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Volumn 1812, Issue 10, 2011, Pages 1263-1271

Cilium, centrosome and cell cycle regulation in polycystic kidney disease

Author keywords

Cell cycle; Centrosome; Cilium; Cystogenesis; Kidney; Planar cell polarity

Indexed keywords

B RAF KINASE; CALCIUM ION; CYCLIC AMP; CYCLINE; EPIDERMAL GROWTH FACTOR RECEPTOR; EPIDERMAL GROWTH FACTOR RECEPTOR 2; FIBROCYSTIN; JANUS KINASE 2; KI 67 ANTIGEN; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; MAMMALIAN TARGET OF RAPAMYCIN INHIBITOR; MITOGEN ACTIVATED PROTEIN KINASE; OCTREOTIDE; PHOSPHATIDYLINOSITOL 3 KINASE; POLYCYSTIN 1; POLYCYSTIN 2; PROTEIN SERINE THREONINE KINASE; RAPAMYCIN; SOMATOSTATIN; STAT6 PROTEIN; TUBERIN; VASCULOTROPIN RECEPTOR; WNT PROTEIN; WNT9B PROTEIN;

EID: 80052270551     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2011.02.008     Document Type: Review
Times cited : (35)

References (150)
  • 4
    • 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
  • 5
    • 0037168674 scopus 로고    scopus 로고
    • Cleavage of polycystin-1 requires the receptor for egg jelly domain and is disrupted by human autosomal-dominant polycystic kidney disease 1-associated mutations
    • Qian F., Boletta A., Bhunia A.K., Xu H., Liu L., Ahrabi A.K., Watnick T.J., Zhou F., Germino G.G. Cleavage of polycystin-1 requires the receptor for egg jelly domain and is disrupted by human autosomal-dominant polycystic kidney disease 1-associated mutations. Proc. Natl Acad. Sci. USA 2002, 99:16981-16986.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 16981-16986
    • Qian, F.1    Boletta, A.2    Bhunia, A.K.3    Xu, H.4    Liu, L.5    Ahrabi, A.K.6    Watnick, T.J.7    Zhou, F.8    Germino, G.G.9
  • 6
    • 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
  • 7
    • 0035079832 scopus 로고    scopus 로고
    • Polycystin: new aspects of structure, function, and regulation
    • Wilson P.D. Polycystin: new aspects of structure, function, and regulation. J. Am. Soc. Nephrol. 2001, 12:834-845.
    • (2001) J. Am. Soc. Nephrol. , vol.12 , pp. 834-845
    • Wilson, P.D.1
  • 9
    • 0037205429 scopus 로고    scopus 로고
    • Polycystin-1 activation of c-Jun N-terminal kinase and AP-1 is mediated by heterotrimeric G proteins
    • Parnell S.C., Magenheimer B.S., Maser R.L., Zien C.A., Frischauf A.-M., Calvet J.P. Polycystin-1 activation of c-Jun N-terminal kinase and AP-1 is mediated by heterotrimeric G proteins. J. Biol. Chem. 2002, 277:19566-19572.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19566-19572
    • Parnell, S.C.1    Magenheimer, B.S.2    Maser, R.L.3    Zien, C.A.4    Frischauf, A.-M.5    Calvet, J.P.6
  • 13
    • 6344229834 scopus 로고    scopus 로고
    • Global cytoskeletal control of mechanotransduction in kidney epithelial cells
    • Alenghat F.J., Nauli S.M., Kolb R., Zhou J., Ingber D.E. Global cytoskeletal control of mechanotransduction in kidney epithelial cells. Exp. Cell Res. 2004, 301:23-30.
    • (2004) Exp. Cell Res. , vol.301 , pp. 23-30
    • Alenghat, F.J.1    Nauli, S.M.2    Kolb, R.3    Zhou, J.4    Ingber, D.E.5
  • 14
    • 34547535644 scopus 로고    scopus 로고
    • TRPP2 and autosomal dominant polycystic kidney disease
    • Köttgen M. TRPP2 and autosomal dominant polycystic kidney disease. Biochim. Biophys. Acta 2007, 1772:836-850.
    • (2007) Biochim. Biophys. Acta , vol.1772 , pp. 836-850
    • Köttgen, M.1
  • 15
  • 17
    • 0037378484 scopus 로고    scopus 로고
    • Native polycystin 2 functions as a plasma membrane Ca2+-permeable cation channel in renal epithelia
    • Luo Y., Vassilev P.M., Li X., Kawanabe Y., Zhou J. Native polycystin 2 functions as a plasma membrane Ca2+-permeable cation channel in renal epithelia. Mol. Cell. Biol. 2003, 23:2600-2607.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 2600-2607
    • Luo, Y.1    Vassilev, P.M.2    Li, X.3    Kawanabe, Y.4    Zhou, J.5
  • 18
    • 33645950434 scopus 로고    scopus 로고
    • Lack of a laterality phenotype in Pkd1 knock-out embryos correlates with absence of polycystin-1 in nodal cilia
    • Karcher C., Fischer A., Schweickert A., Bitzer E., Horie S., Witzgall R., Blum M. Lack of a laterality phenotype in Pkd1 knock-out embryos correlates with absence of polycystin-1 in nodal cilia. Differentiation 2005, 73:425-432.
    • (2005) Differentiation , vol.73 , pp. 425-432
    • Karcher, C.1    Fischer, A.2    Schweickert, A.3    Bitzer, E.4    Horie, S.5    Witzgall, R.6    Blum, M.7
  • 20
    • 67650657515 scopus 로고    scopus 로고
    • Function and regulation of TRPP2 at the plasma membrane
    • Tsiokas L. Function and regulation of TRPP2 at the plasma membrane. Am. J. Physiol. Ren. Physiol. 2009, 297:F1-F9.
    • (2009) Am. J. Physiol. Ren. Physiol. , vol.297
    • Tsiokas, L.1
  • 21
    • 51749087052 scopus 로고    scopus 로고
    • Submembraneous microtubule cytoskeleton: interaction of TRPP2 with the cell cytoskeleton
    • Chen X.-Z., Li Q., Wu Y., Liang G., Lara C.J., Cantiello H.F. Submembraneous microtubule cytoskeleton: interaction of TRPP2 with the cell cytoskeleton. FEBS J. 2008, 275:4675-4683.
    • (2008) FEBS J. , vol.275 , pp. 4675-4683
    • Chen, X.-Z.1    Li, Q.2    Wu, Y.3    Liang, G.4    Lara, C.J.5    Cantiello, H.F.6
  • 22
    • 0032744937 scopus 로고    scopus 로고
    • Polycystin-1, the PKD1 gene product, is in a complex containing E-cadherin and the catenins
    • Huan Y., van Adelsberg J. Polycystin-1, the PKD1 gene product, is in a complex containing E-cadherin and the catenins. J. Clin. Invest. 1999, 104:1459-1468.
    • (1999) J. Clin. Invest. , vol.104 , pp. 1459-1468
    • Huan, Y.1    van Adelsberg, J.2
  • 23
    • 0034672628 scopus 로고    scopus 로고
    • Modification of the composition of polycystin-1 multiprotein complexes by calcium and tyrosine phosphorylation
    • Geng L., Burrow C., Li H., Wilson P. 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.2    Li, H.3    Wilson, P.4
  • 24
    • 34948834648 scopus 로고    scopus 로고
    • Polycystin-1 induces cell migration by regulating phosphatidylinositol 3-kinase-dependent cytoskeletal rearrangements and GSK3beta-dependent cell-cell mechanical adhesion
    • Boca M., D'Amato L., Distefano G., Polishchuk R., Germino G., Boletta A. Polycystin-1 induces cell migration by regulating phosphatidylinositol 3-kinase-dependent cytoskeletal rearrangements and GSK3beta-dependent cell-cell mechanical adhesion. Mol. Biol. Cell 2007, 18:4050-4061.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4050-4061
    • Boca, M.1    D'Amato, L.2    Distefano, G.3    Polishchuk, R.4    Germino, G.5    Boletta, A.6
  • 28
    • 67649841563 scopus 로고    scopus 로고
    • Autosomal dominant polycystic kidney disease: the last 3 years
    • Torres V.E., Harris P.C. Autosomal dominant polycystic kidney disease: the last 3 years. Kidney Int. 2009, 76:149-168.
    • (2009) Kidney Int. , vol.76 , pp. 149-168
    • Torres, V.E.1    Harris, P.C.2
  • 29
    • 67449103268 scopus 로고    scopus 로고
    • 2008 Homer W. Smith Award insights into pathogenesis polycystic kidney disease gene discovery
    • Harris P.C. 2008 Homer W. Smith Award insights into pathogenesis polycystic kidney disease gene discovery. J Am Soc Nephrol 2009, 20:1188-1198.
    • (2009) J Am Soc Nephrol , vol.20 , pp. 1188-1198
    • Harris, P.C.1
  • 30
    • 67649844614 scopus 로고    scopus 로고
    • Polycystins and primary cilia: primers for cell cycle progression
    • Zhou J. Polycystins and primary cilia: primers for cell cycle progression. Annu. Rev. Physiol. 2009, 71:83-113.
    • (2009) Annu. Rev. Physiol. , vol.71 , pp. 83-113
    • Zhou, J.1
  • 31
    • 78349286779 scopus 로고    scopus 로고
    • The cell biology of polycystic kidney disease
    • Chapin H.C., Caplan M.J. The cell biology of polycystic kidney disease. J. Cell Biol. 2010, 191:701-710.
    • (2010) J. Cell Biol. , vol.191 , pp. 701-710
    • Chapin, H.C.1    Caplan, M.J.2
  • 33
    • 33646710257 scopus 로고    scopus 로고
    • Volume progression in autosomal dominant polycystic kidney disease: the major factor determining clinical outcomes
    • Grantham J.J., Chapman A.B., Torres V.E. Volume progression in autosomal dominant polycystic kidney disease: the major factor determining clinical outcomes. Clin. journal Am. Soc. Nephrol. CJASN 2006, 1:148-157.
    • (2006) Clin. journal Am. Soc. Nephrol. CJASN , vol.1 , pp. 148-157
    • Grantham, J.J.1    Chapman, A.B.2    Torres, V.E.3
  • 35
    • 33748085676 scopus 로고    scopus 로고
    • Haploinsufficiency of Pkd2 is associated with increased tubular cell proliferation and interstitial fibrosis in two murine Pkd2 models
    • Chang M.Y., Parker E., Ibrahim S., Shortland J.R., Nahas M.E., Haylor J.L., Ong A.C.M. Haploinsufficiency of Pkd2 is associated with increased tubular cell proliferation and interstitial fibrosis in two murine Pkd2 models. Nephrol. Dial. Transplant. 2006, 21:2078-2084.
    • (2006) Nephrol. Dial. Transplant. , vol.21 , pp. 2078-2084
    • Chang, M.Y.1    Parker, E.2    Ibrahim, S.3    Shortland, J.R.4    Nahas, M.E.5    Haylor, J.L.6    Ong, A.C.M.7
  • 38
    • 73349107436 scopus 로고    scopus 로고
    • Cyclic nucleotide signaling in polycystic kidney disease
    • Wang X., Ward C.J., Harris P.C., Torres V.E. Cyclic nucleotide signaling in polycystic kidney disease. Kidney Int. 2010, 77:129-140.
    • (2010) Kidney Int. , vol.77 , pp. 129-140
    • Wang, X.1    Ward, C.J.2    Harris, P.C.3    Torres, V.E.4
  • 39
  • 40
    • 0034123281 scopus 로고    scopus 로고
    • CAMP regulates cell proliferation and cyst formation in autosomal polycystic kidney disease cells
    • Hanaoka K., Guggino W.B. cAMP regulates cell proliferation and cyst formation in autosomal polycystic kidney disease cells. J. Am. Soc. Nephrol. 2000, 11:1179-1187.
    • (2000) J. Am. Soc. Nephrol. , vol.11 , pp. 1179-1187
    • Hanaoka, K.1    Guggino, W.B.2
  • 44
    • 60549101698 scopus 로고    scopus 로고
    • CAMP-dependent chloride secretion mediates tubule enlargement and cyst formation by cultured mammalian collecting duct cells
    • Montesano R., Ghzili H., Carrozzino F., Rossier B.C., Féraille E. cAMP-dependent chloride secretion mediates tubule enlargement and cyst formation by cultured mammalian collecting duct cells. Am. J. Physiol. Ren. Physiol. 2009, 296:F446-F457.
    • (2009) Am. J. Physiol. Ren. Physiol. , vol.296
    • Montesano, R.1    Ghzili, H.2    Carrozzino, F.3    Rossier, B.C.4    Féraille, E.5
  • 46
    • 0029082997 scopus 로고
    • Abnormal polarization of EGF receptors and autocrine stimulation of cyst epithelial growth in human ADPKD
    • Du J., Wilson P.D. Abnormal polarization of EGF receptors and autocrine stimulation of cyst epithelial growth in human ADPKD. Am. J. Physiol. 1995, 269:C487-C495.
    • (1995) Am. J. Physiol. , vol.269
    • Du, J.1    Wilson, P.D.2
  • 47
    • 0028909692 scopus 로고
    • Epidermal growth factor receptor expression is abnormal in murine polycystic kidney
    • Orellana S.A., Sweeney W.E., Neff C.D., Avner E.D. Epidermal growth factor receptor expression is abnormal in murine polycystic kidney. Kidney Int. 1995, 47:490-499.
    • (1995) Kidney Int. , vol.47 , pp. 490-499
    • Orellana, S.A.1    Sweeney, W.E.2    Neff, C.D.3    Avner, E.D.4
  • 48
    • 33746845683 scopus 로고    scopus 로고
    • Inhibition of HER-2(neu/ErbB2) restores normal function and structure to polycystic kidney disease (PKD) epithelia
    • Wilson S., Amsler K., Hyink D., Li X., Lu W., Zhou J., Burrow C., Wilson P. Inhibition of HER-2(neu/ErbB2) restores normal function and structure to polycystic kidney disease (PKD) epithelia. Biochim. Biophys. Acta 2006, 1762:647-655.
    • (2006) Biochim. Biophys. Acta , vol.1762 , pp. 647-655
    • Wilson, S.1    Amsler, K.2    Hyink, D.3    Li, X.4    Lu, W.5    Zhou, J.6    Burrow, C.7    Wilson, P.8
  • 49
    • 0032807280 scopus 로고    scopus 로고
    • In vitro modulation of cyst formation by a novel tyrosine kinase inhibitor
    • Sweeney W.E., Futey L., Frost P., Avner E.D. In vitro modulation of cyst formation by a novel tyrosine kinase inhibitor. Kidney Int. 1999, 56:406-413.
    • (1999) Kidney Int. , vol.56 , pp. 406-413
    • Sweeney, W.E.1    Futey, L.2    Frost, P.3    Avner, E.D.4
  • 50
    • 0141451943 scopus 로고    scopus 로고
    • Combination treatment of PKD utilizing dual inhibition of EGF-receptor activity and ligand bioavailability
    • Sweeney W., Hamahira K., Sweeney J., Garcia-Gatrell M., Frost P., Avner E. Combination treatment of PKD utilizing dual inhibition of EGF-receptor activity and ligand bioavailability. Kidney Int. 2003, 64:1310-1319.
    • (2003) Kidney Int. , vol.64 , pp. 1310-1319
    • Sweeney, W.1    Hamahira, K.2    Sweeney, J.3    Garcia-Gatrell, M.4    Frost, P.5    Avner, E.6
  • 51
    • 0033995015 scopus 로고    scopus 로고
    • Treatment of polycystic kidney disease with a novel tyrosine kinase inhibitor
    • Sweeney W.E., Chen Y., Nakanishi K., Frost P., Avner E.D. Treatment of polycystic kidney disease with a novel tyrosine kinase inhibitor. Kidney Int. 2000, 57:33-40.
    • (2000) Kidney Int. , vol.57 , pp. 33-40
    • Sweeney, W.E.1    Chen, Y.2    Nakanishi, K.3    Frost, P.4    Avner, E.D.5
  • 52
    • 0142249413 scopus 로고    scopus 로고
    • EGF receptor tyrosine kinase inhibition attenuates the development of PKD in Han:SPRD rats
    • Torres V., Sweeney W., Wang X., Qian Q., Harris P., Frost P., Avner E. EGF receptor tyrosine kinase inhibition attenuates the development of PKD in Han:SPRD rats. Kidney Int. 2003, 64:1573-1579.
    • (2003) Kidney Int. , vol.64 , pp. 1573-1579
    • Torres, V.1    Sweeney, W.2    Wang, X.3    Qian, Q.4    Harris, P.5    Frost, P.6    Avner, E.7
  • 53
    • 16244414716 scopus 로고    scopus 로고
    • Epidermal growth factor receptor tyrosine kinase inhibition is not protective in PCK rats
    • Torres V., Sweeney W., Wang X., Qian Q., Harris P., Frost P., Avner E. Epidermal growth factor receptor tyrosine kinase inhibition is not protective in PCK rats. Kidney Int. 2004, 66:1766-1773.
    • (2004) Kidney Int. , vol.66 , pp. 1766-1773
    • Torres, V.1    Sweeney, W.2    Wang, X.3    Qian, Q.4    Harris, P.5    Frost, P.6    Avner, E.7
  • 55
    • 77954510897 scopus 로고    scopus 로고
    • Emerging evidence of a link between the polycystins and the mTOR pathways
    • Boletta A. Emerging evidence of a link between the polycystins and the mTOR pathways. PathoGenetics 2009, 2:6.
    • (2009) PathoGenetics , vol.2 , pp. 6
    • Boletta, A.1
  • 56
    • 44449161481 scopus 로고    scopus 로고
    • The TSC1-TSC2 complex: a molecular switchboard controlling cell growth
    • Huang J., Manning B.D. The TSC1-TSC2 complex: a molecular switchboard controlling cell growth. Biochem. J. 2008, 412:179-190.
    • (2008) Biochem. J. , vol.412 , pp. 179-190
    • Huang, J.1    Manning, B.D.2
  • 57
    • 77952007543 scopus 로고    scopus 로고
    • Mammalian target of rapamycin (mTOR): conducting the cellular signaling symphony
    • Foster K.G., Fingar D.C. Mammalian target of rapamycin (mTOR): conducting the cellular signaling symphony. J. Biol. Chem. 2010, 285:14071-14077.
    • (2010) J. Biol. Chem. , vol.285 , pp. 14071-14077
    • Foster, K.G.1    Fingar, D.C.2
  • 58
    • 4043050174 scopus 로고    scopus 로고
    • G1 cell cycle progression and the expression of G1 cyclins are regulated by PI3K/AKT/mTOR/p70S6K1 signaling in human ovarian cancer cells
    • Gao N., Flynn D.C., Zhang Z., Zhong X.-S., Walker V., Liu K.J., Shi X., Jiang B.-H. G1 cell cycle progression and the expression of G1 cyclins are regulated by PI3K/AKT/mTOR/p70S6K1 signaling in human ovarian cancer cells. Am. J. Physiol. Cell Physiol. 2004, 287:C281-C291.
    • (2004) Am. J. Physiol. Cell Physiol. , vol.287
    • Gao, N.1    Flynn, D.C.2    Zhang, Z.3    Zhong, X.-S.4    Walker, V.5    Liu, K.J.6    Shi, X.7    Jiang, B.-H.8
  • 59
    • 65449176538 scopus 로고    scopus 로고
    • Polycystin-1 regulates ERKs-dependent phosphorylation of Tuberin to control cell size through mTOR and its downstream effectors S6K and 4EBP1
    • Distefano G., Boca M., Rowe I., Claas W., Ma L., Piontek K., Germino G., Pandolfi P., Boletta A. Polycystin-1 regulates ERKs-dependent phosphorylation of Tuberin to control cell size through mTOR and its downstream effectors S6K and 4EBP1. Mol. Cell. Biol. 2009.
    • (2009) Mol. Cell. Biol.
    • Distefano, G.1    Boca, M.2    Rowe, I.3    Claas, W.4    Ma, L.5    Piontek, K.6    Germino, G.7    Pandolfi, P.8    Boletta, A.9
  • 60
    • 77949528561 scopus 로고    scopus 로고
    • Carboxy terminal tail of polycystin-1 regulates localization of TSC2 to repress mTOR
    • Dere R., Wilson P.D., Sandford R.N., Walker C.L. Carboxy terminal tail of polycystin-1 regulates localization of TSC2 to repress mTOR. PLoS ONE 2010, 5:e9239.
    • (2010) PLoS ONE , vol.5
    • Dere, R.1    Wilson, P.D.2    Sandford, R.N.3    Walker, C.L.4
  • 61
    • 0035019467 scopus 로고    scopus 로고
    • Tuberin-dependent membrane localization of polycystin-1: a functional link between polycystic kidney disease and the TSC2 tumor suppressor gene
    • Kleymenova E., Ibraghimov-Beskrovnaya O., Kugoh H., Everitt J., Xu H., Kiguchi K., Landes G., Harris P., Walker C. Tuberin-dependent membrane localization of polycystin-1: a functional link between polycystic kidney disease and the TSC2 tumor suppressor gene. Mol. Cell 2001, 7:823-832.
    • (2001) Mol. Cell , vol.7 , pp. 823-832
    • Kleymenova, E.1    Ibraghimov-Beskrovnaya, O.2    Kugoh, H.3    Everitt, J.4    Xu, H.5    Kiguchi, K.6    Landes, G.7    Harris, P.8    Walker, C.9
  • 62
    • 50049122515 scopus 로고    scopus 로고
    • Better understanding of ADPKD results in potential new treatment options: ready for the cure?
    • Meijer E., de Jong P., Peters D., Gansevoort R. Better understanding of ADPKD results in potential new treatment options: ready for the cure?. J. Nephrol. 2008, 21:133-138.
    • (2008) J. Nephrol. , vol.21 , pp. 133-138
    • Meijer, E.1    de Jong, P.2    Peters, D.3    Gansevoort, R.4
  • 64
    • 33845989853 scopus 로고    scopus 로고
    • Polycystic kidney disease: genes, proteins, animal models, disease mechanisms and therapeutic opportunities
    • Torres V.E., Harris P.C. Polycystic kidney disease: genes, proteins, animal models, disease mechanisms and therapeutic opportunities. J. Intern. Med. 2007, 261:17-31.
    • (2007) J. Intern. Med. , vol.261 , pp. 17-31
    • Torres, V.E.1    Harris, P.C.2
  • 65
    • 34248184040 scopus 로고    scopus 로고
    • Autosomal dominant polycystic kidney disease: time for a change?
    • Chapman A.B. Autosomal dominant polycystic kidney disease: time for a change?. J. Am. Soc. Nephrol. 2007, 18:1399-1407.
    • (2007) J. Am. Soc. Nephrol. , vol.18 , pp. 1399-1407
    • Chapman, A.B.1
  • 69
    • 77249163235 scopus 로고    scopus 로고
    • Treatment strategies and clinical trial design in ADPKD
    • Torres V.E. Treatment strategies and clinical trial design in ADPKD. Adv. Chron. Kidney Dis. 2010, 17:190-204.
    • (2010) Adv. Chron. Kidney Dis. , vol.17 , pp. 190-204
    • Torres, V.E.1
  • 73
    • 77956048123 scopus 로고    scopus 로고
    • MTOR inhibitors in polycystic kidney disease
    • Watnick T., Germino G.G. mTOR inhibitors in polycystic kidney disease. N. Engl. J. Med. 2010, 363:879-881.
    • (2010) N. Engl. J. Med. , vol.363 , pp. 879-881
    • Watnick, T.1    Germino, G.G.2
  • 74
    • 79955007824 scopus 로고    scopus 로고
    • Polycystic kidney disease: do mTOR inhibitors still have a future in ADPKD?
    • Perico N., Remuzzi G. Polycystic kidney disease: do mTOR inhibitors still have a future in ADPKD?. Nat. Rev. Nephrol. 2010, 6:696-698.
    • (2010) Nat. Rev. Nephrol. , vol.6 , pp. 696-698
    • Perico, N.1    Remuzzi, G.2
  • 76
    • 0034735526 scopus 로고    scopus 로고
    • Chlamydomonas IFT88 and its mouse homologue, polycystic kidney disease gene tg737, are required for assembly of cilia and flagella
    • Pazour G.J., Dickert B.L., Vucica Y., Seeley E.S., Rosenbaum J.L., Witman G.B., Cole D.G. Chlamydomonas IFT88 and its mouse homologue, polycystic kidney disease gene tg737, are required for assembly of cilia and flagella. J. Cell Biol. 2000, 151:709-718.
    • (2000) J. Cell Biol. , vol.151 , pp. 709-718
    • Pazour, G.J.1    Dickert, B.L.2    Vucica, Y.3    Seeley, E.S.4    Rosenbaum, J.L.5    Witman, G.B.6    Cole, D.G.7
  • 78
    • 0036785149 scopus 로고    scopus 로고
    • The polycystic kidney disease proteins, polycystin-1, polycystin-2, polaris, and cystin, are co-localized in renal cilia
    • Yoder B.K., Hou X., Guay-Woodford L.M. The polycystic kidney disease proteins, polycystin-1, polycystin-2, polaris, and cystin, are co-localized in renal cilia. J. Am. Soc. Nephrol. 2002, 13:2508-2516.
    • (2002) J. Am. Soc. Nephrol. , vol.13 , pp. 2508-2516
    • Yoder, B.K.1    Hou, X.2    Guay-Woodford, L.M.3
  • 80
    • 68649098302 scopus 로고    scopus 로고
    • The primary cilium as a cellular signaling center: lessons from disease
    • Lancaster M.A., Gleeson J.G. The primary cilium as a cellular signaling center: lessons from disease. Curr. Opin. Genet. Dev. 2009, 19:220-229.
    • (2009) Curr. Opin. Genet. Dev. , vol.19 , pp. 220-229
    • Lancaster, M.A.1    Gleeson, J.G.2
  • 81
  • 82
    • 77950473097 scopus 로고    scopus 로고
    • Cystic diseases of the kidney: molecular biology and genetics
    • Deltas C., Papagregoriou G. Cystic diseases of the kidney: molecular biology and genetics. Arch. Pathol. Lab. Med. 2010, 134:569-582.
    • (2010) Arch. Pathol. Lab. Med. , vol.134 , pp. 569-582
    • Deltas, C.1    Papagregoriou, G.2
  • 83
    • 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
  • 84
    • 33746891890 scopus 로고    scopus 로고
    • The primary cilium as the cell's antenna: signaling at a sensory organelle
    • Singla V., Reiter J.F. The primary cilium as the cell's antenna: signaling at a sensory organelle. Science 2006, 313:629-633.
    • (2006) Science , vol.313 , pp. 629-633
    • Singla, V.1    Reiter, J.F.2
  • 85
    • 0035498717 scopus 로고    scopus 로고
    • Bending the MDCK cell primary cilium increases intracellular calcium
    • Praetorius H.A., Spring K.R. Bending the MDCK cell primary cilium increases intracellular calcium. J. Membr. Biol. 2001, 184:71-79.
    • (2001) J. Membr. Biol. , vol.184 , pp. 71-79
    • Praetorius, H.A.1    Spring, K.R.2
  • 87
    • 34147215806 scopus 로고    scopus 로고
    • Fibrocystin/polyductin, found in the same protein complex with polycystin-2, regulates calcium responses in kidney epithelia
    • Wang S., Zhang J., Nauli S.M., Li X., Starremans P.G., Luo Y., Roberts K.A., Zhou J. Fibrocystin/polyductin, found in the same protein complex with polycystin-2, regulates calcium responses in kidney epithelia. Mol. Cell. Biol. 2007, 27:3241-3252.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 3241-3252
    • Wang, S.1    Zhang, J.2    Nauli, S.M.3    Li, X.4    Starremans, P.G.5    Luo, Y.6    Roberts, K.A.7    Zhou, J.8
  • 88
    • 29744470060 scopus 로고    scopus 로고
    • Polycystin-1, STAT6, and P100 function in a pathway that transduces ciliary mechanosensation and is activated in polycystic kidney disease
    • Low S.H., Vasanth S., Larson C.H., Mukherjee S., Sharma N., Kinter M.T., Kane M.E., Obara T., Weimbs T. Polycystin-1, STAT6, and P100 function in a pathway that transduces ciliary mechanosensation and is activated in polycystic kidney disease. Dev. Cell 2006, 10:57-69.
    • (2006) Dev. Cell , vol.10 , pp. 57-69
    • Low, S.H.1    Vasanth, S.2    Larson, C.H.3    Mukherjee, S.4    Sharma, N.5    Kinter, M.T.6    Kane, M.E.7    Obara, T.8    Weimbs, T.9
  • 90
    • 36249030528 scopus 로고    scopus 로고
    • Kidney-specific inactivation of the Pkd1 gene induces rapid cyst formation in developing kidneys and a slow onset of disease in adult mice
    • Lantinga-van Leeuwen I.S., Leonhard W.N., van der Wal A., Breuning M.H., de Heer E., Peters D.J.M. Kidney-specific inactivation of the Pkd1 gene induces rapid cyst formation in developing kidneys and a slow onset of disease in adult mice. Hum. Mol. Genet. 2007, 16:3188-3196.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 3188-3196
    • Lantinga-van Leeuwen, I.S.1    Leonhard, W.N.2    van der Wal, A.3    Breuning, M.H.4    de Heer, E.5    Peters, D.J.M.6
  • 91
    • 36849037019 scopus 로고    scopus 로고
    • A critical developmental switch defines the kinetics of kidney cyst formation after loss of Pkd1
    • Piontek K., Menezes L.F., Garcia-Gonzalez M.A., Huso D.L., Germino G.G. A critical developmental switch defines the kinetics of kidney cyst formation after loss of Pkd1. Nat. Med. 2007, 13:1490-1495.
    • (2007) Nat. Med. , vol.13 , pp. 1490-1495
    • Piontek, K.1    Menezes, L.F.2    Garcia-Gonzalez, M.A.3    Huso, D.L.4    Germino, G.G.5
  • 92
    • 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
  • 93
    • 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
  • 94
    • 67649884993 scopus 로고    scopus 로고
    • Toxic tubular injury in kidneys from Pkd1-deletion mice accelerates cystogenesis accompanied by dysregulated planar cell polarity and canonical Wnt signaling pathways
    • Happé H., Leonhard W.N., van der Wal A., van de Water B., Lantinga-van Leeuwen I.S., Breuning M.H., de Heer E., Peters D.J.M. Toxic tubular injury in kidneys from Pkd1-deletion mice accelerates cystogenesis accompanied by dysregulated planar cell polarity and canonical Wnt signaling pathways. Hum. Mol. Genet. 2009, 18:2532-2542.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 2532-2542
    • Happé, H.1    Leonhard, W.N.2    van der Wal, A.3    van de Water, B.4    Lantinga-van Leeuwen, I.S.5    Breuning, M.H.6    de Heer, E.7    Peters, D.J.M.8
  • 96
    • 27744538492 scopus 로고    scopus 로고
    • Planar cell polarization: an emerging model points in the right direction
    • Klein T.J., Mlodzik M. Planar cell polarization: an emerging model points in the right direction. Annu. Rev. Cell Dev. Biol. 2005, 21:155-176.
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 155-176
    • Klein, T.J.1    Mlodzik, M.2
  • 103
    • 33644624937 scopus 로고    scopus 로고
    • Ciliogenesis defects in embryos lacking inturned or fuzzy function are associated with failure of planar cell polarity and Hedgehog signaling
    • Park T.J., Haigo S.L., Wallingford J.B. Ciliogenesis defects in embryos lacking inturned or fuzzy function are associated with failure of planar cell polarity and Hedgehog signaling. Nat. Genet. 2006, 38:303-311.
    • (2006) Nat. Genet. , vol.38 , pp. 303-311
    • Park, T.J.1    Haigo, S.L.2    Wallingford, J.B.3
  • 104
    • 77950505396 scopus 로고    scopus 로고
    • Vangl2 directs the posterior tilting and asymmetric localization of motile primary cilia
    • Borovina A., Superina S., Voskas D., Ciruna B. Vangl2 directs the posterior tilting and asymmetric localization of motile primary cilia. Nat. Cell Biol. 2010, 12:407-412.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 407-412
    • Borovina, A.1    Superina, S.2    Voskas, D.3    Ciruna, B.4
  • 105
    • 50049127831 scopus 로고    scopus 로고
    • Flow modulates centriole movements in tubular epithelial cells
    • Kotsis F., Nitschke R., Doerken M., Walz G., Kuehn E.W. Flow modulates centriole movements in tubular epithelial cells. Pflugers Arch 2008, 456:1025-1035.
    • (2008) Pflugers Arch , vol.456 , pp. 1025-1035
    • Kotsis, F.1    Nitschke, R.2    Doerken, M.3    Walz, G.4    Kuehn, E.W.5
  • 109
    • 58149326846 scopus 로고    scopus 로고
    • Intraflagellar transport (IFT) role in ciliary assembly, resorption and signalling
    • Pedersen L.B., Rosenbaum J.L. Intraflagellar transport (IFT) role in ciliary assembly, resorption and signalling. Curr. Top. Dev. Biol. 2008, 85:23-61.
    • (2008) Curr. Top. Dev. Biol. , vol.85 , pp. 23-61
    • Pedersen, L.B.1    Rosenbaum, J.L.2
  • 113
    • 0037134898 scopus 로고    scopus 로고
    • The centrosome cycle
    • Meraldi P., Nigg E. The centrosome cycle. FEBS Lett. 2002, 521:9-13.
    • (2002) FEBS Lett. , vol.521 , pp. 9-13
    • Meraldi, P.1    Nigg, E.2
  • 114
    • 33748327050 scopus 로고    scopus 로고
    • The intraflagellar transport protein IFT20 is associated with the Golgi complex and is required for cilia assembly
    • Follit J.A., Tuft R.A., Fogarty K.E., Pazour G.J. The intraflagellar transport protein IFT20 is associated with the Golgi complex and is required for cilia assembly. Mol. Biol. Cell 2006, 17:3781-3792.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3781-3792
    • Follit, J.A.1    Tuft, R.A.2    Fogarty, K.E.3    Pazour, G.J.4
  • 115
    • 4444320182 scopus 로고    scopus 로고
    • Pericentrin forms a complex with intraflagellar transport proteins and polycystin-2 and is required for primary cilia assembly
    • Jurczyk A., Gromley A., Redick S., San Agustin J., Witman G., Pazour G.J., Peters D.J.M., Doxsey S. Pericentrin forms a complex with intraflagellar transport proteins and polycystin-2 and is required for primary cilia assembly. J. Cell Biol. 2004, 166:637-643.
    • (2004) J. Cell Biol. , vol.166 , pp. 637-643
    • Jurczyk, A.1    Gromley, A.2    Redick, S.3    San Agustin, J.4    Witman, G.5    Pazour, G.J.6    Peters, D.J.M.7    Doxsey, S.8
  • 116
    • 33947322678 scopus 로고    scopus 로고
    • The intraflagellar transport component IFT88/polaris is a centrosomal protein regulating G1-S transition in non-ciliated cells
    • Robert A., Margall-Ducos G., Guidotti J.-E., Brégerie O., Celati C., Bréchot C., Desdouets C. The intraflagellar transport component IFT88/polaris is a centrosomal protein regulating G1-S transition in non-ciliated cells. J. Cell Sci. 2007, 120:628-637.
    • (2007) J. Cell Sci. , vol.120 , pp. 628-637
    • Robert, A.1    Margall-Ducos, G.2    Guidotti, J.-E.3    Brégerie, O.4    Celati, C.5    Bréchot, C.6    Desdouets, C.7
  • 117
    • 33748102496 scopus 로고    scopus 로고
    • Inhibition of centrosome protein assembly leads to p53-dependent exit from the cell cycle
    • Srsen V., Gnadt N., Dammermann A., Merdes A. Inhibition of centrosome protein assembly leads to p53-dependent exit from the cell cycle. J. Cell Biol. 2006, 174:625-630.
    • (2006) J. Cell Biol. , vol.174 , pp. 625-630
    • Srsen, V.1    Gnadt, N.2    Dammermann, A.3    Merdes, A.4
  • 120
    • 0037048323 scopus 로고    scopus 로고
    • Loss of p53 and centrosome hyperamplification
    • Tarapore P., Fukasawa K. Loss of p53 and centrosome hyperamplification. Oncogene 2002, 21:6234-6240.
    • (2002) Oncogene , vol.21 , pp. 6234-6240
    • Tarapore, P.1    Fukasawa, K.2
  • 121
    • 0034972059 scopus 로고    scopus 로고
    • Direct regulation of the centrosome duplication cycle by the p53-p21Waf1/Cip1 pathway
    • Tarapore P., Horn H., Tokuyama Y., Fukasawa K. Direct regulation of the centrosome duplication cycle by the p53-p21Waf1/Cip1 pathway. Oncogene 2001, 20:3173-3184.
    • (2001) Oncogene , vol.20 , pp. 3173-3184
    • Tarapore, P.1    Horn, H.2    Tokuyama, Y.3    Fukasawa, K.4
  • 122
    • 34247887536 scopus 로고    scopus 로고
    • Direct evidence for the role of centrosomally localized p53 in the regulation of centrosome duplication
    • Shinmura K., Bennett R., Tarapore P., Fukasawa K. Direct evidence for the role of centrosomally localized p53 in the regulation of centrosome duplication. Oncogene 2007, 26:2939-2944.
    • (2007) Oncogene , vol.26 , pp. 2939-2944
    • Shinmura, K.1    Bennett, R.2    Tarapore, P.3    Fukasawa, K.4
  • 123
    • 0037133954 scopus 로고    scopus 로고
    • PKD1 induces p21(waf1) and regulation of the cell cycle via direct activation of the JAK-STAT signaling pathway in a process requiring PKD2
    • Bhunia A., Piontek K., Boletta A., Liu L., Qian F., Xu P., Germino F., Germino G. PKD1 induces p21(waf1) and regulation of the cell cycle via direct activation of the JAK-STAT signaling pathway in a process requiring PKD2. Cell 2002, 109:157-168.
    • (2002) Cell , vol.109 , pp. 157-168
    • Bhunia, A.1    Piontek, K.2    Boletta, A.3    Liu, L.4    Qian, F.5    Xu, P.6    Germino, F.7    Germino, G.8
  • 124
    • 28544433252 scopus 로고    scopus 로고
    • Polycystin-1 and polycystin-2 regulate the cell cycle through the helix-loop-helix inhibitor Id2
    • Li X., Luo Y., Starremans P.G., McNamara C.A., Pei Y., Zhou J. Polycystin-1 and polycystin-2 regulate the cell cycle through the helix-loop-helix inhibitor Id2. Nat. Cell Biol. 2005, 7:1202-1212.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 1202-1212
    • Li, X.1    Luo, Y.2    Starremans, P.G.3    McNamara, C.A.4    Pei, Y.5    Zhou, J.6
  • 125
    • 3142735085 scopus 로고    scopus 로고
    • Depletion of PKD1 by an antisense oligodeoxynucleotide induces premature G1/S-phase transition
    • Kim H., Bae Y., Jeong W., Ahn C., Kang S. Depletion of PKD1 by an antisense oligodeoxynucleotide induces premature G1/S-phase transition. Eur. J. Hum. Genet. 2004, 12:433-440.
    • (2004) Eur. J. Hum. Genet. , vol.12 , pp. 433-440
    • Kim, H.1    Bae, Y.2    Jeong, W.3    Ahn, C.4    Kang, S.5
  • 126
  • 127
    • 16844375093 scopus 로고    scopus 로고
    • Pkd1 regulates immortalized proliferation of renal tubular epithelial cells through p53 induction and JNK activation
    • Nishio S., Hatano M., Nagata M., Horie S., Koike T., Tokuhisa T., Mochizuki T. Pkd1 regulates immortalized proliferation of renal tubular epithelial cells through p53 induction and JNK activation. J. Clin. Invest. 2005, 115:910-918.
    • (2005) J. Clin. Invest. , vol.115 , pp. 910-918
    • Nishio, S.1    Hatano, M.2    Nagata, M.3    Horie, S.4    Koike, T.5    Tokuhisa, T.6    Mochizuki, T.7
  • 132
    • 77955351090 scopus 로고    scopus 로고
    • Polycystic kidney disease protein fibrocystin localizes to the mitotic spindle and regulates spindle bipolarity
    • Zhang J., Wu M., Wang S., Shah J., Wilson P.D., Zhou J. Polycystic kidney disease protein fibrocystin localizes to the mitotic spindle and regulates spindle bipolarity. Hum. Mol. Genet. 2010.
    • (2010) Hum. Mol. Genet.
    • Zhang, J.1    Wu, M.2    Wang, S.3    Shah, J.4    Wilson, P.D.5    Zhou, J.6
  • 133
    • 3142707455 scopus 로고    scopus 로고
    • PKD2 interacts and co-localizes with mDia1 to mitotic spindles of dividing cells: role of mDia1 IN PKD2 localization to mitotic spindles
    • Rundle D.R., Gorbsky G., Tsiokas L. PKD2 interacts and co-localizes with mDia1 to mitotic spindles of dividing cells: role of mDia1 IN PKD2 localization to mitotic spindles. J. Biol. Chem. 2004, 279:29728-29739.
    • (2004) J. Biol. Chem. , vol.279 , pp. 29728-29739
    • Rundle, D.R.1    Gorbsky, G.2    Tsiokas, L.3
  • 134
    • 0034907213 scopus 로고    scopus 로고
    • MDia mediates Rho-regulated formation and orientation of stable microtubules
    • Palazzo A.F., Cook T.A., Alberts A.S., Gundersen G.G. mDia mediates Rho-regulated formation and orientation of stable microtubules. Nat. Cell Biol. 2001, 3:723-729.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 723-729
    • Palazzo, A.F.1    Cook, T.A.2    Alberts, A.S.3    Gundersen, G.G.4
  • 136
    • 33750399423 scopus 로고    scopus 로고
    • Polycystin-2 cation channel function is under the control of microtubular structures in primary cilia of renal epithelial cells
    • Li Q., Montalbetti N., Wu Y., Ramos A., Raychowdhury M.K., Chen X.-Z., Cantiello H.F. Polycystin-2 cation channel function is under the control of microtubular structures in primary cilia of renal epithelial cells. J. Biol. Chem. 2006, 281:37566-37575.
    • (2006) J. Biol. Chem. , vol.281 , pp. 37566-37575
    • Li, Q.1    Montalbetti, N.2    Wu, Y.3    Ramos, A.4    Raychowdhury, M.K.5    Chen, X.-Z.6    Cantiello, H.F.7
  • 139
    • 0035527666 scopus 로고    scopus 로고
    • The redistribution of Ca2+ stores with inositol 1,4,5-trisphosphate receptor to the cleavage furrow in a microtubule-dependent manner
    • Mitsuyama F., Sawai T. The redistribution of Ca2+ stores with inositol 1,4,5-trisphosphate receptor to the cleavage furrow in a microtubule-dependent manner. Int. J. Dev. Biol. 2001, 45:861-868.
    • (2001) Int. J. Dev. Biol. , vol.45 , pp. 861-868
    • Mitsuyama, F.1    Sawai, T.2
  • 140
    • 0037127006 scopus 로고    scopus 로고
    • Calcium, calmodulin, and CaMKII requirement for initiation of centrosome duplication in Xenopus egg extracts
    • Matsumoto Y., Maller J.L. Calcium, calmodulin, and CaMKII requirement for initiation of centrosome duplication in Xenopus egg extracts. Science 2002, 295:499-502.
    • (2002) Science , vol.295 , pp. 499-502
    • Matsumoto, Y.1    Maller, J.L.2
  • 145
    • 31144452534 scopus 로고    scopus 로고
    • Hamartin, the tuberous sclerosis complex 1 gene product, interacts with polo-like kinase 1 in a phosphorylation-dependent manner
    • Astrinidis A., Senapedis W., Henske E.P. Hamartin, the tuberous sclerosis complex 1 gene product, interacts with polo-like kinase 1 in a phosphorylation-dependent manner. Hum. Mol. Genet. 2006, 15:287-297.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 287-297
    • Astrinidis, A.1    Senapedis, W.2    Henske, E.P.3
  • 147
    • 56149097603 scopus 로고    scopus 로고
    • Deletion of IFT20 in the mouse kidney causes misorientation of the mitotic spindle and cystic kidney disease
    • Jonassen J.A., San Agustin J., Follit J.A., Pazour G.J. Deletion of IFT20 in the mouse kidney causes misorientation of the mitotic spindle and cystic kidney disease. J. Cell Biol. 2008, 183:377-384.
    • (2008) J. Cell Biol. , vol.183 , pp. 377-384
    • Jonassen, J.A.1    San Agustin, J.2    Follit, J.A.3    Pazour, G.J.4
  • 148
    • 0031035050 scopus 로고    scopus 로고
    • Loss of the polycystic kidney disease (PKD1) region of chromosome 16p13 in renal cyst cells supports a loss-of-function model for cyst pathogenesis
    • Brasier J.L., Henske E.P. Loss of the polycystic kidney disease (PKD1) region of chromosome 16p13 in renal cyst cells supports a loss-of-function model for cyst pathogenesis. J. Clin. Invest. 1997, 99:194-199.
    • (1997) J. Clin. Invest. , vol.99 , pp. 194-199
    • Brasier, J.L.1    Henske, E.P.2
  • 150
    • 58149345565 scopus 로고    scopus 로고
    • Basal bodies platforms for building cilia
    • Marshall W.F. Basal bodies platforms for building cilia. Curr. Top. Dev. Biol. 2008, 85:1-22.
    • (2008) Curr. Top. Dev. Biol. , vol.85 , pp. 1-22
    • Marshall, W.F.1


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