding ability of C-terminal polycystic kidney disease domain, and implication for its novel role in deep-sea sedimentary particulate organic nitrogen degradation
    • Zhao G.Y., Chen X.L., Zhao H.L., Xie B.B., Zhou B.C., Zhang Y.Z. Hydrolysis of insoluble collagen by deseasin MCP-01 from deep-sea Pseudoalteromonas sp. SM9913: collagenolytic characters, collagen-binding ability of C-terminal polycystic kidney disease domain, and implication for its novel role in deep-sea sedimentary particulate organic nitrogen degradation. J. Biol. Chem. 2008, 283:36100-36107.
    • (2008) J. Biol. Chem. , vol.283 , pp. 36100-36107
    • Zhao, G.Y.1    Chen, X.L.2    Zhao, H.L.3    Xie, B.B.4    Zhou, B.C.5    Zhang, Y.Z.6
  • 64
    • 77951989369 scopus 로고    scopus 로고
    • Mechanistic insight into the function of the C-terminal PKD domain of the collagenolytic serine protease deseasin MCP-01 from deep sea Pseudoalteromonas sp. SM9913: binding of the PKD domain to collagen results in collagen swelling but does not unwind the collagen triple helix
    • Wang Y.K., Zhao G.Y., Li Y., Chen X.L., Xie B.B., Su H.N., Lv Y.H., He H.L., Liu H., Hu J., Zhou B.C., Zhang Y.Z. Mechanistic insight into the function of the C-terminal PKD domain of the collagenolytic serine protease deseasin MCP-01 from deep sea Pseudoalteromonas sp. SM9913: binding of the PKD domain to collagen results in collagen swelling but does not unwind the collagen triple helix. J. Biol. Chem. 2010, 285:14285-14291.
    • (2010) J. Biol. Chem. , vol.285 , pp. 14285-14291
    • Wang, Y.K.1    Zhao, G.Y.2    Li, Y.3    Chen, X.L.4    Xie, B.B.5    Su, H.N.6    Lv, Y.H.7    He, H.L.8    Liu, H.9    Hu, J.10    Zhou, B.C.11    Zhang, Y.Z.12
  • 65
    • 33645780908 scopus 로고    scopus 로고
    • Mechanotransduction involving multimodular proteins: converting force into biochemical signals
    • Vogel V. Mechanotransduction involving multimodular proteins: converting force into biochemical signals. Annu. Rev. Biophys. Biomol. Struct. 2006, 35:459-488.
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 459-488
    • Vogel, V.1
  • 66
    • 0037117522 scopus 로고    scopus 로고
    • Fibronectin extension and unfolding within cell matrix fibrils controlled by cytoskeletal tension
    • Baneyx G., Baugh L., Vogel V. Fibronectin extension and unfolding within cell matrix fibrils controlled by cytoskeletal tension. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:5139-5143.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 5139-5143
    • Baneyx, G.1    Baugh, L.2    Vogel, V.3
  • 68
    • 28844435249 scopus 로고    scopus 로고
    • The nanomechanics of polycystin-1 extracellular region
    • Qian F., Wei W., Germino G., Oberhauser A. The nanomechanics of polycystin-1 extracellular region. J. Biol. Chem. 2005, 280:40723-40730.
    • (2005) J. Biol. Chem. , vol.280 , pp. 40723-40730
    • Qian, F.1    Wei, W.2    Germino, G.3    Oberhauser, A.4
  • 69
    • 19444372522 scopus 로고    scopus 로고
    • The remarkable mechanical strength of polycystin-1 supports a direct role in mechanotransduction
    • Forman J.R., Qamar S., Paci E., Sandford R.N., Clarke J. The remarkable mechanical strength of polycystin-1 supports a direct role in mechanotransduction. J. Mol. Biol. 2005, 349:861-871.
    • (2005) J. Mol. Biol. , vol.349 , pp. 861-871
    • Forman, J.R.1    Qamar, S.2    Paci, E.3    Sandford, R.N.4    Clarke, J.5
  • 70
    • 70450239574 scopus 로고    scopus 로고
    • Naturally occurring mutations alter the stability of polycystin-1 polycystic kidney disease (PKD) domains
    • Ma L., Xu M., Forman J.R., Clarke J., Oberhauser A.F. Naturally occurring mutations alter the stability of polycystin-1 polycystic kidney disease (PKD) domains. J. Biol. Chem. 2009, 284:32942-32949.
    • (2009) J. Biol. Chem. , vol.284 , pp. 32942-32949
    • Ma, L.1    Xu, M.2    Forman, J.R.3    Clarke, J.4    Oberhauser, A.F.5
  • 71
    • 78649677842 scopus 로고    scopus 로고
    • Naturally occurring osmolytes modulate the nanomechanical properties of polycystic kidney disease domains
    • Ma L., Xu M., Oberhauser A.F. Naturally occurring osmolytes modulate the nanomechanical properties of polycystic kidney disease domains. J. Biol. Chem. 2010, 285:38438-38443.
    • (2010) J. Biol. Chem. , vol.285 , pp. 38438-38443
    • Ma, L.1    Xu, M.2    Oberhauser, A.F.3
  • 72
    • 34547580803 scopus 로고    scopus 로고
    • Characterization of cis-autoproteolysis of polycystin-1, the product of human polycystic kidney disease 1 gene
    • Wei W., Hackmann K., Xu H., Germino G., Qian F. Characterization of cis-autoproteolysis of polycystin-1, the product of human polycystic kidney disease 1 gene. J. Biol. Chem. 2007, 282:21729-21737.
    • (2007) J. Biol. Chem. , vol.282 , pp. 21729-21737
    • Wei, W.1    Hackmann, K.2    Xu, H.3    Germino, G.4    Qian, F.5
  • 73
    • 58049220350 scopus 로고    scopus 로고
    • Mechanotransduction in development: a growing role for contractility
    • Wozniak M.A., Chen C.S. Mechanotransduction in development: a growing role for contractility. Nat. Rev. Mol. Cell Biol. 2009, 10:34-43.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 34-43
    • Wozniak, M.A.1    Chen, C.S.2
  • 75
    • 40349101964 scopus 로고    scopus 로고
    • Low substratum rigidity of collagen gel promotes ERK phosphorylation via lipid raft to augment cell migration
    • Wei W.C., Hsu Y.C., Chiu W.T., Wang C.Z., Wu C.M., Wang Y.K., Shen M.R., Tang M.J. Low substratum rigidity of collagen gel promotes ERK phosphorylation via lipid raft to augment cell migration. J. Cell. Biochem. 2008, 103:1111-1124.
    • (2008) J. Cell. Biochem. , vol.103 , pp. 1111-1124
    • Wei, W.C.1    Hsu, Y.C.2    Chiu, W.T.3    Wang, C.Z.4    Wu, C.M.5    Wang, Y.K.6    Shen, M.R.7    Tang, M.J.8
  • 76
    • 33646005836 scopus 로고    scopus 로고
    • Substrate rigidity regulates the formation and maintenance of tissues
    • Guo W.H., Frey M.T., Burnham N.A., Wang Y.L. Substrate rigidity regulates the formation and maintenance of tissues. Biophys. J. 2006, 90:2213-2220.
    • (2006) Biophys. J. , vol.90 , pp. 2213-2220
    • Guo, W.H.1    Frey, M.T.2    Burnham, N.A.3    Wang, Y.L.4
  • 77
    • 0037484207 scopus 로고    scopus 로고
    • Rigidity of collagen fibrils controls collagen gel-induced down-regulation of focal adhesion complex proteins mediated by alpha2beta1 integrin
    • Wang Y.K., Wang Y.H., Wang C.Z., Sung J.M., Chiu W.T., Lin S.H., Chang Y.H., Tang M.J. Rigidity of collagen fibrils controls collagen gel-induced down-regulation of focal adhesion complex proteins mediated by alpha2beta1 integrin. J. Biol. Chem. 2003, 278:21886-21892.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21886-21892
    • Wang, Y.K.1    Wang, Y.H.2    Wang, C.Z.3    Sung, J.M.4    Chiu, W.T.5    Lin, S.H.6    Chang, Y.H.7    Tang, M.J.8
  • 78
    • 0033917881 scopus 로고    scopus 로고
    • Cell movement is guided by the rigidity of the substrate
    • Lo C.M., Wang H.B., Dembo M., Wang Y.L. Cell movement is guided by the rigidity of the substrate. Biophys. J. 2000, 79:144-152.
    • (2000) Biophys. J. , vol.79 , pp. 144-152
    • Lo, C.M.1    Wang, H.B.2    Dembo, M.3    Wang, Y.L.4
  • 79
    • 0242509224 scopus 로고    scopus 로고
    • ROCK-generated contractility regulates breast epithelial cell differentiation in response to the physical properties of a three-dimensional collagen matrix
    • Wozniak M.A., Desai R., Solski P.A., Der C.J., Keely P.J. ROCK-generated contractility regulates breast epithelial cell differentiation in response to the physical properties of a three-dimensional collagen matrix. J. Cell Biol. 2003, 163:583-595.
    • (2003) J. Cell Biol. , vol.163 , pp. 583-595
    • Wozniak, M.A.1    Desai, R.2    Solski, P.A.3    Der, C.J.4    Keely, P.J.5
  • 81
    • 0023899090 scopus 로고
    • Basement membrane gene expression in polycystic kidney disease
    • Haverty T.P., Neilson E.G. Basement membrane gene expression in polycystic kidney disease. Lab. Invest. 1988, 58:245-248.
    • (1988) Lab. Invest. , vol.58 , pp. 245-248
    • Haverty, T.P.1    Neilson, E.G.2
  • 82
    • 21244468364 scopus 로고    scopus 로고
    • A mechanistic approach to inherited polycystic kidney disease
    • Bissler J.J., Dixon B.P. A mechanistic approach to inherited polycystic kidney disease. Pediatr. Nephrol. 2005, 20:558-566.
    • (2005) Pediatr. Nephrol. , vol.20 , pp. 558-566
    • Bissler, J.J.1    Dixon, B.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.